ID A0A3B5BD83_9TELE Unreviewed; 2313 AA.
AC A0A3B5BD83;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Fibronectin {ECO:0000256|ARBA:ARBA00020368};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000030921.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000030921.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR Ensembl; ENSSPAT00000031418.1; ENSSPAP00000030921.1; ENSSPAG00000022384.1.
DR GeneTree; ENSGT00940000155126; -.
DR Proteomes; UP000261400; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd00061; FN1; 11.
DR CDD; cd00062; FN2; 2.
DR CDD; cd00063; FN3; 12.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 12.
DR Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 14.
DR InterPro; IPR000083; Fibronectin_type1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013806; Kringle-like.
DR PANTHER; PTHR46708:SF2; FIBRONECTIN TYPE-III DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46708; TENASCIN; 1.
DR Pfam; PF00039; fn1; 10.
DR Pfam; PF00040; fn2; 2.
DR Pfam; PF00041; fn3; 13.
DR PRINTS; PR00013; FNTYPEII.
DR SMART; SM00058; FN1; 12.
DR SMART; SM00059; FN2; 2.
DR SMART; SM00060; FN3; 14.
DR SUPFAM; SSF49265; Fibronectin type III; 9.
DR SUPFAM; SSF57603; FnI-like domain; 12.
DR SUPFAM; SSF57440; Kringle-like; 2.
DR PROSITE; PS01253; FN1_1; 4.
DR PROSITE; PS51091; FN1_2; 10.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 2.
DR PROSITE; PS50853; FN3; 13.
PE 4: Predicted;
KW Acute phase {ECO:0000256|ARBA:ARBA00022486};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00479}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heparin-binding {ECO:0000256|ARBA:ARBA00022674};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..2313
FT /note="Fibronectin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017281222"
FT DOMAIN 88..131
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 132..175
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 177..221
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 222..266
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 351..399
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 411..459
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 464..508
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 513..555
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 556..599
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 607..700
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 713..796
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 798..890
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 897..986
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 987..1074
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1131..1225
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1283..1371
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1372..1462
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1468..1559
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1560..1649
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1658..1758
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1760..1852
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1855..1946
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2142..2186
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 2187..2229
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 2231..2271
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DISULFID 356..382
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 370..397
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 416..442
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 430..457
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 2313 AA; 253311 MW; 95009C4790C1DD09 CRC64;
MSGSTVARVL VALCIGSAVN CMPKDAHRNR RQAQQHHVSS VDALYGCIEN GNFYGVNDQW
ERPFLGSTLI CTCHGVAGIK CKSKPEEERC YDKINQQYYA VGDTYERPKD GMIWDCTCIG
SGRGKISCTI ANRCHEGGAS YKIGDTWRRP HETGGYMLEC VCLGNGKGEW TCKPVAERCY
DNSAGTSYVV GETWEKPYQG WMVVDCTCLG EGSGRITCTS RNRCNDQDTL SSYRIGDTWT
KTDARGHLLQ CLCTGNGRGE WKCERHASLH TTGLGTGSRV ITNIQPAVYQ PATVPEIAQE
GPCRTDTGLS YFIGQRWIKN QGAKQMICTC LGNGVSCDQW DGPAPVYGGN SGGLPCVFPF
VYKGKTYHSC TSDGRSDGQL WCSTSSDFET DQKYSFCTEK NVMVTTRGGN SNGALCQFPF
VYNGRNYTDC TADGRRDGMK WCGTTTDYDT EHRFGFCPMA AHEEVCTTSE GVMYRVGDQW
DKRHDVLGHM MRCTCVGNGR GEWSCVAYSQ LKDQCSVDGL TYDVNQTFTK QHDEGYMMNC
TCFGQGRGRW KCDAIDQCQE PETRAFYQIG ESWDKVIHGI MYKCRCYGNG VGELSCEPQQ
SYPGGHRPVQ VIITESGNQP NSHPIQWNAP PSAHITQYIL KWKVKNTHSP WREVMIPGHL
NSYTISGLKP GITYEGQLIS VLRFGRREVT RFDFTTTYGS LATSQGETTM PPPVVDISES
VTEITSSSFV VSWVSASDTV SGFRVEYELS EQGQDLPRTA TSVNINELLP GRKYTVNVYE
VTDGGEDNLI LTTSQTTAPD APKEHEVEEV GETSIVISWE KPLAPITGYR VVYTPSVEGE
STELTLPDTA TSVTLSDLRP GKMYNISIYA VEESLESEPI FVQVNTSGDP LPEEVASPTD
LQFFEVSDKK IVLTWSGPAG DVSGYRVTVV PVDESGSPQR EMPVSQNSYI EVTHLQPGTM
YRFSVYSIHN GEESLPLIGE QTTKPDAPTD IHFANVTEDS AVMMWYAPRA KITGYRLFLT
VEGSNPKQLR LPARLTEYTL LNLKPDTEYM ATLHAEQDNT LSEGETAVFT TSEFRPSQGG
EAPRDVTSDS GSIYVSGLTP GVEYTYSVQP VINGQEQGTP ITRRVVTPLS PPTDLNLESN
PGTGELTVQW NGASAPDITG YRVTCSPTNG QQGNSVEEFV EAGQNSCTLE NLSPGVEYNV
SVVTVKDDME STPVSTVITP AVPAPTNLGF GQVGPDTMEV TWVSTCKHRN DYDITETSVG
GRTNNVDFLP SFSVSHPSVA LDSPVDLRFS EILTNSFTIH WLAPQSKITG YRIRYQMVSG
GRFKDERLPP SRSHFTLTGL TPDTEYLVNI FAVSGTQESQ PLGGKQKTIS DAPTDLEVLD
SNPTSITVRW TAPPVTVRYY RITHGESGGH SNPKEFTVPG SQSTATINNL KPGTDYTVTV
YAVTGRGDSP ASSIPIYVTH KTGTGVDSPS GMEVTEVNDN SVTVRWSPAQ GPIKGYRVTG
VPKNGQGPSF TEVVAPDQTE ITFSGLMPTV EYTLSVSALG QDGESSPLVV NAVTNVDRPK
DLTFSDIDST SLRINWDSPE GIVTSYRVMY SSSEEGEREL RPAPRGDAES TVIYGLQPGT
EYTVKVIALH DGTSSTPLVG TQATEIGDTN TSTEAISSPT NLQFSQVSPT SFTMRWAVPG
QENRLNGLTG LTGYRVVVNP KNKSGPTKEI NLAPDTTQAH ISGLMVSIAT TYEVHVYALK
NSLTSRPVQG EVTTLENISP PRRVRISDVN DSSITLTWRS KTETISGFLV EATPTSASSG
YVPIQKTIGP DSRSFTITGL EPGTSYKINV YTLKGNGRSV PLTLTATTAQ PLVLPPTNIR
FTSLNPNSIS FMWEPSRSPR VTGYYVTYEE AGGLPREVIP RPHAGQSYSN IDGLKPGTEY
VIKIVALQNA LRSTPLVGKA RTRKYNHHWL LLVNFDSNYV HLAGTSGQNQ PGQQGQHIYT
EFQSLGPNNG LHGPYSGPKE GQRPTLREPL VYIPVPGPDG NRIPLVKVSD GPLPGLAFGF
PDNETEFPQE AQTITTISWQ PIPQTSEYEV SCNPITHLEE QGFQMRLPGT SNSATLIGLT
SGASYNVIVE AMTGGAKEKV LEEVVTVGNA VPGDIPLTSN RDVCYDTFTQ TYHEVGSEWE
RMSETGFKLW CRCLGLGSGH FRCDSSKWCH DNGNNYRIGE KWDRHAENGH MMSCTCLGNG
KGEFKCEPHE STCYDDGKMY QVGNQWQKEY LGAICTCTCY GGQQGWRCEN CRRPGGQTDV
DADLLQPVHT DNIQCPIECL RPELLADAQS PSE
//
