                         SEQUENCE LISTING

<110>  DiMarchi, Richard
 
<120>  DIPEPTIDE LINKED MEDICINAL AGENTS

<130>  29920-210275

<150>  61/139,227
<151>  2008-12-19

<160>  58    

<170>  PatentIn version 3.3

<210>  1
<211>  29
<212>  PRT
<213>  Homo sapiens

<400>  1

His Ser Gln Gly Thr Phe Thr Ser Asp Tyr Ser Lys Tyr Leu Asp Ser 
1               5                   10                  15      


Arg Arg Ala Gln Asp Phe Val Gln Trp Leu Met Asn Thr 
            20                  25                  


<210>  2
<211>  6
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Glucagon analogue

<400>  2

His Thr Arg Gly Thr Phe 
1               5       


<210>  3
<211>  8
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Glucagon analogue


<220>
<221>  MISC_FEATURE
<222>  (2)..(2)
<223>  Xaa at position 2 is sarcosine

<400>  3

Lys Xaa His Thr Arg Gly Thr Phe 
1               5               


<210>  4
<211>  6
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  glucagon analogue


<220>
<221>  MOD_RES
<222>  (1)..(1)
<223>  d-histidine

<220>
<221>  MOD_RES
<222>  (2)..(2)
<223>  d-threonine

<220>
<221>  MOD_RES
<222>  (3)..(3)
<223>  d-arginine

<220>
<221>  MOD_RES
<222>  (5)..(5)
<223>  d-threonine

<220>
<221>  MOD_RES
<222>  (6)..(6)
<223>  d-phenylalanine

<400>  4

Xaa Xaa Xaa Gly Xaa Xaa 
1               5       


<210>  5
<211>  8
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  glucagon analogue


<220>
<221>  MOD_RES
<222>  (2)..(2)
<223>  Xaa at position 2 is sarcosine

<220>
<221>  MOD_RES
<222>  (3)..(3)
<223>  d-histidine

<220>
<221>  MOD_RES
<222>  (4)..(4)
<223>  d-threonine

<220>
<221>  MOD_RES
<222>  (5)..(5)
<223>  d-arginine

<220>
<221>  MOD_RES
<222>  (7)..(7)
<223>  d-threonine

<220>
<221>  MOD_RES
<222>  (8)..(8)
<223>  d-phenylalanine

<400>  5

Lys Xaa Xaa Xaa Xaa Gly Xaa Xaa 
1               5               


<210>  6
<211>  11
<212>  PRT
<213>  Homo sapiens

<400>  6

Cys Tyr Phe Gln Asn Cys Pro Arg Gly Gly Lys 
1               5                   10      


<210>  7
<211>  28
<212>  PRT
<213>  Homo sapiens

<400>  7

Ser Leu Arg Arg Ser Ser Cys Phe Gly Gly Arg Met Asp Arg Ile Gly 
1               5                   10                  15      


Ala Gln Ser Gly Leu Gly Cys Asn Ser Phe Arg Tyr 
            20                  25              


<210>  8
<211>  44
<212>  PRT
<213>  Homo sapiens

<400>  8

Tyr Ala Asp Ala Ile Phe Thr Asn Ser Tyr Arg Lys Val Leu Gly Gln 
1               5                   10                  15      


Leu Ser Ala Arg Lys Leu Leu Gln Asp Ile Met Ser Arg Gln Gln Gly 
            20                  25                  30          


Glu Ser Asn Gln Glu Arg Gly Ala Arg Ala Arg Leu 
        35                  40                  


<210>  9
<211>  36
<212>  PRT
<213>  Homo sapiens

<400>  9

Tyr Pro Ser Lys Pro Asp Asn Pro Gly Glu Asp Ala Pro Ala Glu Asp 
1               5                   10                  15      


Met Ala Arg Tyr Tyr Ser Ala Leu Arg His Tyr Ile Asn Leu Ile Thr 
            20                  25                  30          


Arg Gln Arg Tyr 
        35      


<210>  10
<211>  9
<212>  PRT
<213>  Homo sapiens

<400>  10

Cys Tyr Ile Gln Asn Cys Pro Leu Gly 
1               5                   


<210>  11
<211>  36
<212>  PRT
<213>  Homo sapiens

<400>  11

Ala Pro Leu Glu Pro Val Tyr Pro Gly Asp Asn Ala Thr Pro Glu Gln 
1               5                   10                  15      


Met Ala Gln Tyr Ala Ala Asp Leu Arg Arg Tyr Ile Asn Met Leu Thr 
            20                  25                  30          


Arg Pro Arg Tyr 
        35      


<210>  12
<211>  28
<212>  PRT
<213>  Homo sapiens

<400>  12

Ser Ala Asn Ser Asn Pro Ala Met Ala Pro Arg Glu Arg Lys Ala Gly 
1               5                   10                  15      


Cys Lys Asn Phe Phe Trp Lys Thr Phe Thr Ser Cys 
            20                  25              


<210>  13
<211>  14
<212>  PRT
<213>  Homo sapiens

<400>  13

Ala Gly Cys Lys Asn Phe Phe Trp Lys Thr Phe Thr Ser Cys 
1               5                   10                  



<210>  14
<211>  32
<212>  PRT
<213>  Homo sapiens


<220>
<221>  DISULFID
<222>  (1)..(7)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (32)..(32)
<223>  C-terminal amidation

<400>  14

Cys Gly Asn Leu Ser Thr Cys Met Leu Gly Thr Tyr Thr Gln Asp Phe 
1               5                   10                  15      


Asn Lys Phe His Thr Phe Pro Gln Thr Ala Ile Gly Val Gly Ala Pro 
            20                  25                  30          


<210>  15
<211>  48
<212>  PRT
<213>  Mus musculus


<220>
<221>  DISULFID
<222>  (10)..(16)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (48)..(48)
<223>  C-terminal amidation

<400>  15

Ser Leu Asp Ser Pro Arg Ser Lys Arg Cys Gly Asn Leu Ser Thr Cys 
1               5                   10                  15      


Met Leu Gly Thr Tyr Thr Gln Asp Leu Asn Glu Phe His Thr Phe Pro 
            20                  25                  30          


Gln Thr Ser Ile Gly Val Glu Ala Pro Gly Lys Lys Arg Asp Val Ala 
        35                  40                  45              


<210>  16
<211>  32
<212>  PRT
<213>  Rattus norvegicus


<220>
<221>  DISULFID
<222>  (1)..(7)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (32)..(32)
<223>  C-terminal amidation

<400>  16

Cys Gly Asn Leu Ser Thr Cys Met Leu Gly Thr Tyr Thr Gln Asp Leu 
1               5                   10                  15      


Asn Lys Phe His Thr Phe Pro Gln Thr Ser Ile Gly Val Gly Ala Pro 
            20                  25                  30          


<210>  17
<211>  32
<212>  PRT
<213>  Sus scrofa


<220>
<221>  MOD_RES
<222>  (32)..(32)
<223>  C-terminal amidation

<400>  17

Cys Ser Asn Leu Ser Thr Cys Val Leu Ser Ala Tyr Trp Arg Asn Leu 
1               5                   10                  15      


Asn Asn Phe His Arg Phe Ser Gly Met Gly Phe Gly Pro Glu Thr Pro 
            20                  25                  30          


<210>  18
<211>  32
<212>  PRT
<213>  Canis lupus


<220>
<221>  DISULFID
<222>  (1)..(7)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (32)..(32)
<223>  C-terminal amidation

<400>  18

Cys Ser Asn Leu Ser Thr Cys Val Leu Gly Thr Tyr Ser Lys Asp Leu 
1               5                   10                  15      


Asn Asn Phe His Thr Phe Ser Gly Ile Gly Phe Gly Ala Glu Thr Pro 
            20                  25                  30          


<210>  19
<211>  32
<212>  PRT
<213>  Bos taurus


<220>
<221>  DISULFID
<222>  (1)..(7)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (32)..(32)
<223>  C-terminal amidation

<400>  19

Cys Ser Asn Leu Ser Thr Cys Val Leu Ser Ala Tyr Trp Lys Asp Leu 
1               5                   10                  15      


Asn Asn Tyr His Arg Phe Ser Gly Met Gly Phe Gly Pro Glu Thr Pro 
            20                  25                  30          


<210>  20
<211>  126
<212>  PRT
<213>  Danio rerio


<220>
<221>  DISULFID
<222>  (82)..(87)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (126)..(126)
<223>  C-terminal amidation

<400>  20

Met Val Met Leu Lys Ile Ser Ala Phe Leu Val Ala Tyr Ala Leu Ile 
1               5                   10                  15      


Ile Cys Gln Met Tyr Ser Ser Asn Ala Ala Pro Ala Arg Pro Ala Leu 
            20                  25                  30          


Glu Ser Ser Pro Asp Arg Thr Thr Leu Ser Asp Tyr Glu Ala Arg Arg 
        35                  40                  45              


Leu Leu Gln Ala Ile Val Lys Glu Phe Met Gln Met Thr Ala Glu Asp 
    50                  55                  60                  


Met Glu Gln Gln Ala Thr Glu Glu Asn Ser Val Thr Thr Gln Lys Arg 
65                  70                  75                  80  


Ala Cys Asn Thr Ala Thr Cys Val Thr His Arg Leu Ala Asp Phe Leu 
                85                  90                  95      


Ser Arg Ser Gly Gly Ile Gly Ser Ser Lys Phe Val Pro Thr Asn Val 
            100                 105                 110         


Gly Ser Gln Ala Phe Gly Arg Arg Arg Arg Leu Ser Gln Glu 
        115                 120                 125     


<210>  21
<211>  127
<212>  PRT
<213>  Oryzias latipes


<220>
<221>  DISULFID
<222>  (82)..(113)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (127)..(127)
<223>  C-terminal amidation

<400>  21

Met Thr Met Leu Lys Leu Trp Thr Leu Leu Leu Ala Asn Ala Leu Leu 
1               5                   10                  15      


Leu Cys Gln Met Tyr Ile Ser Glu Ala Ala Pro Ser Arg Thr Ser Lys 
            20                  25                  30          


Glu Phe Val Thr Asp Gly Val Pro Leu Leu Asn Asn Glu Ala Glu Thr 
        35                  40                  45              


Leu Phe Arg Ala Ile Lys Asp Tyr Ile Glu Met Thr Ser Glu Glu Ala 
    50                  55                  60                  


Ala Lys Glu Glu Ala Glu Glu Glu Ser Leu Asp Arg Pro Leu Ser Lys 
65                  70                  75                  80  


Arg Cys Thr Gly Leu Ser Thr Cys Val Leu Gly Arg Leu Ser Gln Asp 
                85                  90                  95      


Ile His Lys Leu Gln Thr Tyr Pro Arg Thr Asp Val Gly Ala Gly Thr 
            100                 105                 110         


Pro Gly Lys Lys Arg Ser Leu Phe Glu Gln Phe Glu Asn Tyr Ser 
        115                 120                 125         


<210>  22
<211>  32
<212>  PRT
<213>  Gallus gallus


<220>
<221>  DISULFID
<222>  (1)..(7)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (32)..(32)
<223>  C-terminal amidation

<400>  22

Cys Ala Ser Leu Ser Thr Cys Val Leu Gly Lys Leu Ser Gln Glu Leu 
1               5                   10                  15      


His Lys Leu Gln Thr Tyr Pro Arg Thr Asp Val Gly Ala Gly Thr Pro 
            20                  25                  30          


<210>  23
<211>  32
<212>  PRT
<213>  Oncorhynchus gorbuscha


<220>
<221>  DISULFID
<222>  (1)..(7)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (32)..(32)
<223>  C-terminal amidation

<400>  23

Cys Ser Asn Leu Ser Thr Cys Val Leu Gly Lys Leu Ser Gln Glu Leu 
1               5                   10                  15      


His Lys Leu Gln Thr Tyr Pro Arg Thr Asn Thr Gly Ser Gly Thr Pro 
            20                  25                  30          


<210>  24
<211>  32
<212>  PRT
<213>  Ovis aries


<220>
<221>  DISULFID
<222>  (1)..(7)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (32)..(32)
<223>  C-terminal amidation

<400>  24

Cys Ser Asn Leu Ser Thr Cys Val Leu Ser Ala Tyr Trp Lys Asp Leu 
1               5                   10                  15      


Asn Asn Tyr His Arg Tyr Ser Gly Met Gly Phe Gly Pro Glu Thr Pro 
            20                  25                  30          


<210>  25
<211>  136
<212>  PRT
<213>  Takifugu rubripes


<220>
<221>  DISULFID
<222>  (83)..(89)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (136)..(136)
<223>  C-terminal amidation

<400>  25

Met Val Met Leu Lys Ile Ser Ala Phe Leu Leu Ala Tyr Ala Leu Val 
1               5                   10                  15      


Ile Cys Gln Met Tyr Ser Ser His Ala Ala Pro Ala Arg Pro Gly Leu 
            20                  25                  30          


Glu Ser Met Ser Asp Arg Val Thr Leu Thr Asp Tyr Glu Ala Arg Arg 
        35                  40                  45              


Leu Leu Asn Ala Ile Val Lys Glu Phe Val Gln Met Thr Ala Glu Glu 
    50                  55                  60                  


Leu Glu Gln Gln Ala Thr Glu Gly Asn Ser Met Asp Arg Pro Leu Thr 
65                  70                  75                  80  


Lys Arg Cys Ser Asn Leu Ser Thr Cys Val Leu Gly Lys Leu Ser Gln 
                85                  90                  95      


Glu Leu His Lys Leu Gln Thr Phe Pro Arg Thr Asn Val Gly Ala Gly 
            100                 105                 110         


Thr Pro Gly Lys Lys Arg Ser Ala Ala Glu Ser Asp Ser Tyr Ala Ser 
        115                 120                 125             


Tyr Gly Glu Thr Phe Gly Arg Ile 
    130                 135     


<210>  26
<211>  50
<212>  PRT
<213>  Paralichthys olivaceus


<220>
<221>  DISULFID
<222>  (1)..(7)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (50)..(50)
<223>  C-terminal amidation

<400>  26

Cys Thr Gly Leu Ser Thr Cys Val Leu Gly Lys Leu Ser Gln Asp Ile 
1               5                   10                  15      


His Lys Leu Gln Thr Tyr Pro Arg Thr Asn Val Gly Ala Gly Thr Pro 
            20                  25                  30          


Gly Lys Lys Arg Ser Leu Ser Glu Gln Tyr Glu Asn His Gly Ser Ser 
        35                  40                  45              


Tyr Asn 
    50  


<210>  27
<211>  32
<212>  PRT
<213>  Sardinops melanostictus


<220>
<221>  DISULFID
<222>  (1)..(7)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (32)..(32)
<223>  C-terminal amidation

<400>  27

Cys Ser Asn Leu Ser Thr Cys Ala Leu Gly Lys Leu Ser Gln Glu Leu 
1               5                   10                  15      


His Lys Leu Gln Ser Tyr Pro Arg Thr Asn Val Gly Ala Gly Thr Pro 
            20                  25                  30          


<210>  28
<211>  32
<212>  PRT
<213>  Carassius auratus


<220>
<221>  DISULFID
<222>  (1)..(7)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (32)..(32)
<223>  C-terminal amidation

<400>  28

Cys Ser Ser Leu Ser Thr Cys Val Leu Gly Lys Leu Ser Gln Glu Leu 
1               5                   10                  15      


His Lys Leu Gln Thr Tyr Pro Arg Thr Asn Val Gly Ala Gly Thr Pro 
            20                  25                  30          


<210>  29
<211>  32
<212>  PRT
<213>  Salvelinus alpinus


<220>
<221>  DISULFID
<222>  (1)..(7)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (32)..(32)
<223>  C-terminal amidation

<400>  29

Cys Ser Asn Leu Ser Thr Cys Val Leu Gly Lys Leu Ser Gln Glu Leu 
1               5                   10                  15      


His Lys Leu Gln Thr Tyr Pro Arg Thr Asn Thr Gly Ser Gly Thr Pro 
            20                  25                  30          


<210>  30
<211>  32
<212>  PRT
<213>  Anguilliformes


<220>
<221>  DISULFID
<222>  (1)..(7)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (32)..(32)
<223>  C-terminal amidation

<400>  30

Cys Ser Asn Leu Ser Thr Cys Val Leu Gly Lys Leu Ser Gln Glu Leu 
1               5                   10                  15      


His Lys Leu Gln Thr Tyr Pro Arg Thr Asp Val Gly Ala Gly Thr Pro 
            20                  25                  30          


<210>  31
<211>  32
<212>  PRT
<213>  Oncorhynchus keta


<220>
<221>  DISULFID
<222>  (1)..(7)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (32)..(32)
<223>  C-terminal amidation

<400>  31

Cys Ser Asn Leu Ser Thr Cys Val Leu Gly Lys Leu Ser Gln Glu Leu 
1               5                   10                  15      


His Lys Leu Gln Thr Tyr Pro Arg Thr Asn Thr Gly Asn Gly Thr Pro 
            20                  25                  30          


<210>  32
<211>  32
<212>  PRT
<213>  Oncorhynchus kisutch


<220>
<221>  DISULFID
<222>  (1)..(7)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (32)..(32)
<223>  C-terminal amidation

<400>  32

Cys Ser Asn Leu Ser Thr Cys Val Leu Gly Lys Leu Ser Gln Glu Leu 
1               5                   10                  15      


His Lys Leu Gln Thr Tyr Pro Arg Thr Asn Thr Gly Ser Gly Thr Pro 
            20                  25                  30          


<210>  33
<211>  32
<212>  PRT
<213>  Salmo salar


<220>
<221>  DISULFID
<222>  (1)..(7)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (32)..(32)
<223>  C-terminal amidation

<400>  33

Cys Ser Asn Leu Ser Thr Cys Val Leu Gly Lys Leu Ser Gln Glu Leu 
1               5                   10                  15      


His Lys Leu Gln Thr Tyr Pro Arg Thr Asn Thr Gly Ser Gly Thr Pro 
            20                  25                  30          


<210>  34
<211>  31
<212>  PRT
<213>  Dasyatis akajei


<220>
<221>  DISULFID
<222>  (1)..(7)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (31)..(31)
<223>  C-terminal amidation

<400>  34

Cys Thr Ser Leu Ser Thr Cys Val Val Gly Lys Ser Gln Gln Leu His 
1               5                   10                  15      


Lys Leu Gln Asn Ile Gln Arg Thr Asp Val Gly Ala Ala Thr Pro 
            20                  25                  30      



<210>  35
<211>  37
<212>  PRT
<213>  Homo sapiens


<220>
<221>  DISULFID
<222>  (2)..(7)
<223>  Cys2 and Cys 7 linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (37)..(37)
<223>  AMIDATION

<400>  35

Lys Cys Asn Thr Ala Thr Cys Ala Thr Gln Arg Leu Ala Asn Phe Leu 
1               5                   10                  15      


Val His Ser Ser Asn Asn Phe Gly Ala Ile Leu Ser Ser Thr Asn Val 
            20                  25                  30          


Gly Ser Asn Thr Tyr 


<210>  36
<211>  93
<212>  PRT
<213>  Mus musculus


<220>
<221>  DISULFID
<222>  (39)..(44)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (93)..(93)
<223>  C-terminal amidation

<400>  36

Met Met Cys Ile Ser Lys Leu Pro Ala Val Leu Leu Ile Leu Ser Val 
1               5                   10                  15      


Ala Leu Asn His Leu Arg Ala Thr Pro Val Arg Ser Gly Ser Asn Pro 
            20                  25                  30          


Gln Met Asp Lys Arg Lys Cys Asn Thr Ala Thr Cys Ala Thr Gln Arg 
        35                  40                  45              


Leu Ala Asn Phe Leu Val Arg Ser Ser Asn Asn Leu Gly Pro Val Leu 
    50                  55                  60                  


Pro Pro Thr Asn Val Gly Ser Asn Thr Tyr Gly Lys Arg Asn Ala Ala 
65                  70                  75                  80  


Gly Asp Pro Asn Arg Glu Ser Leu Asp Phe Leu Leu Val 
                85                  90              


<210>  37
<211>  93
<212>  PRT
<213>  Rattus norvegicus


<220>
<221>  DISULFID
<222>  (39)..(44)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (93)..(93)
<223>  C-terminal amidation

<400>  37

Met Arg Cys Ile Ser Arg Leu Pro Ala Val Leu Leu Ile Leu Ser Val 
1               5                   10                  15      


Ala Leu Gly His Leu Arg Ala Thr Pro Val Gly Ser Gly Thr Asn Pro 
            20                  25                  30          


Gln Val Asp Lys Arg Lys Cys Asn Thr Ala Thr Cys Ala Thr Gln Arg 
        35                  40                  45              


Leu Ala Asn Phe Leu Val Arg Ser Ser Asn Asn Leu Gly Pro Val Leu 
    50                  55                  60                  


Pro Pro Thr Asn Val Gly Ser Asn Thr Tyr Gly Lys Arg Asn Val Ala 
65                  70                  75                  80  


Glu Asp Pro Asn Arg Glu Ser Leu Asp Phe Leu Leu Leu 
                85                  90              


<210>  38
<211>  92
<212>  PRT
<213>  Cavia porcellus


<220>
<221>  DISULFID
<222>  (38)..(43)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (92)..(92)
<223>  C-terminal amidation

<400>  38

Met Cys Leu Leu Arg Leu Pro Val Thr Leu Leu Val Leu Cys Val Ala 
1               5                   10                  15      


Leu Asn Glu Leu Lys Ala Thr Ser Ile Ala Ser Asp Thr Gly His Gln 
            20                  25                  30          


Val Gly Lys Arg Lys Cys Asn Thr Ala Thr Cys Ala Thr Gln Arg Leu 
        35                  40                  45              


Thr Asn Phe Leu Val Arg Ser Ser His Asn Leu Gly Ala Ala Leu Leu 
    50                  55                  60                  


Pro Thr Asp Val Gly Ser Asn Thr Tyr Gly Lys Arg Asn Ala Pro Gln 
65                  70                  75                  80  


Ile Ser Asp Arg Glu Leu Leu His Tyr Leu Pro Leu 
                85                  90          


<210>  39
<211>  89
<212>  PRT
<213>  Canis lupis


<220>
<221>  DISULFID
<222>  (35)..(40)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (89)..(89)
<223>  C-terminal amidation

<400>  39

Met Cys Leu Leu Lys Leu Pro Val Val Leu Ile Ile Leu Ser Val Ala 
1               5                   10                  15      


Leu Asn His Leu Lys Ala Thr Pro Ile Lys Ser His Gln Met Glu Lys 
            20                  25                  30          


Arg Lys Cys Asn Thr Ala Thr Cys Ala Thr Gln Arg Leu Ala Asn Phe 
        35                  40                  45              


Leu Val Arg Thr Ser Asn Asn Leu Gly Ala Ile Leu Ser Pro Thr Asn 
    50                  55                  60                  


Val Gly Ser Asn Thr Tyr Gly Lys Arg Asn Thr Ile Glu Ile Leu Asn 
65                  70                  75                  80  


Arg Gly Pro Leu Asn Tyr Leu Pro Leu 
                85                  


<210>  40
<211>  89
<212>  PRT
<213>  Felis catus


<220>
<221>  DISULFID
<222>  (35)..(40)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (89)..(89)
<223>  C-terminal amidation

<400>  40

Met Cys Leu Leu Lys Leu Pro Val Val Leu Ile Val Leu Leu Val Ala 
1               5                   10                  15      


Leu His His Leu Lys Ala Thr Pro Ile Glu Ser Asn Gln Val Glu Lys 
            20                  25                  30          


Arg Lys Cys Asn Thr Ala Thr Cys Ala Thr Gln Arg Leu Ala Asn Phe 
        35                  40                  45              


Leu Ile Arg Ser Ser Asn Asn Leu Gly Ala Ile Leu Ser Pro Thr Asn 
    50                  55                  60                  


Val Gly Ser Asn Thr Tyr Gly Lys Arg Ser Thr Val Asp Ile Leu Asn 
65                  70                  75                  80  


Arg Glu Pro Leu Asn Tyr Leu Pro Phe 
                85                  


<210>  41
<211>  89
<212>  PRT
<213>  Papio hamadrys


<220>
<221>  DISULFID
<222>  (35)..(40)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (89)..(89)
<223>  C-terminal amidation

<400>  41

Met Cys Ile Leu Lys Leu Gln Val Phe Leu Ile Val Leu Phe Val Ala 
1               5                   10                  15      


Leu Asn His Leu Lys Ala Thr Pro Ile Glu Ser His Gln Gly Glu Lys 
            20                  25                  30          


Arg Ile Cys Asn Thr Ala Thr Cys Ala Thr Gln Arg Leu Ala Asn Phe 
        35                  40                  45              


Leu Val Arg Ser Ser Asn Asn Phe Gly Thr Ile Leu Ser Ser Thr Asn 
    50                  55                  60                  


Val Gly Ser Asn Thr Tyr Gly Lys Arg Asn Ala Val Glu Val Leu Lys 
65                  70                  75                  80  


Arg Glu Pro Leu Asn Tyr Leu Pro Leu 
                85                  


<210>  42
<211>  92
<212>  PRT
<213>  Mesocricetus auratus


<220>
<221>  DISULFID
<222>  (38)..(43)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (92)..(92)
<223>  C-terminal amidation

<400>  42

Met His Ile Ser Lys Leu Pro Ala Ala Leu Leu Ile Phe Ser Val Ala 
1               5                   10                  15      


Leu Asn His Leu Lys Ala Thr Pro Val Arg Ser Gly Thr Asn His Gln 
            20                  25                  30          


Met Asp Lys Arg Lys Cys Asn Thr Ala Thr Cys Ala Thr Gln Arg Leu 
        35                  40                  45              


Ala Asn Phe Leu Val His Ser Asn Asn Asn Leu Gly Pro Val Leu Ser 
    50                  55                  60                  


Pro Thr Asn Val Gly Ser Asn Thr Tyr Gly Lys Arg Ser Ala Ala Glu 
65                  70                  75                  80  


Ile Pro Asp Gly Asp Ser Leu Asp Leu Phe Leu Leu 
                85                  90          


<210>  43
<211>  91
<212>  PRT
<213>  Octodon degus


<220>
<221>  DISULFID
<222>  (38)..(43)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (91)..(91)
<223>  C-terminal amidation

<400>  43

Met Cys Leu Leu Gln Leu Pro Val Val Leu Leu Leu Leu Ser Ala Ala 
1               5                   10                  15      


Leu Asn Thr Leu Lys Ala Thr Pro Ile Ala Ser Asp Thr Asp His Arg 
            20                  25                  30          


Val Asp Lys Arg Lys Cys Asn Thr Ala Thr Cys Ala Thr Gln Arg Leu 
        35                  40                  45              


Thr Asn Phe Leu Val Arg Ser Ser His Asn Leu Gly Ala Ala Leu Pro 
    50                  55                  60                  


Pro Thr Lys Val Gly Ser Asn Thr Tyr Gly Arg Arg Asn Ala Glu Val 
65                  70                  75                  80  


Val Asp Val Glu Leu Leu His Tyr Leu Pro Leu 
                85                  90      


<210>  44
<211>  89
<212>  PRT
<213>  Monodelphis domestica


<220>
<221>  DISULFID
<222>  (35)..(40)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (89)..(89)
<223>  C-terminal amidation

<400>  44

Met Tyr Asn Leu Lys Leu Pro Ile Val Phe Ile Val Leu Ser Val Ala 
1               5                   10                  15      


Leu Ser Cys Leu Glu Ala Thr Pro Ile Asp Ser His His Leu Glu Lys 
            20                  25                  30          


Arg Lys Cys Asn Thr Ala Thr Cys Val Thr Gln Arg Leu Ala Asp Phe 
        35                  40                  45              


Leu Ile Arg Ser Ser Asn Asn Ile Gly Ala Val Phe Ser Pro Thr Asn 
    50                  55                  60                  


Val Gly Ser Asn Thr Tyr Gly Lys Arg Glu Ile Ala Gly Ile Leu Ser 
65                  70                  75                  80  


Arg Glu Pro Leu Asn Gln Phe Pro His 
                85                  


<210>  45
<211>  126
<212>  PRT
<213>  Carrassius auratus


<220>
<221>  DISULFID
<222>  (77)..(82)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (126)..(126)
<223>  C-terminal amidation

<400>  45

Met Tyr Leu Pro Ser Gln Ile Leu Ile Phe Leu Val Met Leu Gln Cys 
1               5                   10                  15      


Val Ala Thr Val Pro Tyr Asn Arg Tyr Ser Leu Ser Ser Asn Asp Lys 
            20                  25                  30          


Pro Asp Ala Ser Arg Glu Val Asn Gly Trp Leu Val Thr Asp Leu Ser 
        35                  40                  45              


Asp Asn Pro Phe Val Ser Phe Thr Arg Pro Arg Pro Pro Trp Gly Leu 
    50                  55                  60                  


Pro Ala Val Asn Ser His Tyr Met Glu Lys Arg Lys Cys Asn Thr Ala 
65                  70                  75                  80  


Thr Cys Val Thr Gln Arg Leu Ala Asp Phe Leu Val Arg Ser Ser Asn 
                85                  90                  95      


Thr Arg Gly Thr Val Tyr Ala Pro Thr Asn Val Gly Ala Asn Thr Tyr 
            100                 105                 110         


Gly Lys Arg Asp Leu Leu Gln Ser Pro Ile Tyr Leu Pro Leu 
        115                 120                 125     


<210>  46
<211>  130
<212>  PRT
<213>  Osmerus mordax


<220>
<221>  DISULFID
<222>  (81)..(86)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (130)..(130)
<223>  C-terminal amidation

<400>  46

Met Tyr His Leu Arg Leu Pro Met Leu Leu Ile Val Pro Leu Val Leu 
1               5                   10                  15      


Leu Pro Cys Val Ile Thr Ala Pro Ser Asn Arg Tyr Phe Ser Pro Ile 
            20                  25                  30          


Ser Ser Gly Gln Glu Ser Ala Pro Pro Glu Arg Glu Asp Trp Leu Leu 
        35                  40                  45              


Pro Glu Trp Val Ser Asn Pro Phe Leu Ser Leu Val Gly Ala Arg Pro 
    50                  55                  60                  


Gln Arg Gly Leu Pro Ala Val Asn Ser His His Ile Glu Lys Arg Lys 
65                  70                  75                  80  


Cys Asn Thr Ala Thr Cys Val Thr Gln Arg Leu Ala Asp Phe Leu Val 
                85                  90                  95      


Arg Ser Ser Asn Thr Ile Gly Thr Val Tyr Ala Pro Thr Asn Val Gly 
            100                 105                 110         


Ser Ser Thr Tyr Gly Lys Arg Glu Leu Leu Gln Pro Pro Ser Tyr Phe 
        115                 120                 125             


Pro Leu 
    130 


<210>  47
<211>  37
<212>  PRT
<213>  Cricetulus griseus


<220>
<221>  DISULFID
<222>  (2)..(7)
<223>  Cys residues linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (37)..(37)
<223>  C-terminal amidation

<400>  47

Lys Cys Asn Thr Ala Thr Cys Ala Thr Gln Arg Leu Ala Asn Phe Leu 
1               5                   10                  15      


Val His Ser Asn Asn Asn Leu Gly Pro Val Leu Ser Pro Thr Asn Val 
            20                  25                  30          


Gly Ser Asn Thr Tyr 
        35          



<210>  48
<211>  37
<212>  PRT
<213>  Artificial Sequence

<220>
<223>  Synthetic peptide


<220>
<221>  DISULFID
<222>  (2)..(7)
<223>  Cys2 and Cys7 linked via disulfide bridge

<220>
<221>  MOD_RES
<222>  (37)..(37)
<223>  AMIDATION

<400>  48

Lys Cys Asn Thr Ala Thr Cys Ala Thr Gln Arg Leu Ala Asn Phe Leu 
1               5                   10                  15      


Val His Ser Ser Asn Asn Phe Gly Pro Ile Leu Pro Pro Thr Asn Val 
            20                  25                  30          


Gly Ser Asn Thr Tyr 
        35 


<210>  49
<211>  84
<212>  PRT
<213>  Homo sapiens

<400>  49

Ser Val Ser Glu Ile Gln Leu Met His Asn Leu Gly Lys His Leu Asn 
1               5                   10                  15      


Ser Met Glu Arg Val Glu Trp Leu Arg Lys Lys Leu Gln Asp Val His 
            20                  25                  30          


Asn Phe Val Ala Leu Gly Ala Pro Leu Ala Pro Arg Asp Ala Gly Ser 
        35                  40                  45              


Gln Arg Pro Arg Lys Lys Glu Asp Asn Val Leu Val Glu Ser His Glu 
    50                  55                  60                  


Lys Ser Leu Gly Glu Ala Asp Lys Ala Asp Val Asn Val Leu Thr Lys 
65                  70                  75                  80  


Ala Lys Ser Gln 



<210>  50
<211>  31
<212>  PRT
<213>  Homo sapiens

<400>  50

His Ala Glu Gly Thr Phe Thr Ser Asp Val Ser Ser Tyr Leu Glu Gly 
1               5                   10                  15      


Gln Ala Ala Lys Glu Phe Ile Ala Trp Leu Val Lys Gly Arg Gly 
            20                  25                  30      



<210>  51
<211>  37
<212>  PRT
<213>  Homo sapiens

<400>  51

His Ser Gln Gly Thr Phe Thr Ser Asp Tyr Ser Lys Tyr Leu Asp Ser 
1               5                   10                  15      


Arg Arg Ala Gln Asp Phe Val Gln Trp Leu Met Asp Thr Lys Arg Asn 
            20                  25                  30          


Arg Asn Asn Ile Ala 
        35          


<210>  52
<211>  42
<212>  PRT
<213>  Homo sapiens

<400>  52

Tyr Ala Glu Gly Thr Phe Ile Ser Asp Tyr Ser Ile Ala Met Asp Lys 
1               5                   10                  15      


Ile His Gln Gln Asp Phe Val Asn Trp Leu Leu Ala Gln Lys Gly Lys 
            20                  25                  30          


Lys Asn Asp Trp Lys His Asn Ile Thr Gln 
        35                  40          


<210>  53
<211>  33
<212>  PRT
<213>  Homo sapiens

<400>  53

His Ala Asp Gly Ser Phe Ser Asp Glu Met Asn Thr Ile Leu Asp Asn 
1               5                   10                  15      


Leu Ala Ala Arg Asp Phe Ile Asn Trp Leu Ile Gln Thr Lys Ile Thr 
            20                  25                  30          


Asp 
    



<210>  54
<211>  39
<212>  PRT
<213>  Heloderma suspectum

<400>  54

His Gly Glu Gly Thr Phe Thr Ser Asp Leu Ser Lys Gln Met Glu Glu 
1               5                   10                  15      


Glu Ala Val Arg Leu Phe Ile Glu Trp Leu Lys Asn Gly Gly Pro Ser 
            20                  25                  30          


Ser Gly Ala Pro Pro Pro Ser 
        35                  




<210>  55
<211>  28
<212>  PRT
<213>  Homo sapiens


<220>
<221>  MOD_RES
<222>  (28)..(28)
<223>  AMIDATION

<400>  55

His Ser Asp Ala Val Phe Thr Asp Asn Tyr Thr Arg Leu Arg Lys Gln 
1               5                   10                  15      


Met Ala Val Lys Lys Tyr Leu Asn Ser Ile Leu Asn 
            20                  25              


<210>  56
<211>  27
<212>  PRT
<213>  Homo sapiens

<400>  56

His Ser Asp Gly Ile Phe Thr Asp Ser Tyr Ser Arg Tyr Arg Lys Gln 
1               5                   10                  15      


Met Ala Val Lys Lys Tyr Leu Ala Ala Val Leu 
            20                  25          


<210>  57
<211>  27
<212>  PRT
<213>  Homo sapiens


<220>
<221>  MOD_RES
<222>  (27)..(27)
<223>  AMIDATION

<400>  57

His Ala Asp Gly Val Phe Thr Ser Asp Phe Ser Lys Leu Leu Gly Gln 
1               5                   10                  15      


Leu Ser Ala Lys Lys Tyr Leu Glu Ser Leu Met 
            20                  25          




<210>  58
<211>  27
<212>  PRT
<213>  Homo sapiens


<220>
<221>  MOD_RES
<222>  (27)..(27)
<223>  AMIDATION

<400>  58

His Ser Asp Gly Thr Phe Thr Ser Glu Leu Ser Arg Leu Arg Glu Gly 
1               5                   10                  15      


Ala Arg Leu Gln Arg Leu Leu Gln Gly Leu Val 
            20                  25          
