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Database: UniProt
Entry: E9FSS4_DAPPU
LinkDB: E9FSS4_DAPPU
Original site: E9FSS4_DAPPU 
ID   E9FSS4_DAPPU            Unreviewed;       381 AA.
AC   E9FSS4;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=Follistatin-related protein 1 {ECO:0000256|ARBA:ARBA00019697};
DE   AltName: Full=Follistatin-like protein 1 {ECO:0000256|ARBA:ARBA00042478};
GN   ORFNames=DAPPUDRAFT_303124 {ECO:0000313|EMBL:EFX89772.1};
OS   Daphnia pulex (Water flea).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX89772.1, ECO:0000313|Proteomes:UP000000305};
RN   [1] {ECO:0000313|EMBL:EFX89772.1, ECO:0000313|Proteomes:UP000000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21292972; DOI=10.1126/science.1197761;
RA   Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA   Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA   Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA   Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA   Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA   Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA   Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA   Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA   Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA   Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA   Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA   Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT   "The ecoresponsive genome of Daphnia pulex.";
RL   Science 331:555-561(2011).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR   EMBL; GL732524; EFX89772.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9FSS4; -.
DR   STRING; 6669.E9FSS4; -.
DR   EnsemblMetazoa; EFX89772; EFX89772; DAPPUDRAFT_303124.
DR   KEGG; dpx:DAPPUDRAFT_303124; -.
DR   eggNOG; ENOG502QQAG; Eukaryota.
DR   HOGENOM; CLU_726195_0_0_1; -.
DR   InParanoid; E9FSS4; -.
DR   OMA; CIERCKP; -.
DR   PhylomeDB; E9FSS4; -.
DR   Proteomes; UP000000305; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0030510; P:regulation of BMP signaling pathway; IBA:GO_Central.
DR   Gene3D; 3.30.60.30; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036058; Kazal_dom_sf.
DR   PANTHER; PTHR10913; FOLLISTATIN-RELATED; 1.
DR   PANTHER; PTHR10913:SF13; FOLLISTATIN-RELATED PROTEIN 1; 1.
DR   Pfam; PF07648; Kazal_2; 1.
DR   SMART; SM00280; KAZAL; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF57603; FnI-like domain; 1.
DR   SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
PE   4: Predicted;
KW   Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000305};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..381
FT                   /note="Follistatin-related protein 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003236345"
FT   DOMAIN          52..106
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51465"
FT   DOMAIN          207..242
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          290..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..309
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..336
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..365
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   381 AA;  43412 MW;  96D4DA077F97F1F1 CRC64;
     MLRILGLVSL FCILFQAALA SNSEENALDM SLVEDECSMM VCRAGRECKV GADGEAACAC
     LATCPDHFVP VCGSNNQSYD NFCLMHRDAC LTGVHISLKK KGYCSNKSIK KKSSKKDKLK
     DENHFEPVVC FQWERDALRR QIINYFRHHT ADQSWYRPDL KSYEKQFARF FMCDTTKDNF
     VDANELAACV TEVPFALRTT AATNELVKVL CVDAIIDSAD TNSDWRLDFE EYKTLMDSSF
     QPKEKLCSLE GKKYEDGSQT KVDCNDCVCA CGSWVCSSKK CDEELNEIDD LDEDEDLDDE
     LDEAEDQSED NTKDEVKILK IEEDIDLKID DPDEDQPPKI NSDDDDDMDD EEDEEDDEEE
     DEEIDVEPIK KSSKNKKKKL T
//
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