                         SEQUENCE LISTING

<110>  Arcarios B.V.
       Eijken, Hermanus Johannes Marco
       de Wilde, Gert
 
<120>  Follistatin derivatives

<130>  233.005 WO

<150>  EP13168577.8
<151>  2013-05-21

<160>  23    

<170>  PatentIn version 3.5

<210>  1
<211>  344
<212>  PRT
<213>  Homo sapiens


<220>
<221>  SIGNAL
<222>  (1)..(29)

<220>
<221>  DOMAIN
<222>  (30)..(92)
<223>  FSND

<220>
<221>  DOMAIN
<222>  (93)..(165)
<223>  FSD1

<220>
<221>  SITE
<222>  (104)..(113)
<223>  Heparin Binding Site

<220>
<221>  DOMAIN
<222>  (166)..(240)
<223>  FSD2

<220>
<221>  DOMAIN
<222>  (241)..(317)
<223>  FSD3

<220>
<221>  DOMAIN
<222>  (318)..(344)
<223>  CD

<400>  1

Met Val Arg Ala Arg His Gln Pro Gly Gly Leu Cys Leu Leu Leu Leu 
1               5                   10                  15      


Leu Leu Cys Gln Phe Met Glu Asp Arg Ser Ala Gln Ala Gly Asn Cys 
            20                  25                  30          


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


Glu Leu Ser Lys Glu Glu Cys Cys Ser Thr Gly Arg Leu Ser Thr Ser 
    50                  55                  60                  


Trp Thr Glu Glu Asp Val Asn Asp Asn Thr Leu Phe Lys Trp Met Ile 
65                  70                  75                  80  


Phe Asn Gly Gly Ala Pro Asn Cys Ile Pro Cys Lys Glu Thr Cys Glu 
                85                  90                  95      


Asn Val Asp Cys Gly Pro Gly Lys Lys Cys Arg Met Asn Lys Lys Asn 
            100                 105                 110         


Lys Pro Arg Cys Val Cys Ala Pro Asp Cys Ser Asn Ile Thr Trp Lys 
        115                 120                 125             


Gly Pro Val Cys Gly Leu Asp Gly Lys Thr Tyr Arg Asn Glu Cys Ala 
    130                 135                 140                 


Leu Leu Lys Ala Arg Cys Lys Glu Gln Pro Glu Leu Glu Val Gln Tyr 
145                 150                 155                 160 


Gln Gly Arg Cys Lys Lys Thr Cys Arg Asp Val Phe Cys Pro Gly Ser 
                165                 170                 175     


Ser Thr Cys Val Val Asp Gln Thr Asn Asn Ala Tyr Cys Val Thr Cys 
            180                 185                 190         


Asn Arg Ile Cys Pro Glu Pro Ala Ser Ser Glu Gln Tyr Leu Cys Gly 
        195                 200                 205             


Asn Asp Gly Val Thr Tyr Ser Ser Ala Cys His Leu Arg Lys Ala Thr 
    210                 215                 220                 


Cys Leu Leu Gly Arg Ser Ile Gly Leu Ala Tyr Glu Gly Lys Cys Ile 
225                 230                 235                 240 


Lys Ala Lys Ser Cys Glu Asp Ile Gln Cys Thr Gly Gly Lys Lys Cys 
                245                 250                 255     


Leu Trp Asp Phe Lys Val Gly Arg Gly Arg Cys Ser Leu Cys Asp Glu 
            260                 265                 270         


Leu Cys Pro Asp Ser Lys Ser Asp Glu Pro Val Cys Ala Ser Asp Asn 
        275                 280                 285             


Ala Thr Tyr Ala Ser Glu Cys Ala Met Lys Glu Ala Ala Cys Ser Ser 
    290                 295                 300                 


Gly Val Leu Leu Glu Val Lys His Ser Gly Ser Cys Asn Ser Ile Ser 
305                 310                 315                 320 


Glu Asp Thr Glu Glu Glu Glu Glu Asp Glu Asp Gln Asp Tyr Ser Phe 
                325                 330                 335     


Pro Ile Ser Ser Ile Leu Glu Trp 
            340                 


<210>  2
<211>  227
<212>  PRT
<213>  Homo sapiens


<220>
<221>  DOMAIN
<222>  (1)..(227)
<223>  Human IgG1 Fc domain

<400>  2

Asp Lys Thr His Thr Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu Gly 
1               5                   10                  15      


Gly Pro Ser Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met 
            20                  25                  30          


Ile Ser Arg Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His 
        35                  40                  45              


Glu Asp Pro Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val 
    50                  55                  60                  


His Asn Ala Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr 
65                  70                  75                  80  


Arg Val Val Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly 
                85                  90                  95      


Lys Glu Tyr Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile 
            100                 105                 110         


Glu Lys Thr Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val 
        115                 120                 125             


Tyr Thr Leu Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser 
    130                 135                 140                 


Leu Thr Cys Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu 
145                 150                 155                 160 


Trp Glu Ser Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro 
                165                 170                 175     


Val Leu Asp Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val 
            180                 185                 190         


Asp Lys Ser Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Met 
        195                 200                 205             


His Glu Ala Leu His Asn His Tyr Thr Gln Lys Ser Leu Ser Leu Ser 
    210                 215                 220                 


Pro Gly Lys 
225         


<210>  3
<211>  571
<212>  PRT
<213>  Artificial sequence

<220>
<223>  Full length human follistatin (315 aa splice variant) linked to 
       human Fc


<220>
<221>  SIGNAL
<222>  (1)..(29)

<220>
<221>  DOMAIN
<222>  (30)..(344)
<223>  Human follistatin 315 splice variant

<220>
<221>  DOMAIN
<222>  (345)..(571)
<223>  Human IgG1 Fc domain

<400>  3

Met Val Arg Ala Arg His Gln Pro Gly Gly Leu Cys Leu Leu Leu Leu 
1               5                   10                  15      


Leu Leu Cys Gln Phe Met Glu Asp Arg Ser Ala Gln Ala Gly Asn Cys 
            20                  25                  30          


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


Glu Leu Ser Lys Glu Glu Cys Cys Ser Thr Gly Arg Leu Ser Thr Ser 
    50                  55                  60                  


Trp Thr Glu Glu Asp Val Asn Asp Asn Thr Leu Phe Lys Trp Met Ile 
65                  70                  75                  80  


Phe Asn Gly Gly Ala Pro Asn Cys Ile Pro Cys Lys Glu Thr Cys Glu 
                85                  90                  95      


Asn Val Asp Cys Gly Pro Gly Lys Lys Cys Arg Met Asn Lys Lys Asn 
            100                 105                 110         


Lys Pro Arg Cys Val Cys Ala Pro Asp Cys Ser Asn Ile Thr Trp Lys 
        115                 120                 125             


Gly Pro Val Cys Gly Leu Asp Gly Lys Thr Tyr Arg Asn Glu Cys Ala 
    130                 135                 140                 


Leu Leu Lys Ala Arg Cys Lys Glu Gln Pro Glu Leu Glu Val Gln Tyr 
145                 150                 155                 160 


Gln Gly Arg Cys Lys Lys Thr Cys Arg Asp Val Phe Cys Pro Gly Ser 
                165                 170                 175     


Ser Thr Cys Val Val Asp Gln Thr Asn Asn Ala Tyr Cys Val Thr Cys 
            180                 185                 190         


Asn Arg Ile Cys Pro Glu Pro Ala Ser Ser Glu Gln Tyr Leu Cys Gly 
        195                 200                 205             


Asn Asp Gly Val Thr Tyr Ser Ser Ala Cys His Leu Arg Lys Ala Thr 
    210                 215                 220                 


Cys Leu Leu Gly Arg Ser Ile Gly Leu Ala Tyr Glu Gly Lys Cys Ile 
225                 230                 235                 240 


Lys Ala Lys Ser Cys Glu Asp Ile Gln Cys Thr Gly Gly Lys Lys Cys 
                245                 250                 255     


Leu Trp Asp Phe Lys Val Gly Arg Gly Arg Cys Ser Leu Cys Asp Glu 
            260                 265                 270         


Leu Cys Pro Asp Ser Lys Ser Asp Glu Pro Val Cys Ala Ser Asp Asn 
        275                 280                 285             


Ala Thr Tyr Ala Ser Glu Cys Ala Met Lys Glu Ala Ala Cys Ser Ser 
    290                 295                 300                 


Gly Val Leu Leu Glu Val Lys His Ser Gly Ser Cys Asn Ser Ile Ser 
305                 310                 315                 320 


Glu Asp Thr Glu Glu Glu Glu Glu Asp Glu Asp Gln Asp Tyr Ser Phe 
                325                 330                 335     


Pro Ile Ser Ser Ile Leu Glu Trp Asp Lys Thr His Thr Cys Pro Pro 
            340                 345                 350         


Cys Pro Ala Pro Glu Leu Leu Gly Gly Pro Ser Val Phe Leu Phe Pro 
        355                 360                 365             


Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr Pro Glu Val Thr 
    370                 375                 380                 


Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu Val Lys Phe Asn 
385                 390                 395                 400 


Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys Thr Lys Pro Arg 
                405                 410                 415     


Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser Val Leu Thr Val 
            420                 425                 430         


Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys Cys Lys Val Ser 
        435                 440                 445             


Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile Ser Lys Ala Lys 
    450                 455                 460                 


Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro Pro Ser Arg Glu 
465                 470                 475                 480 


Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu Val Lys Gly Phe 
                485                 490                 495     


Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn Gly Gln Pro Glu 
            500                 505                 510         


Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser Asp Gly Ser Phe 
        515                 520                 525             


Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg Trp Gln Gln Gly 
    530                 535                 540                 


Asn Val Phe Ser Cys Ser Val Met His Glu Ala Leu His Asn His Tyr 
545                 550                 555                 560 


Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
                565                 570     


<210>  4
<211>  571
<212>  PRT
<213>  Artificial sequence

<220>
<223>  FST315-hFc-dHBS


<220>
<221>  DOMAIN
<222>  (1)..(344)
<223>  Human follistatin (315 aa splice variant)

<220>
<221>  SIGNAL
<222>  (1)..(29)

<220>
<221>  SITE
<222>  (104)..(113)
<223>  Mutated Heparin Binding Site, wild type sequence of FSD1 replaced
       by corresponding domain in FSD2

<220>
<221>  DOMAIN
<222>  (177)..(186)
<223>  Corresponding domain FSD2

<220>
<221>  DOMAIN
<222>  (345)..(571)
<223>  Human IgG2A Fc domain

<400>  4

Met Val Arg Ala Arg His Gln Pro Gly Gly Leu Cys Leu Leu Leu Leu 
1               5                   10                  15      


Leu Leu Cys Gln Phe Met Glu Asp Arg Ser Ala Gln Ala Gly Asn Cys 
            20                  25                  30          


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


Glu Leu Ser Lys Glu Glu Cys Cys Ser Thr Gly Arg Leu Ser Thr Ser 
    50                  55                  60                  


Trp Thr Glu Glu Asp Val Asn Asp Asn Thr Leu Phe Lys Trp Met Ile 
65                  70                  75                  80  


Phe Asn Gly Gly Ala Pro Asn Cys Ile Pro Cys Lys Glu Thr Cys Glu 
                85                  90                  95      


Asn Val Asp Cys Gly Pro Gly Ser Thr Cys Val Val Asp Gln Thr Asn 
            100                 105                 110         


Asn Pro Arg Cys Val Cys Ala Pro Asp Cys Ser Asn Ile Thr Trp Lys 
        115                 120                 125             


Gly Pro Val Cys Gly Leu Asp Gly Lys Thr Tyr Arg Asn Glu Cys Ala 
    130                 135                 140                 


Leu Leu Lys Ala Arg Cys Lys Glu Gln Pro Glu Leu Glu Val Gln Tyr 
145                 150                 155                 160 


Gln Gly Arg Cys Lys Lys Thr Cys Arg Asp Val Phe Cys Pro Gly Ser 
                165                 170                 175     


Ser Thr Cys Val Val Asp Gln Thr Asn Asn Ala Tyr Cys Val Thr Cys 
            180                 185                 190         


Asn Arg Ile Cys Pro Glu Pro Ala Ser Ser Glu Gln Tyr Leu Cys Gly 
        195                 200                 205             


Asn Asp Gly Val Thr Tyr Ser Ser Ala Cys His Leu Arg Lys Ala Thr 
    210                 215                 220                 


Cys Leu Leu Gly Arg Ser Ile Gly Leu Ala Tyr Glu Gly Lys Cys Ile 
225                 230                 235                 240 


Lys Ala Lys Ser Cys Glu Asp Ile Gln Cys Thr Gly Gly Lys Lys Cys 
                245                 250                 255     


Leu Trp Asp Phe Lys Val Gly Arg Gly Arg Cys Ser Leu Cys Asp Glu 
            260                 265                 270         


Leu Cys Pro Asp Ser Lys Ser Asp Glu Pro Val Cys Ala Ser Asp Asn 
        275                 280                 285             


Ala Thr Tyr Ala Ser Glu Cys Ala Met Lys Glu Ala Ala Cys Ser Ser 
    290                 295                 300                 


Gly Val Leu Leu Glu Val Lys His Ser Gly Ser Cys Asn Ser Ile Ser 
305                 310                 315                 320 


Glu Asp Thr Glu Glu Glu Glu Glu Asp Glu Asp Gln Asp Tyr Ser Phe 
                325                 330                 335     


Pro Ile Ser Ser Ile Leu Glu Trp Asp Lys Thr His Thr Cys Pro Pro 
            340                 345                 350         


Cys Pro Ala Pro Glu Leu Leu Gly Gly Pro Ser Val Phe Leu Phe Pro 
        355                 360                 365             


Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg Thr Pro Glu Val Thr 
    370                 375                 380                 


Cys Val Val Val Asp Val Ser His Glu Asp Pro Glu Val Lys Phe Asn 
385                 390                 395                 400 


Trp Tyr Val Asp Gly Val Glu Val His Asn Ala Lys Thr Lys Pro Arg 
                405                 410                 415     


Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val Ser Val Leu Thr Val 
            420                 425                 430         


Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys Cys Lys Val Ser 
        435                 440                 445             


Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile Ser Lys Ala Lys 
    450                 455                 460                 


Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro Pro Ser Arg Glu 
465                 470                 475                 480 


Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys Leu Val Lys Gly Phe 
                485                 490                 495     


Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser Asn Gly Gln Pro Glu 
            500                 505                 510         


Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp Ser Asp Gly Ser Phe 
        515                 520                 525             


Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg Trp Gln Gln Gly 
    530                 535                 540                 


Asn Val Phe Ser Cys Ser Val Met His Glu Ala Leu His Asn His Tyr 
545                 550                 555                 560 


Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
                565                 570     


<210>  5
<211>  544
<212>  PRT
<213>  Artificial sequence

<220>
<223>  FST288-hFc-dHBS - Human follistatin (288 aa splice variant) 
       linked to human IgG1 Fc domain and withthe HBS domain replaced


<220>
<221>  SIGNAL
<222>  (1)..(29)

<220>
<221>  DOMAIN
<222>  (30)..(317)
<223>  Human follistatin (288 aa splice variant)

<220>
<221>  SITE
<222>  (104)..(113)
<223>  Mutated Heparin Binding Site, wild type sequence of FSD1 replaced
       by corresponding domain in FSD2

<220>
<221>  DOMAIN
<222>  (177)..(186)
<223>  Corresponding domain FSD2

<220>
<221>  DOMAIN
<222>  (318)..(544)
<223>  Human IgG1 Fc domain

<400>  5

Met Val Arg Ala Arg His Gln Pro Gly Gly Leu Cys Leu Leu Leu Leu 
1               5                   10                  15      


Leu Leu Cys Gln Phe Met Glu Asp Arg Ser Ala Gln Ala Gly Asn Cys 
            20                  25                  30          


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


Glu Leu Ser Lys Glu Glu Cys Cys Ser Thr Gly Arg Leu Ser Thr Ser 
    50                  55                  60                  


Trp Thr Glu Glu Asp Val Asn Asp Asn Thr Leu Phe Lys Trp Met Ile 
65                  70                  75                  80  


Phe Asn Gly Gly Ala Pro Asn Cys Ile Pro Cys Lys Glu Thr Cys Glu 
                85                  90                  95      


Asn Val Asp Cys Gly Pro Gly Ser Thr Cys Val Val Asp Gln Thr Asn 
            100                 105                 110         


Asn Pro Arg Cys Val Cys Ala Pro Asp Cys Ser Asn Ile Thr Trp Lys 
        115                 120                 125             


Gly Pro Val Cys Gly Leu Asp Gly Lys Thr Tyr Arg Asn Glu Cys Ala 
    130                 135                 140                 


Leu Leu Lys Ala Arg Cys Lys Glu Gln Pro Glu Leu Glu Val Gln Tyr 
145                 150                 155                 160 


Gln Gly Arg Cys Lys Lys Thr Cys Arg Asp Val Phe Cys Pro Gly Ser 
                165                 170                 175     


Ser Thr Cys Val Val Asp Gln Thr Asn Asn Ala Tyr Cys Val Thr Cys 
            180                 185                 190         


Asn Arg Ile Cys Pro Glu Pro Ala Ser Ser Glu Gln Tyr Leu Cys Gly 
        195                 200                 205             


Asn Asp Gly Val Thr Tyr Ser Ser Ala Cys His Leu Arg Lys Ala Thr 
    210                 215                 220                 


Cys Leu Leu Gly Arg Ser Ile Gly Leu Ala Tyr Glu Gly Lys Cys Ile 
225                 230                 235                 240 


Lys Ala Lys Ser Cys Glu Asp Ile Gln Cys Thr Gly Gly Lys Lys Cys 
                245                 250                 255     


Leu Trp Asp Phe Lys Val Gly Arg Gly Arg Cys Ser Leu Cys Asp Glu 
            260                 265                 270         


Leu Cys Pro Asp Ser Lys Ser Asp Glu Pro Val Cys Ala Ser Asp Asn 
        275                 280                 285             


Ala Thr Tyr Ala Ser Glu Cys Ala Met Lys Glu Ala Ala Cys Ser Ser 
    290                 295                 300                 


Gly Val Leu Leu Glu Val Lys His Ser Gly Ser Cys Asn Asp Lys Thr 
305                 310                 315                 320 


His Thr Cys Pro Pro Cys Pro Ala Pro Glu Leu Leu Gly Gly Pro Ser 
                325                 330                 335     


Val Phe Leu Phe Pro Pro Lys Pro Lys Asp Thr Leu Met Ile Ser Arg 
            340                 345                 350         


Thr Pro Glu Val Thr Cys Val Val Val Asp Val Ser His Glu Asp Pro 
        355                 360                 365             


Glu Val Lys Phe Asn Trp Tyr Val Asp Gly Val Glu Val His Asn Ala 
    370                 375                 380                 


Lys Thr Lys Pro Arg Glu Glu Gln Tyr Asn Ser Thr Tyr Arg Val Val 
385                 390                 395                 400 


Ser Val Leu Thr Val Leu His Gln Asp Trp Leu Asn Gly Lys Glu Tyr 
                405                 410                 415     


Lys Cys Lys Val Ser Asn Lys Ala Leu Pro Ala Pro Ile Glu Lys Thr 
            420                 425                 430         


Ile Ser Lys Ala Lys Gly Gln Pro Arg Glu Pro Gln Val Tyr Thr Leu 
        435                 440                 445             


Pro Pro Ser Arg Glu Glu Met Thr Lys Asn Gln Val Ser Leu Thr Cys 
    450                 455                 460                 


Leu Val Lys Gly Phe Tyr Pro Ser Asp Ile Ala Val Glu Trp Glu Ser 
465                 470                 475                 480 


Asn Gly Gln Pro Glu Asn Asn Tyr Lys Thr Thr Pro Pro Val Leu Asp 
                485                 490                 495     


Ser Asp Gly Ser Phe Phe Leu Tyr Ser Lys Leu Thr Val Asp Lys Ser 
            500                 505                 510         


Arg Trp Gln Gln Gly Asn Val Phe Ser Cys Ser Val Met His Glu Ala 
        515                 520                 525             


Leu His Asn His Tyr Thr Gln Lys Ser Leu Ser Leu Ser Pro Gly Lys 
    530                 535                 540                 


<210>  6
<211>  10
<212>  PRT
<213>  Homo sapiens


<220>
<221>  SITE
<222>  (1)..(10)
<223>  Heparin Binding Site

<400>  6

Lys Lys Cys Arg Met Asn Lys Lys Asn Lys 
1               5                   10  


<210>  7
<211>  10
<212>  PRT
<213>  Homo sapiens


<220>
<221>  DOMAIN
<222>  (1)..(10)
<223>  FSD2 domain used to replace the HBS domain in FSD1

<400>  7

Ser Thr Cys Val Val Asp Gln Thr Asn Asn 
1               5                   10  


<210>  8
<211>  699
<212>  DNA
<213>  Mus musculus


<220>
<221>  misc_feature
<222>  (1)..(699)
<223>  IgG2A Fc domain

<400>  8
cccagaggcc ccaccatcaa gccttgcccc ccttgcaagt gccctgcccc taatctgctg       60

ggaggcccct ccgtgttcat cttcccaccc aagatcaagg acgtgctgat gatctccctg      120

tcccccatcg tgacatgcgt ggtggtggac gtgtccgagg acgaccctga cgtgcagatc      180

agttggttcg tgaacaacgt ggaagtgcac accgcccaga cccagaccca cagagaggac      240

tacaactcca ccctgcgggt ggtgtccgcc ctgcctatcc agcaccagga ttggatgtcc      300

ggcaaagaat tcaagtgcaa agtgaacaac aaggacctgc ctgccccaat cgagcggacc      360

atctccaagc ctaagggctc cgtgcgtgcc ccccaggtgt acgtgctgcc acctcccgaa      420

gaagagatga ccaagaaaca agtgaccctg acctgtatgg tcaccgactt catgcctgag      480

gacatctacg tggaatggac caacaatggc aaaaccgagc tgaactacaa gaacaccgag      540

cccgtgctgg actccgacgg ctcctacttc atgtactcca agctgcgcgt ggaaaagaaa      600

aactgggtgg aacggaactc ctactcctgc tccgtggtgc acgagggcct gcacaatcac      660

cacaccacca agtccttctc ccggaccccc ggcaagtga                             699


<210>  9
<211>  25
<212>  DNA
<213>  Artificial sequence

<220>
<223>  hFST-for primer


<220>
<221>  hFST-for
<222>  (1)..(25)

<400>  9
caccatggtc cgcgcgaggc accag                                             25


<210>  10
<211>  41
<212>  DNA
<213>  Artificial sequence

<220>
<223>  288/mFc-rev primer


<220>
<221>  288/mFc-rev
<222>  (1)..(41)

<400>  10
gcttgatggt ggggcctctg gggttgcaag atccggagtg c                           41


<210>  11
<211>  46
<212>  DNA
<213>  Artificial sequence

<220>
<223>  315/mFc-rev primer


<220>
<221>  315/mFc-rev
<222>  (1)..(46)

<400>  11
gcttgatggt ggggcctctg ggccactcta gaatagaaga tatagg                      46


<210>  12
<211>  40
<212>  DNA
<213>  Artificial sequence

<220>
<223>  288/hFc-rev primer


<220>
<221>  288/hFc-rev
<222>  (1)..(40)

<400>  12
gggcatgtgt gagttttgtc gttgcaagat ccggagtgct                             40


<210>  13
<211>  40
<212>  DNA
<213>  Artificial sequence

<220>
<223>  315/hFc-rev primer


<220>
<221>  315/hFc-rev
<222>  (1)..(40)

<400>  13
gggcatgtgt gagttttgtc ccactctaga atagaagata                             40


<210>  14
<211>  41
<212>  DNA
<213>  Artificial sequence

<220>
<223>  288/mFc-for primer


<220>
<221>  288/mFc-for
<222>  (1)..(41)

<400>  14
gcactccgga tcttgcaacc ccagagggcc caccatcaag c                           41


<210>  15
<211>  46
<212>  DNA
<213>  Artificial sequence

<220>
<223>  315/mFc-for primer


<220>
<221>  315/mFc-for
<222>  (1)..(46)

<400>  15
cctatatctt ctattctaga gtggcccaga ggccccacca tcaagc                      46


<210>  16
<211>  20
<212>  DNA
<213>  Artificial sequence

<220>
<223>  mFc-rev primer


<220>
<221>  mFc-rev
<222>  (1)..(20)

<400>  16
tcacttgccg ggggtccggg                                                   20


<210>  17
<211>  40
<212>  DNA
<213>  Artificial sequence

<220>
<223>  288/hFc-for primer


<220>
<221>  288/hFc-for
<222>  (1)..(40)

<400>  17
agcactccgg atcttgcaac gacaaaactc acacatgccc                             40


<210>  18
<211>  40
<212>  DNA
<213>  Artificial sequence

<220>
<223>  315/hFc-for primer


<220>
<221>  315/hFc-for
<222>  (1)..(40)

<400>  18
tatcttctat tctagagtgg gacaaaactc acacatgccc                             40


<210>  19
<211>  17
<212>  DNA
<213>  Artificial sequence

<220>
<223>  hFc-rev primer


<220>
<221>  hFc-rev
<222>  (1)..(17)

<400>  19
tcatttaccc ggagaca                                                      17


<210>  20
<211>  59
<212>  DNA
<213>  Artificial sequence

<220>
<223>  hFST-Swop-rev1 primer


<220>
<221>  hFST-Swop-rev1
<222>  (1)..(59)

<400>  20
gttgttggtc tgatccacca cgcaggtgct cccaggtcca cagtccacgt tctcacacg        59


<210>  21
<211>  61
<212>  DNA
<213>  Artificial sequence

<220>
<223>  hFST-Swop-for primer


<220>
<221>  hFST-Swop-for
<222>  (1)..(61)

<400>  21
agcacctgcg tggtggatca gaccaacaac cccccgctgc gtctgcgccc cggattgttc       60

c                                                                       61


<210>  22
<211>  60
<212>  DNA
<213>  Artificial sequence

<220>
<223>  hFST-Swop-rev2 primer


<220>
<221>  hFST-Swop-rev2
<222>  (1)..(60)

<400>  22
ggaacaatcc ggggcgcaga cgcagcgggg gttgttggtc tgatccacca cgcaggtgct       60


<210>  23
<211>  315
<212>  PRT
<213>  Artificial sequence

<220>
<223>  FST315-dHBS


<220>
<221>  DOMAIN
<222>  (1)..(315)
<223>  Human FST315 with mutated HBS

<220>
<221>  DOMAIN
<222>  (1)..(63)
<223>  FSND

<220>
<221>  DOMAIN
<222>  (64)..(136)
<223>  FSD1

<220>
<221>  SITE
<222>  (75)..(84)
<223>  Mutated Heparin Binding Site, wild type sequence of FSD1 replaced
       by corresponding domain in FSD2

<220>
<221>  DOMAIN
<222>  (137)..(211)
<223>  FSD2

<220>
<221>  SITE
<222>  (148)..(157)
<223>  Corresponding domain FSD2

<220>
<221>  DOMAIN
<222>  (212)..(288)
<223>  FSD3

<220>
<221>  DOMAIN
<222>  (289)..(315)
<223>  C terminal domain

<400>  23

Gly Asn Cys Trp Leu Arg Gln Ala Lys Asn Gly Arg Cys Gln Val Leu 
1               5                   10                  15      


Tyr Lys Thr Glu Leu Ser Lys Glu Glu Cys Cys Ser Thr Gly Arg Leu 
            20                  25                  30          


Ser Thr Ser Trp Thr Glu Glu Asp Val Asn Asp Asn Thr Leu Phe Lys 
        35                  40                  45              


Trp Met Ile Phe Asn Gly Gly Ala Pro Asn Cys Ile Pro Cys Lys Glu 
    50                  55                  60                  


Thr Cys Glu Asn Val Asp Cys Gly Pro Gly Ser Thr Cys Val Val Asp 
65                  70                  75                  80  


Gln Thr Asn Asn Pro Arg Cys Val Cys Ala Pro Asp Cys Ser Asn Ile 
                85                  90                  95      


Thr Trp Lys Gly Pro Val Cys Gly Leu Asp Gly Lys Thr Tyr Arg Asn 
            100                 105                 110         


Glu Cys Ala Leu Leu Lys Ala Arg Cys Lys Glu Gln Pro Glu Leu Glu 
        115                 120                 125             


Val Gln Tyr Gln Gly Arg Cys Lys Lys Thr Cys Arg Asp Val Phe Cys 
    130                 135                 140                 


Pro Gly Ser Ser Thr Cys Val Val Asp Gln Thr Asn Asn Ala Tyr Cys 
145                 150                 155                 160 


Val Thr Cys Asn Arg Ile Cys Pro Glu Pro Ala Ser Ser Glu Gln Tyr 
                165                 170                 175     


Leu Cys Gly Asn Asp Gly Val Thr Tyr Ser Ser Ala Cys His Leu Arg 
            180                 185                 190         


Lys Ala Thr Cys Leu Leu Gly Arg Ser Ile Gly Leu Ala Tyr Glu Gly 
        195                 200                 205             


Lys Cys Ile Lys Ala Lys Ser Cys Glu Asp Ile Gln Cys Thr Gly Gly 
    210                 215                 220                 


Lys Lys Cys Leu Trp Asp Phe Lys Val Gly Arg Gly Arg Cys Ser Leu 
225                 230                 235                 240 


Cys Asp Glu Leu Cys Pro Asp Ser Lys Ser Asp Glu Pro Val Cys Ala 
                245                 250                 255     


Ser Asp Asn Ala Thr Tyr Ala Ser Glu Cys Ala Met Lys Glu Ala Ala 
            260                 265                 270         


Cys Ser Ser Gly Val Leu Leu Glu Val Lys His Ser Gly Ser Cys Asn 
        275                 280                 285             


Ser Ile Ser Glu Asp Thr Glu Glu Glu Glu Glu Asp Glu Asp Gln Asp 
    290                 295                 300                 


Tyr Ser Phe Pro Ile Ser Ser Ile Leu Glu Trp 
305                 310                 315 


