ID A0A1S3WI58_ERIEU Unreviewed; 2270 AA.
AC A0A1S3WI58;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Fibronectin {ECO:0000256|ARBA:ARBA00020368};
GN Name=FN1 {ECO:0000313|RefSeq:XP_016045819.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016045819.1};
RN [1] {ECO:0000313|RefSeq:XP_016045819.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Secreted by contracting muscle, induces liver autophagy, a
CC degradative pathway for nutrient mobilization and damage removal, and
CC systemic insulin sensitization via hepatic ITGA5:ITGB1 integrin
CC receptor signaling. {ECO:0000256|ARBA:ARBA00035619}.
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DR RefSeq; XP_016045819.1; XM_016190333.1.
DR OrthoDB; 5399734at2759; -.
DR Proteomes; UP000079721; 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; 14.
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; 15.
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:SF8; FIBRONECTIN; 1.
DR PANTHER; PTHR46708; TENASCIN; 1.
DR Pfam; PF00039; fn1; 11.
DR Pfam; PF00040; fn2; 2.
DR Pfam; PF00041; fn3; 15.
DR PRINTS; PR00013; FNTYPEII.
DR SMART; SM00058; FN1; 12.
DR SMART; SM00059; FN2; 2.
DR SMART; SM00060; FN3; 15.
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; 5.
DR PROSITE; PS51091; FN1_2; 11.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 2.
DR PROSITE; PS50853; FN3; 15.
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 Oxidation {ECO:0000256|ARBA:ARBA00023097};
KW Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW Signal {ECO:0000256|SAM:SignalP};
KW Sulfation {ECO:0000256|ARBA:ARBA00022641}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..2270
FT /note="Fibronectin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010302908"
FT DOMAIN 50..90
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 95..138
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 139..182
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 184..228
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 229..273
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 355..403
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 415..463
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 468..510
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 515..557
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 558..601
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 609..704
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 721..811
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 812..901
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 908..999
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1000..1087
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1088..1174
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1175..1265
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1268..1360
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1361..1448
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1449..1542
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1543..1633
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1634..1726
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1727..1813
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1814..1907
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1988..2077
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2088..2132
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 2133..2175
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 2177..2217
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT REGION 697..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1943..1964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 360..386
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 374..401
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 420..446
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 434..461
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 2270 AA; 250217 MW; A6CBA2293DEDB31A CRC64;
MLRAPGPGLL LLAALCLGSA VPATGVSKSK RQAQQIVQPQ TPVAVSQSKL GCYDNGKHYQ
INQQWERTYL GNALVCTCYG GSRGFNCESK PEPEETCFDK YTGSTYRVGD TYERPKDHMI
WDCTCIGAGR GRISCTIANR CHEGGQSYKI GDTWRRPHET GGYMLECVCL GNGKGEWTCK
PIAEKCFDHA AGTSYVVGET WEKPYQGWMM VDCTCLGEGN GRITCTSRNR CNDQDTKTSY
RIGDTWSKKD NRGHLLQCIC TGNGRGEWKC ERHASLQTTS TGTGTITDVR TAIYQPQPQP
QPVPHGHCVT DSGVVYSVGM QWLKTQGNNQ MLCTCLGNGV SCQETATTQT YGGNSNGEPC
VLPFTYNGRT FYSCTTEGRQ DGRLWCSTTS NYEQDQKYSF CTDHTALVQT RGGNSNGALC
HFPFLYNNHN YTDCTSEGRR DNMKWCGTTW NYDADQKFGF CPMAAHEEVC TTDGVMYRIG
DQWDKQHDMG HMMKCTCVGN GRGEWTCVAY SQLRDQCIVD DITYNVNDTF HKRHEEGHML
NCTCFGQGRG RWKCDPIDQC QDSETRTFYQ IGDIWEKFVH GIRYRCYCYG RGIGEWHCQP
LQAYPGSTGP VQVIITETPS QPNSHPIHWN APEPSHISQY ILRWKPKNAR GGWKEATIPG
HLNSYTIKGL KPGMVYEGQL ISIQHYGQQE VTRFDFTTTS TSPPVTSNTV TGETTPLSPV
VSTSESVTEI TASSFVVSWV SASDTVSGFR VEYELSEEGD EPQYLDLPST ATSVSIPDLL
PGRKYIVNVY QISEEGEQSL ILSTSQTTAP DAPPDPAVDR VDDTSIVVRW NRPQAPITGY
RIVYSPSVEG SSTELNLPET ANSVTLSDLQ PGVQYNITIY AVEENQESTP VFIQQETTGV
PRSDKVPPPR DLQFVEVTDV KVTIMWTPPE SPVTGYRVDV IPVNLPGEHG QRLPVNRNAF
AEITGLTPGV TYHFKVFAVN QGRESEPLTA QQTTKLDAPT NLQFTGETDS TVTVIWTPPR
ARIAGYRLTV GLTRGGQPKQ YNVGPSARQY PLRNLQPGSE YTVSLVAVKG NQQSPKTTGV
FTTLQPVSSI PPYNTEVTET TIVITWTPAP RIGFKLGVRP SEGGEAPREV TSESGSIVVS
GLTPGVEYTY TVSVLRDGKE RDTPIVKKVV TPLSPPTNLQ LEANPDTGVL TVSWDRSTTP
DITGYRITTT PTNDQQGYTL EEVVHADQSS CTFENLSPGL EYNVSVYTVK DDKESVPISD
TIIPAVPPPT DLRFTNIGPD TMRVTWAPPP SIELTNLVVR YSPVKNEKDV AELSISPSDN
AVVLTNLLPG TEYLVNVSSV YEQHESIPLR GRQKTGLDAP TGIDFSDITA NSFTVHWIPP
RAPITGIKIR HHPEHAVGRP REDRVPPTRN SITLTNLNPG TEYVVTITGL NGKEESPLLV
GQQATVSDVP RELEVVAANP TSLMISWEPP AVTVRYYRIT YGETGGHSPV QEFTVPGSKS
TATISDLKPG VDYTITVYAV TGRGDSPASS KPISINYRTE IDKPSQMQVT DVQDNSISVR
WLPSSSPVTG YKVTTVPKNG PGPTKTKIAG PDQTEMTIEG LQPTVEYVVS VYAQDGNEES
QPLVQTAVTT IPAPTNLKFT QVTPTSLTAV WTAPNVQLTG YRVRVTPKEK TGPMKEINLS
PDSTSVVVSG LMVATKYEVS VYALKDTLTS RPAQGVITTL ENVSPPRRAR VTDATETTIT
ISWRTKTETI TGFQVDAIPA NGQTPVQRNI SPDIRSYTIT GLQPGTDYKI YLYTLNDNAR
SSPVVIDAST AIDAPSNLHF LATTPSSVLL SWQPPRARIT GYIIKYEKPG FPPREVFPRP
RPGVTEATIT GLEPGTEYTF QIIALKNNQK SEPLIGRRKT VQKTPFITNS GYDTGNGIQL
PGTTGQQPSV GQQMIFEEHG FRRTTPPTTV APVRHRPRPY PPNVNEEIQI GHVPRGDVDH
HLYPHLLGPN PNASTGQEAL SQTTISWAPL QESSEYIISC QPIGIDEEPL QFRVPGTSAS
ATLTGLTRGA TYNIIVEAVK DQQRHRVREE VVTVGNSVDQ GLQQPSDDSC FDPYTVSHYS
VGEEWERLSE SGFKLSCQCL GFGSGHFKCD SSKWCHDNGV NYKIGEKWDR QGENGQMMSC
TCLGNGKGEF KCDPHETTCY DDGKTYSVGE QWQKEYLGAI CSCTCFGGQR GWRCDNCRRP
GSEPGHDGSP DRTYNQYSQR YHQRTNTNVN CPIECFMPLD IQADREDSRE
//
