ID W5QDG8_SHEEP Unreviewed; 2478 AA.
AC W5QDG8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Fibronectin {ECO:0000256|ARBA:ARBA00020368};
GN Name=FN1 {ECO:0000313|Ensembl:ENSOARP00000020766.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000020766.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000020766.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000020766.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000020766.1}
RP IDENTIFICATION.
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; AMGL01055878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004004956.1; XM_004004907.3.
DR Ensembl; ENSOART00000021052.1; ENSOARP00000020766.1; ENSOARG00000019329.1.
DR GeneID; 100216462; -.
DR CTD; 2335; -.
DR HOGENOM; CLU_000916_0_0_1; -.
DR OrthoDB; 5399734at2759; -.
DR Proteomes; UP000002356; Chromosome 2.
DR Bgee; ENSOARG00000019329; Expressed in mitral valve and 54 other cell types or tissues.
DR ExpressionAtlas; W5QDG8; baseline.
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:UP000002356};
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_5004870182"
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 356..404
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 416..464
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 469..512
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 517..559
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 560..603
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 611..706
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..1001
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1002..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..1452
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1453..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..2289
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 1485..1504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1666..1685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2150..2170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1485..1499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 361..387
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 375..402
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 421..447
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 435..462
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 2478 AA; 272105 MW; 73AD53D397E4768B CRC64;
MLGGPGPGLL LLLAVLSLGT AVPSAGASKS RRQAQQIVQP QSPLTVSQSK PGCYDNGKHY
QINQQWERTY LGSALVCTCY GGSRGFNCES KPEPEETCFD KYTGNTYRVG DTYERPKDSM
IWDCTCIGAG RGRISCTIAN RCHEGGQSYK IGDTWRRPHE TGGYMLECVC LGNGKGEWTC
KPIAEKCFDQ AAGTSYVVGE TWEKPYQGWM MVDCTCLGEG SGRITCTSRN RCNDQDTRTS
YRIGDTWSKK DNRGNLLQCI CTGNGRGEWK CERHTSLQTT SAGSGSFTDI RPAIYQPQPH
PQPPPYGHCV TDSGVVYSVG MQWLKTQGNK QMLCTCLGNG VSCQETAITQ TYGGNSNGEP
CVLPFTYNGR TFYSCTTEGR QDGHLWCSTT SNYEQDQKYS FCTDHTVLVQ TRGGNSNGAL
CHFPFLYNNR NYTDCTSEGR RDNMKWCGTT QNYDADQKFG FCPMAAHEEI CTTNEGVMYR
IGDQWDKQHD MGHMMRCTCV GNGRGEWTCV AYSQLRDQCI VDGITYNVND TFHKRHEEGH
MLNCTCFGQG RGRWKCDPVD QCQDSETRTF YQIGDSWEKY LQGVRYQCYC YGRGIGEWAC
QPLQTYPDAS GPVQVIITET PSQPNSHPIQ WNAPESSHIS KYILRWKPKN SPNRWKEATI
PGHLNSYTIK GLRPGVVYEG QLISVQHYGQ REVTRFDFTT TSTSPAVTSN TVTGETTPLT
PVVATSESVT EITASSFVVS WVSASDTVSG FRVEYELSEE GDEPQYLDLP STATSVNIPD
LLPGRKYTVN VYEISEEGEQ NLILSTSQTT APDAPPDPTV DQVDDTSIVV RWSRPRAPIT
GYRIVYSPSV EGSSTELNLP ETANSVTLSD LQPGVQYNIT IYAVEENQES TPVFIQQETT
GVPRSDKVPP PRDLQFVEVT DVKITIMWTP PESPVTGYRV DVIPVNLPGE HGQRLPVSRN
TFAEVTGLSP GVTYHFKVFA VNQGRESKPL TAQQATKLDA PTNLQFINET DTTVIVTWTP
PRARIVGYRL TVGLTRGGQP KQYNVGPAAS QYPLRNLQPG SEYAVSLVAV KGNQQSPRVT
GVFTTLQPLG SIPPYNTEVT ETTIVITWTP APRIGFKLGV RPSQGGEAPR EVTSESGSIV
VSGLTPGVEY VYTISVLRDG QERDAPIVKK VVTPLSPPTN LHLEANPDTG VLTVSWERST
TPDITGYRIT TTPTNGQQGY SLEEVVHADQ SSCTFENLSP GLEYNVSVYT VKDDKESVPI
SDTIIPEVPQ LTDLSFVDIT DSSIGLRWTP LNSSTIIGYR ITVVAAGEGI PIFEDFVDSS
VGYYTVTGLE PGIDYDISVI TLINGGESAP TTLTQQTAVP PPTDLRFTNV GPDTMRVTWA
PPSSIELTNL LVRYSPVKNE EDVAELSISP SDNAVVLTNL LPGTEYLVSV SSVYEQHESI
PLRGRQKTAL DSPSGIDFSD ITANSFTVHW IAPRATITGY RIRHHPEHMG GRPREDRVPP
SRNSITLTNL NPGTEYVVSI VALNSKEESQ PLVGQQSTVS DVPRDLEVIA ATPTSLLISW
DAPAVTVRYY RITYGETGGS SPVQDFTVPG SKSTATISGL KPGVDYTITV YAVTGRGDSP
ASSKPVSINY RTEIDKPSQM QVTDVQDNSI SVRWLPSSSP VTGYRVTTAP KNGPGPSKTK
TVGPDQTEMT IEGLQPTVEY VVSVYAQNQN GESQPLVQTA VTNIDRPKGL AFTDVDVNSI
KIAWESPQGQ VSRYRVTYSS PEDGIHELFP APDGEEETAE LQGLRPGSEY TVSVVALHDD
MESQPLIGTQ STAIPAPTNL KFTQVTPTSL TAQWTAPNVQ LTGYRVRVTP KEKTGPMKEI
NLAPDSSSVV VSGLMVATKY EVSVYALKDT LTSRPAQGVI TTLENISPPR RARVTDATET
TITISWRTKT ETITGFQVDA IPANGQTPIQ RTIRPDVRSY TITGLQPGTD YKIHLYTLND
NARSSPVVID ASTAIDAPSN LRFLATTPNS LLVSWQPPRA RITGYIIKYE KPGSPPREVV
PRPRPGVTEA TITGLEPGTE YTIQVIALKN NQKSEPLIGR KKTDELPQLV TLPHPNLHGP
EILDVPSTVQ KTPFITNPGY DTGNGIQLPG TSGQQPSLGQ QMIFEEHGFR RTTPPTTATP
VRHRPRPYPP NVNEEIQIGH VPRGDVDHHL YPHAVGLNPN ASTGQEALSQ TTISWTPFQE
SSEYIISCHP VGVDEEPLQF RVPGTSASAT LTGLTRGATY NIIVEAVKDQ QRQKVREEVV
TVGNSVDQGL SQPTDDSCFD PYTVSHYAVG EEWERLSDSG FKLSCQCLGF GSGHFRCDSS
KWCHDNGVNY KIGEKWDRQG ENGQMMSCTC LGNGKGEFKC DPHEATCYDD GKTYHVGEQW
QKEYLGAICS CTCFGGQRGW RCDNCRRPGA EPGNEGSTAH SYNQYSQRYH QRTNTNVNCP
IECFMPLDVQ ADTEDSRE
//
