ID M3WB06_FELCA Unreviewed; 2475 AA.
AC M3WB06;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Fibronectin {ECO:0000256|ARBA:ARBA00020368};
GN Name=FN1 {ECO:0000313|Ensembl:ENSFCAP00000008544.3,
GN ECO:0000313|VGNC:VGNC:62314};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000008544.3, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000008544.3, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000008544.3,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000008544.3, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000008544.3,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000008544.3}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000008544.3};
RG Ensembl;
RL Submitted (SEP-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 EMBL; AANG04002752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003991167.1; XM_003991118.4.
DR STRING; 9685.ENSFCAP00000008544; -.
DR PaxDb; 9685-ENSFCAP00000008544; -.
DR Ensembl; ENSFCAT00000009220.6; ENSFCAP00000008544.3; ENSFCAG00000009217.6.
DR GeneID; 101081746; -.
DR KEGG; fca:101081746; -.
DR CTD; 2335; -.
DR VGNC; VGNC:62314; FN1.
DR eggNOG; ENOG502QPTS; Eukaryota.
DR GeneTree; ENSGT00940000155126; -.
DR HOGENOM; CLU_000916_0_0_1; -.
DR InParanoid; M3WB06; -.
DR OMA; VHWLAPQ; -.
DR OrthoDB; 5399734at2759; -.
DR Proteomes; UP000011712; Chromosome C1.
DR Bgee; ENSFCAG00000009217; Expressed in liver and 9 other cell types or tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0005577; C:fibrinogen complex; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0016504; F:peptidase activator activity; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0043394; F:proteoglycan binding; IBA:GO_Central.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0051702; P:biological process involved in interaction with symbiont; IEA:Ensembl.
DR GO; GO:0007161; P:calcium-independent cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0007044; P:cell-substrate junction assembly; IBA:GO_Central.
DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0033622; P:integrin activation; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0150102; P:negative regulation of monocyte activation; IEA:Ensembl.
DR GO; GO:0071635; P:negative regulation of transforming growth factor beta production; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:1901166; P:neural crest cell migration involved in autonomic nervous system development; IEA:Ensembl.
DR GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:1904237; P:positive regulation of substrate-dependent cell migration, cell attachment to substrate; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
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:UP000011712};
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..2475
FT /note="Fibronectin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004042368"
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..703
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..1000
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1001..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 2193..2287
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2294..2338
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 2339..2381
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 2383..2423
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT REGION 24..48
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 2148..2169
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 2475 AA; 272035 MW; EA49D1AFC2AD4C18 CRC64;
MLRGPGPRLL LLAVLSLGTA VPSTGASKSK RQAQQIIQPQ TPVAVSQSKP GCYDNGKHYQ
INQQWERTYL GNALVCTCYG GSRGFNCESK PEPEETCFDK YTGNTYRVGD TYERPKDSMI
WDCTCIGAGR GRISCTIANR CHEGGQSYKI GDTWRRPHET GGYMLECVCL GNGKGEWTCK
PIAEKCFDHA AGTSYVVGET WEKPYQGWMM VDCTCLGEGS GRITCTSRNR CNDQDTRTSY
RIGDTWSKKD NRGNLLQCIC TGNGRGEWKC ERHAALQTTS AGSGSFTDVR TAIYQPQPHP
QPAPYGHCVT DSGVVYSVGM QWLKTQGNKQ MLCTCLGNGV SCQETAVTQT YGGNSNGEPC
VLPFTYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF CTDHTVLVQT RGGNSNGALC
HFPFLYNNHN YTDCTSEGRR DNMKWCGTTE NYDADQKFGF CPMAAHEEIC TTNEGVMYRI
GDQWDKQHDM GHMMRCTCVG NGRGEWTCVA YSQLRDQCIV DDITYNVNDT FHKRHEEGHM
LNCTCFGQGR GRWKCDPVDQ CQDSETRTFY QIGDSWEKYV HGVRYQCYCY GRGIGEWHCQ
PLQTYPGTTG PVQVIITETP SQPNSHPIQW NAPEPSHISK YILRWKPKNS PRGWKEATIP
GHLNSYTIKG LTPGVVYEGQ LISVQHYGHR EVTRFDFTTT STSTAVTSNT VTGETTPLSP
VVATSESVTE ITASSFVVSW VSASDTVSGF RVEYELSEEG DEPQYLDLPS TATSVSIPDL
LPGRKYIVNV YQISEEGEQS LILSTSQTTA PDAPPDPAVD RVDDTSIVVR WSRPQAPITG
YRIVYSPSVE GSSTELNLPE TANSVTLSDL QPGVQYNITI YAVEENQEST PVFIQQETTG
VPRSDKVPPP KDLQFVEVTD VKITIMWTPP QSPVTGYRVD VIPVNLPGEH GQRLPISRNT
FAEVTGLSPG VTYHFKVFAV NQGRESKPLT AEQTTKLDAP TNLRFTNETD STVIVTWTPP
RARIAGYRLT VALTRGGQPK QYNIGPSASQ YPLRNLQPAS EYTATLMAVK GNQQSPKATG
VFTTRQPLGS VPPYNTEVTE TTIVITWTPA PRIGFKLGVR PSQGGEAPRE VTSESGSIVV
SGLTPGVEYI YTISVLRDGQ ERDTPIVKKV VTPLSPPTNL HLEANPDTGV LTVSWERSTT
PDITGYRITT TPTNGQQGYS LEEVVHADQS SCTFENLSPG LEYNVSVYTV KDDKESAPIS
DTIIPEVPQL TDLSFVDITD SSIGLRWTPL NSSTIIGYRI TVVAAGEGIP IFEDFVDSSV
GYYTVTGLEP GIDYDISVIT LINGGESAPT TLTQQTAVPP PTDLRFTNIG PDTMRVTWAP
PPSIELTNLL VRYSPVKNEE DVAELSISPS DNAVVLTNLL PGTEYLVSVS SVYEQHESTP
LRGRQKTGLD SPTGIDFSDI TAHSFTVHWI APRATITGYR IRHHPEHTGG RPREDRVPPS
RNSITLTNLT PGTEYVVSIV ALNGREESPP LIGQQSTVSD VPRDLEVIAA TPTSLLISWD
APAVTVRYYR ITYGETGGNS PVQEFTVPGS KSTATISGLK PGADYTITVY AVTGRGDSPA
SSKPISIDYR TEIDKPAQMQ VTDVQENSIS VRWLPSSSPV TGYRVTTTPK NGPGPSKTKT
AGPDQTEMTI EGLQPTVEYV VSVYAQNRNG ESQPLVQTAV TNIDRPKGLA FTDVDVDSIK
IAWESPQGQV SRYRVTYSNP EDGIHELFPA PDGEEDTAEL QGLRPGSEYT VSVVALHDDM
ESQPLIGTQS TAIPAPTDLK FTQVTPTSLT AQWTAPNVQL TGYRVRVTPK EKTGPMKEIN
LAPDSSSVVV SGLMVATKYE VSVYALKDSL TSRPAQGVVT TLENVSPPRR ARVTDATETT
ITISWRTKTE TITGFQVDAI PANGQTPIQR TIKPDVRSYT ITGLQPGMDY KIYLYTLNDN
ARSSPVVIDA STAIDAPSNL RFLATTPNSL LVSWQPPRAR ITGYIIKYEK PGSPPREVVP
RPRPGVTEAT ITGLEPGTEY TIQVIALKNN QKSEPLIGRK KTDELPQLVT LPHPNLHGPE
ILDVPSTVQK TPFINPGYDT GNGIQLPGTS GQQPSVGQQM IFEEHGFRRT TPPTTATPVR
HRPRPYPPNV NEEIQVGHVP RGDVDHHLYP HVLGLNPNAS TGQEALSQTT ISWTPFQESS
EYIISCHPVG IDEEPLQFRV PGTSASATLT GLTRGATYNI IVEALKDHKR HKVREEVVTV
GNSVDQGLNQ PTGDSCFDPY TVSHHAVGEE WERLSESGFK LSCQCLGFGS GHFRCDSSKW
CHDNGVNYKI GEKWDRQGEN GQMMSCTCLG NGKGEFKCDP HEATCYDDGK TYHVGEQWQK
EYLGAICSCT CFGGQRGWRC DNCRRPGAEP GHEGSTGHYN QYSQRYHQRT NTNVNCPIEC
FMPLDVQADR EDSRE
//
