ID A0A2U3W013_ODORO Unreviewed; 2476 AA.
AC A0A2U3W013;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Fibronectin {ECO:0000256|ARBA:ARBA00020368};
GN Name=FN1 {ECO:0000313|RefSeq:XP_004401268.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004401268.1};
RN [1] {ECO:0000313|RefSeq:XP_004401268.1}
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_004401268.1; XM_004401211.1.
DR STRING; 9708.A0A2U3W013; -.
DR GeneID; 101365197; -.
DR KEGG; oro:101365197; -.
DR CTD; 2335; -.
DR InParanoid; A0A2U3W013; -.
DR OrthoDB; 5399734at2759; -.
DR Proteomes; UP000245340; 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; 12.
DR CDD; cd00062; FN2; 2.
DR CDD; cd00063; FN3; 16.
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; 17.
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; 17.
DR PRINTS; PR00013; FNTYPEII.
DR SMART; SM00058; FN1; 12.
DR SMART; SM00059; FN2; 2.
DR SMART; SM00060; FN3; 17.
DR SUPFAM; SSF49265; Fibronectin type III; 11.
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; 17.
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:UP000245340};
KW Signal {ECO:0000256|SAM:SignalP};
KW Sulfation {ECO:0000256|ARBA:ARBA00022641}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..2476
FT /note="Fibronectin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015532954"
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..511
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 516..558
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 559..602
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 610..705
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 717..812
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 813..902
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 909..998
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 999..1088
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1089..1175
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1176..1270
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1271..1359
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1360..1452
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1453..1540
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1541..1634
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1635..1726
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1727..1814
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1815..1908
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1909..1995
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1996..2086
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2194..2284
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2295..2339
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 2340..2382
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 2384..2424
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT REGION 24..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1483..1507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1660..1685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2149..2170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1483..1498
FT /note="Basic and acidic residues"
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 2476 AA; 272437 MW; 7E8BBF2B89AD775E CRC64;
MLRGPGPRLL LLAVLSLGTA VPSTGASKSK RQAQQIVQPQ TPVAVSQTKP GCYDNGKHYQ
INQQWERTYL GNALVCTCYG GSRGFNCESK PEPEETCFDK YTGNTYRVGD TYERPKDSMI
WDCTCIGAGR GRISCTIANR CHEGGQSYKI GDTWRRPHET GGYMLECVCL GNGKGEWTCK
PIAEKCFDHS AGTSYVVGET WEKPYQGWMM VDCTCLGEGS GRITCTSRNR CNDQDTRTSY
RIGDTWSKKD NRGNLLQCLC TGNGRGEWKC ERHASLQTTS TGSGPFTDVR TAIYQPQPQP
QPAPYGHCVT DSGVVYSVGM QWLKTQGNKQ MLCTCLGNGV SCQETAVTQT YGGNSNGEPC
VLPFTYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF CTDHTVLVQT RGGNSNGALC
HFPFLYNNHN YTDCTSEGRR DNMKWCGTTP NYDADQKFGF CPMAAHEEIC TTNEGVMYRI
GDQWDKQHDM GHMMRCTCIG NGRGEWTCVA YSQLRDQCIV DDITYNVNDT FHKRHEEGHM
LNCTCFGQGR GRWKCDPIDQ CQDSETRTFY QIGDSWEKYV HGVRYQCYCY GRGIGEWHCQ
PLQTYPGTTG PVQVIITETP SQPNSHPIQW NAPEPSHISK YILRWKPKNS PGRWKEATIP
GHLNSYTIKG LTPGVVYEGQ LISVQQYGHR EVTRFDFTTT STSPAVTSNT VTGETTPLSP
VVATSESVTE ITASSFVVSW VSASDTVSGF RVEYELSEEG DEPQYLDLPS TATSVNIPDL
LPGRKYIVNV YQISEEGEQS LILSTSQTTA PDAPPDPAVD RVDDTSIVVR WSRPQAPITG
YRIVYSPSVE GSSTELNLPE TANSVTLSDL QPGVQYNITI YAVEENQEST PVFIQQETTG
VPRSDEVPPP RDLQFVEVTD VKVTIMWTPP ESAVTGYRVD VIPVNLPGEH GQRLPISRNT
FAEVTGLSPG VTYHFKIFAV NQGRESKPLM AEQMTRLDAP TNLQFTNETD STVLVIWTPP
RARIAGYRLT VGPTRGGQPK HYNVGPSATR YPLRNLQPAS EYTASLVAVK GNQQSPKATG
VFTTLQPLSS IPPYNTEVTE TTIVITWTPA PRIGFKLGVR PSQGGEAPRE VTSESGSIVV
SGLTPGVEYI YTISVLRDGQ ERDTPIVKKV VTPLSPPTNL HLEANPDTGV LTVSWERSTT
PDITGYRITT TPLNGQQGYS LEEVVHADQS SCTFENLSPG LEYNVSVYTV KDDKESVPIS
DTIIPEVPQL TDLSFVDITD SSIGLRWTPL NSSTIIGYRI TVVAAGEGIP IFEDFVDSSV
GYYTVTGLEP GIDYDISVIT LINGGESAPT TLTQQTAVPP PTDLRFTNVG PDTMRVTWAP
PPSIELTNFL VRYSPVKNEE DVAELSISPS DNAVVLTNLL PGTEYLVSVS SVYEQHESMP
LRGRQKTGLD SPSGIDFSDI TTNSFTVHWI APRATITGYR IRHHPEHTGG RPREDRVPPS
RNSITLTNLN PGTEYVVSIV ALNGREESPP LIGQQSTVSD VPRDLEVIAA TPTSVLISWD
APAVTVRYYR ITYGETGGNS PVQEFTVPGS KSTATISGLK PGADYTITVY AVTGRGDSPA
SSKPISIDYR TEIDKPSQMQ VTDVQDNSIS VRWLPSSSPV TGYRVTTTPK NGSGPSKTKT
AGPDQTEMTI EGLQPTVEYV VSVYAQNRNG ESQPLVQTAV TNIDRPKGLA FTDVDVDSIK
IAWESPQGQV SRYRVTYSSP EDGIRELFPA PDGEEDTAEL QGLRPGSEYT VSVVALHDDM
ESQPLIGTQS TAIPAPADLK FTQVTPTSLT AQWTAPNVQL TGYRVRVTPK EKTGPMKEIN
LAPDSSSVVV SGLMVATKYE VSVYALKDTL TSRPAQGIVT TLENVSPPRR ARVTDATETT
ITISWRTKTE TITGFQVDAI PANGQTPIQR TIRPDVRSYT ITGLQPGTDY KIYLYTLNDN
ARSSPVVIDA STAIDAPSNL RFLATTPNSL LVSWQPPRAK ITGYIIKYEK PGSPPREVVP
RPRPGVTEAT ITGLEPGIEY TIQVIALKNN QKSEPLIGRK KTDELPQLVT LPHPNLHGPE
ILDVPSTVQK TPFITNPGYD TGNGIQLPGT SGQQPSVGQQ MIFEEHGFRR TTPPTTATPV
RHRPRPYPPN VNEEIQVGHV PRGDVDHHLY PHVMGLNPNA STGQEALSQT TISWTPFQES
SEYIISCHPV DTDEEPLQFR VPGTSASATL TGLTRGATYN IIVEALKDQK RHKVREEVIT
VGNSVDQGLN QPTDDSCFDP YTVSHYAVGE EWERLSESGF KLSCQCLGFG SGHFRCDSSK
WCHDNGVNYK IGEKWDRQGE NGQMMSCTCL GNGKGEFKCD PHEATCYDDG KTYHVGEQWQ
KEYLGAICSC TCFGGQQGWR CDNCRRPGAE PGQEGSTGHY NQYSRRYHQR TNTNVNCPIE
CFMPIDVQAD REDSRE
//
