ID F7CN05_HORSE Unreviewed; 2387 AA.
AC F7CN05;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Fibronectin {ECO:0000256|ARBA:ARBA00020368};
GN Name=FN1 {ECO:0000313|Ensembl:ENSECAP00000005229.2,
GN ECO:0000313|VGNC:VGNC:56555};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000005229.2, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000005229.2, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000005229.2,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000005229.2}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000005229.2};
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 Ensembl; ENSECAT00000007212.4; ENSECAP00000005229.2; ENSECAG00000000701.4.
DR VGNC; VGNC:56555; FN1.
DR GeneTree; ENSGT00940000155126; -.
DR Proteomes; UP000002281; Chromosome 6.
DR Bgee; ENSECAG00000000701; Expressed in articular cartilage of joint and 23 other cell types or tissues.
DR ExpressionAtlas; F7CN05; 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; 15.
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; 16.
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; 16.
DR PRINTS; PR00013; FNTYPEII.
DR SMART; SM00058; FN1; 12.
DR SMART; SM00059; FN2; 2.
DR SMART; SM00060; FN3; 16.
DR SUPFAM; SSF49265; Fibronectin type III; 10.
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; 16.
PE 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:F7CN05};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281};
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..2387
FT /note="Fibronectin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018599377"
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 722..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..1725
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1726..1818
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1819..1905
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1906..1996
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2104..2198
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2205..2249
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 2250..2292
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 2294..2334
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 2059..2079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..45
FT /note="Polar 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 2387 AA; 262326 MW; 925914411B6C35B4 CRC64;
MLRGPGPGLL LLVVLSLGTA VPSSGASKRK RQDQQIIQPQ SPVAVGQSKP GCYDNGKHYQ
INQQWERTYL GNALVCTCYG GSRGFNCESK PEPEETCFDK YTGNTYRVGD TYERPKDSMI
WDCTCIGAGR GRISCTIANR CHEGGQSYKI GDTWRRPHET GGYMLECVCL GNGKGEWTCK
PIAEKCFDHA AGTSYVVGET WEKPYQGWMM VDCTCLGEGN GRITCTSRNR CNDQDTRTSY
RIGDTWSKKD NRGNLLQCIC TGNGRGEWKC ERHASLQTTS TGSGPFTDVR TAIYQPQPHP
QPAPYGHCVT DSGVVYSVGM QWLKTQGNKQ MLCTCLGNGV SCQETAVTQT YGGNSNGEPC
VLPFTYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF CTDSAVLVQT RGGNSNGALC
HFPFLYNNHN YTDCTSEGRR DNMKWCGTTQ NYDADQKFGF CPMAAHEEIC TTNEGVMYRV
GDQWDKQHDM GHMMRCTCVG NGRGEWTCVA YSQLRDQCIV DDITYNVNDT FHKRHEEGHM
LNCTCFGQGR GRWKCDPIDQ CQDSETRTFY QIGDSWEKYV HGVRYQCYCY GRGIGEWHCQ
PLQTYPGTTG PVQVIITETP SQPNSHPIQW NAPEPSHISK YILRWKPKNA PGRWKEATIP
GHLNSYTIKG LRPGVVYEGQ LISVQHYGHK EVTRFDFTTT STSPAVTSNT VTGETTPFSP
VVATSESVTE ITASSFVVSW VSASDTVSGF RVEYELSEEG DEPQYLDLPS TATSVNIPDL
LPGRKYIVNV YQISEEGEQS LILSTSQTTA PDAPPDPTVD QVDDTSIVVR WSRPQAPITG
YRIVYSPSVE GSSTELTLPE TANSVTLSDL QPGVQYNITI YAVEENQEST PVFIQQETTG
VPRADKVPPP RDLQFVEVTD VKITIMWTPP ESAVTGYRVD VLPVNLPGEH GQRLPISRNT
FAEVTGLSPG VTYHFKIFAV NHGRESKPLT GEQTTKLDAP TNLRFINETE STVIVTWTPP
RARIAGYRLT VGLTRGGQPK QYNVGPSASQ YPLRSLQPGS EYTVTLVAVK GNQQSPKATG
VFTTLQSPGS IPPYNTEVTE TTIVITWTPA PRIGFKLGVR PSQGGEAPRE VTSDSGSIVV
SGLTPGVEYV YTISVLRDGQ ERDAPIVKKV VTPLSPPTNL HLEANPDTGV LTVSWERSTT
PDITGYRITT TPTSGQQGYS LEEVVHADQS SCTFENLSPG LEYNVSVYTV KDDKESVPIS
DTIIPEVPQL TDLSFVDITD SSIGLRWTPL NSSTIIGYRI TVVAAGEGIP IFEDFVDSSV
GYYTVTGLEP GIDYDISVIT LINGGESAPT TLTQQTAVPP PTDLRFTNVG PDTMRVTWAP
PPSIELTNLL VRYSPVKNEE DVAELSISPS DNAVVLTNLL PGTEYLVSVS SVYEQHESTP
LRGRQKTGLD SPTGIDFSDI TANSFTVHWI APRATITGYR IRHHPEHTGG RPREDRVPPS
RNSITLTNLN PGTEYVVSIV ALNGREESPP LVGQQSTVSD VPRDLEVIAT TPTSILISWD
APAVTVRYYR ITYGETGGNS PVQEFTVPGS KSTATISGLK PGVDYTITVY AVTGRGDSPA
SSKPISIDYR TEIDKPSQMQ VTDVQDNSIS VRWLPSSSPV TGYRVTTTPK NGPGQSKTKT
AGPDQTEMTI EGLQPTVEYV VSVYAQNQNG ESQPLVQTAV TTIPAPTELK FTQVTPTSLT
AQWTAPNVQL TGYRVRVTPK EKTGPMKEIN LAPDSTSVVV SGLMVATKYE VSVYALKDTL
TSRPAQGIVT TLENVSPPRR ARVTDATETT ITISWRTKTE TITGFQVDAV PANGQPPIQR
TIKPDVRSYT ITGLQPGTDY KIYLYTLNDN ARSSPVIIDA STAIDAPSNL HFLATTPNSL
LISWQPPRAR ITGYIIKYEK PGSPPREVVP RPHPGVTEAT ITGLEPGTEY TIQVIAIKNN
QKSEPLIGRR KTDELPQLVT LPHPNLHGPE ILDVPSTVQK TPFITNPGYD NGNGIQLPGT
SGQQPSVGQQ MIFEEHGFRR TTPPTTATPV RHRPRPYPPN VNEEIQIGHV PRGDVDQHLY
PHVLGLNPNT STGQEALSQT TISWTPFQES SEYIISCHPV GIDEEPLQFR VPGTSASATL
TGLTRGATYN IIVEALKDQK RHKVREEVVT VGNSVDQGLG QPTADSCFDP YTVSHYAIGE
EWERLSESGF KLSCQCLGFG SGHFRCDSSK WCHDNGVNYK IGEKWDRQGE NGQMMSCTCL
GNGKGEFKCD PHEATCYDDG KTYHVGEQWQ KEYLGAICSC TCFGGQRGWR CDNCRRPGAE
PGHEGSTGHS YNQYSQRYQQ RTNTNVNCPI ECFMPLDVQA DRDDSRE
//
