ID H0VMA2_CAVPO Unreviewed; 2478 AA.
AC H0VMA2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Fibronectin {ECO:0000256|ARBA:ARBA00020368};
GN Name=FN1 {ECO:0000313|Ensembl:ENSCPOP00000011528.2};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000011528.2, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000011528.2}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000011528.2};
RG Ensembl;
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 EMBL; AAKN02019661; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003474253.1; XM_003474205.3.
DR STRING; 10141.ENSCPOP00000011528; -.
DR Ensembl; ENSCPOT00000012933.3; ENSCPOP00000011528.2; ENSCPOG00000012808.4.
DR GeneID; 100732865; -.
DR KEGG; cpoc:100732865; -.
DR CTD; 2335; -.
DR VEuPathDB; HostDB:ENSCPOG00000012808; -.
DR eggNOG; ENOG502QPTS; Eukaryota.
DR GeneTree; ENSGT00940000155126; -.
DR HOGENOM; CLU_000916_0_0_1; -.
DR InParanoid; H0VMA2; -.
DR OMA; VHWLAPQ; -.
DR OrthoDB; 5399734at2759; -.
DR TreeFam; TF329915; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000012808; Expressed in liver and 12 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; IEA:Ensembl.
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; IEA:Ensembl.
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:0007044; P:cell-substrate junction assembly; IEA:Ensembl.
DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
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: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; 17.
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; 6.
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:UP000005447};
KW Signal {ECO:0000256|SAM:SignalP};
KW Sulfation {ECO:0000256|ARBA:ARBA00022641}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..2478
FT /note="Fibronectin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003543333"
FT DOMAIN 51..91
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 96..139
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 140..183
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 185..229
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 230..274
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 357..405
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 417..465
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 470..513
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 518..560
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 561..604
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 612..720
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 723..813
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 814..903
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 910..999
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1000..1089
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1090..1176
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1177..1271
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1272..1360
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1361..1453
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1454..1541
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1542..1635
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1636..1727
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1728..1815
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1816..1909
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1910..1996
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1997..2087
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2195..2285
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2296..2340
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 2341..2383
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 2385..2425
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT REGION 1663..1686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2151..2170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 362..388
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 376..403
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 422..448
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 436..463
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 2478 AA; 272563 MW; C551C0F4A9ABE4E4 CRC64;
MLRGPRPGLL LLLAALCLGT AVPPVGSSKS KRQTQQIVQP QSPVAVSQSK PGCYDNGKHY
QINQQWERTY LGNALVCTCY GGSRGFNCES KPEREETCFD KYTGNTYRVG DTYERPKDSM
IWDCTCIGAG RGRISCTIAN RCHEGDQSYK IGDTWRRPHE SGGYMLECVC LGNGKGEWTC
KPIAEKCFDH AAGTSYVVGE TWEKPYQGWM MVDCTCLGEG SGRITCTSRN RCNDQDTRTS
YRIGDTWSKK DNRGNLLQCI CTGNGRGEWK CERHASLQTT ATGSGGPFTD IRTAIYQPQP
HPQPAPYGHC VTDSGVVYSV GMQWLKTQGN KQMLCTCLGN GVSCQETAVT QTYGGNSNGE
PCVLPFTYNG RTFYSCTSEG RQDGHLWCST TSNYEQDKKY SFCTDHAVLV QTRGGNSNGA
LCHFPFLYNN HNYTDCTSEG RRDNMKWCGT TQNYDADQKF GFCPMAAHEE ICTTNEGVMY
RIGDQWDKQH DMGHMMRCTC VGNGRGEWTC VAYSQLRDQC IVDNITYNVN DTFHKRHEEG
HMLNCTCFGQ GRGRWKCDPI DQCQDSESRT FYQIGDSWEK YVHGVRYQCY CYGRGIGEWH
CQPLQTYAGS SGPVQVIITE TPSQPNSHPI QWNAPEPSHI TQYVLRWRPK TSTGRWKDAT
IPGHLNSYTI KGLTPGVVYE GQLISYQQYG HREVTRFDFT TSASTPVTSN TVTGESTVPP
PVVATSESVT EITASSFVVS WVSASDTVSG FRVEYELSEE GDEPQYLDLP STATSVNIPD
LLPGRKYIVN VYQISEEGKQ SLILSTSQTT APDAPPNPTV DRVDDTSIVV SWSRPQAPIT
GYRIVYSPSV EGSSTELNLP ETADSVTLSD LQPGIQYNIT IYAVEENQES APIFIQQETT
GVPRSDKVPP PRDLQFVEVT DVKVTIMWTP PDSAVTGYRV EVLPVNLPGE HGQRLPVNRN
TFAEVTGLSP GVTYFFKVFA VNHGRESKPL TAQQTTKLDA PTNLQFTNET DTSVLVVWTP
PRAQVTGYRL TVGLTRGDQP KQYSVGPSAS RYPLRNLQPG SEYTVSLVAV KGNQQSPKVT
GVFTTLQPGT SIPFYNTEVT ETTIVITWTP VPRIGFKLGV RPSQGGEAPR EVTSDSGSIV
VSGLTPGVEY VYSIQVLRDG QERDAPIVNT VVTPLSPPTN LHLETNPDTG VLTVSWERST
TPDITGYRIT TTPTNGQQGY SLEEVVHADQ SSCTFENLSP GVEYNVSVYT VKDNKESVPV
SDTIIPEVPQ LTDLSFVDIT DSSIGLRWTP LNSSTIIGYR ITVVAAGEGI PIFEDFVDSS
VGYYTVTGLE PGIDYDISVI TLINGGESAP TTLTQQTAVP PPTDLRFTNI GPDTMRVTWA
PPPSIELTNF LLRYSPVKNE EDVAELSISP SDNAVVLTNL LPGTDYLVSV SSVYEQHESI
PLRGRQKTGL DSPTGIDFSD ITANSFTVHW IAPRATITGY RIRHHPEHLS GRPREDRVPP
SRNSITLTNL LPGTEYVVSI VAVNGREESP ILIGQQSTIS DVPRDLEVVA STPNSVMIKW
DAPGVTVRYY RITYGETGGN SPVQEFTVPG TKNTATISNL KPGADYTITL YAVTGRGDSP
ASSKPVSIDY RTEIDKPSQM QVTDVQDNSI SVRWLPSKSP VTGYRVTTTP KNGVGPSKTK
NAGPDQTEMT IEGLQPTVEY VVSVYAQNQN GESQPLVKTA VTNIDRPKGL AFTDVDVDSI
KIAWESPQGQ VTRYRVTYSS PEDGIHELFP APDGEEDTAE LQGLRPGSEY TVSVVALHGD
MESKPLIGTQ CTAIPAPTDL RFTQVTPTSL SAEWTAPNVR LTGYRVRVTP KEKTGPMKEI
NLSPDSSSVV VSGLMVATKY EVSVYALKDT LTSRPAQGVV TTLENVSPPR RARVTDATET
TITISWRTKT ETITGFQVDA VPASGQTPVQ RTISPDVRSY TITGLQPGTD YKIYLYTLNS
NARSSPVVID ASTAIDAPSN LRFLTTTPNS LLVSWQPPRA RITGYIIKYE KPGSTPREVL
PRPRPGVTEA TITGLEPGTE YIIYVIALKN NQKSEPLIGR KKTDELPQLV TLPHPNHHGP
EILDVPSTVH QTPFVTNPGY ATGNGIQLPG TSLQQPSVGQ QMIFEEHGFR RTTPPTAATP
VRHRPRPYPP NVDEEIQIGH VPRGDVDHHL YPHVLGLNPN ASTGQEALSQ TTISWTPFQE
SSEYIISCHP VGVDEDLLQF RVPGTSTSAT LTGLTRGATY NIIVEALKDQ KRHKVQEEVV
TVGNSVNEGL NQPTDDSCFD PYTVSHYAIG DEWERLSESG FKLTCQCLGF GSGHFRCDSS
KWCHDNGVNY KIGEKWDRQG ENGQMMSCTC LGNGKGEFKC DPHEATCYDD GKMYHVGEQW
QKEYLGAICT CSCFGGQRGW RCDTCRRPGA EPGPEGSAGH AYGPYTQRYH QRTNTNVNCP
IECFMPLDVQ ADREDSRE
//
