ID G3I1V3_CRIGR Unreviewed; 2486 AA.
AC G3I1V3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Fibronectin {ECO:0000256|ARBA:ARBA00020368};
GN ORFNames=I79_017372 {ECO:0000313|EMBL:EGW14343.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW14343.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH001096; EGW14343.1; -; Genomic_DNA.
DR STRING; 10029.G3I1V3; -.
DR PaxDb; 10029-XP_007626451-1; -.
DR eggNOG; ENOG502QPTS; Eukaryota.
DR InParanoid; G3I1V3; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:UniProt.
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; 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; 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; 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:UP000001075};
KW Signal {ECO:0000256|SAM:SignalP};
KW Sulfation {ECO:0000256|ARBA:ARBA00022641}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..2486
FT /note="Fibronectin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003444887"
FT DOMAIN 55..95
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 100..143
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 144..187
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 189..233
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 234..278
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 359..407
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 419..467
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 478..521
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 526..568
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 569..612
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 620..727
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 731..821
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 822..913
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 918..1009
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1010..1097
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1098..1184
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1185..1279
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1280..1368
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1369..1461
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1462..1549
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1550..1643
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1644..1735
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1736..1823
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1824..1917
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1918..2004
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2005..2095
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2203..2297
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2304..2348
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 2349..2391
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 2393..2433
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT REGION 1669..1694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 364..390
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 378..405
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 424..450
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 438..465
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 2486 AA; 273503 MW; 6E96AF5FDFB3872C CRC64;
MLRGPGPGLL LAVLCLGTAV RCTEAGKSKR QTQQIVQPQQ IVQPQSPVAV SQSKPGCFDN
GKHYQINQQW ERTYLGNALV CTCYGGSRGF NCESKPEPEE TCFDKYTGNT YKVGDTYERP
KDSMIWDCTC IGAGRGRISC TIANRCHEGG QSYKIGDKWR RPHETGGYML ECLCMGNGKG
EWTCKPIAEK CFDHAAGTSY VVGETWEKPY QGWMMVDCTC LGEGSGRITC TSRNRCNDQD
TRTSYRIGDT WTKKDNRGNL LQCVCTGNGR GEWKCERHAL QSTSAGSGSL TDVRTAVYQP
QTHLQPAPYG HCVTDSGVVY SVGMQWLKSQ GNKQMLCTCL GNGVSCQETA VTQTYGGNSN
GEPCVLPFTY NGRTFYSCTA EGRQDGHLWC STTSNYEQDQ KYSFCTDHTV LVQTRGGNSN
GALCHFPFLY NNRNYTDCTS EGRRDNMKWC GTTQNYDADQ KFGFCPMAGK MKKASHEEIC
TTNEGVMYRI GDQWDKQHDL GHMMRCTCVG NGRGEWSCIP YSQLRDQCIV DDITYNVNDT
FHKRHEEGHM LNCTCFGQGR GRWKCDPIDQ CQDSETRTFY QIGDSWEKFV HGVRYQCYCY
GRGIGEWHCQ PLQTYPGTTG PVQVIITETP SQPNSHPIQW NAPEPSHITK YILRWRPKTS
VGRWKEATIP GHLNSYTIKG LTPGVVYEGQ LISIQQYGHR EVTRFDFTTS AGTPVTSNTV
TGETAPFSPV VATSESITEI TASSFVVSWV SASDTLSGFL VEYELSEEGG KPQYLDLPST
ATSVNIPDLL PGRKYIVNVY QISEEGKQSL ILSTSQTTAP DAPPDPTVDQ VDDTSIVVRW
SRPQAPITGY RIVYSPSVEG SSTELNLPET ANSVTLSDLQ PGVQYNITIY AVEDNQESAP
VFIQQETTGT PRSDKVPPPK DLQFVEVTDV KVTIMWTPPD SPVTGYRVDV LPVNLPGEHG
QRLPVNRNTF AEITGLTPGV TYHFNVYAVN QGRESKPLTA QQTTKLDAPT NLQFVNESDR
TVLVTWIPPR ARIAGYRLTV GLTRGGQPKQ YNVGPSASKY PLRNLQPGSE YTVTLVAVKG
NQQSPKATGV FTTLQPMSSI PPYNTEVTET TIVITWTPAP RIGFKLGVRP SQGGEAPREV
TSESGSIVVS GLTPGVEYTY TIQVLRDGQE KDAPIVNRVV TPLSPPTNLH LETNPDTGVL
TVSWERSVTP DITGYRITTT PTNGQQGSSL EEVVHADQSS CTFENLNPGL EYNVSVYTVK
DDKESAPISD TIIPEVPQLT DLSFVDITDS TIGLRWTPLN SSTIIGYRIT VVATGEGIPI
FEDFVDSSVG YYTVTGLEPG IDYDISVITL INGGESAPTT LTQQTAVPPP TDLRFTNIGP
DTMRVTWAPP PSIELTNLLV RYSPVKNEED VAELSISPSD NAVVLTNLLP GTEYLVSVSS
VYEQHESTPL RGRQKTGLDS PTGFDSSDIT ANSFTVHWVA LRAPITGYII RHHAEQSVGR
PRQDRVPPSR NSITLSNLNP GTEYIVSIIA VNGREESAPL IGQQSTVSDV PRDLEVIAST
PTSLLISWEP PAVSVRYYRV TYGETGGNSP VQEFTVPGSK STATINNIKT GTDYTITLYA
ITGRGDSPAS SKPISINYRT EIDKPSQMQV TDVQDNSISV RWLPSSSPVT GYRVTTTPKN
GPGPSKTKTA GPDQTEMTIE GLQPTVEYVV SVYAQNQNGE SQPLVQTAVT NIDRPKGLAF
TDVDVDSIKI AWESPQGQVS RYRVTYSSPE DGIHELFPAP DGEEDTAELQ GLRPGSEYTV
SVVALHDDME SQPLIGIQST AIPAPTNLKF TQVTPTSFSA QWVAPNVQLT GYRVRVTPKE
KTGPMKEINL SPDSSSVVVS GLMVATKYEV SVYALKDTLT SRPAQGVITT LENVSPPRRA
RVTDATETTI TISWRTKTET ITGFQVDAIP ANGQPPVQRT ISPDIRTYTI TGLQPGTDYK
IHVYTLNDNA RSSPVIIDAS TAIDAPSNLR FLATTPNSLL VSWQAPRARI TGYIIKYEKP
GSPPREVVPR PRPGVTEATI TGLEPGTEYT IYVIALKNNQ KSEPLIGRKK TDELPQLVTL
PHPNLHGPEI LDVPSTVQKT PFITNPGYDT ENGIQLPGTT HQQPSVGQQM IFEEHGFRRT
TPPTAATPVR LRPRPYLPNV DEEVQIGHVP RGDVDYHLYP HVPGLNPNAS TGQEALSQTT
ISWTPFQESS EYIISCHPVG TDEEPLQFQV PGTSTSATLT GLTRGVTYNI IVEALQNQRR
HKVREEVVTV GNAVNEGLNQ PTDDSCFDPY TVSHYAIGEE WERLSDSGFK LTCQCLGFGS
GHFRCDSSKW CHDNGVNYKI GEKWDRQGEN GQRMSCTCLG NGKGEFKCDP HEATCYDDGK
TYHVGEQWQK EYLGAICSCT CFGGQRGWRC DNCRRPGGEP SPDGTTGHTY NQYTQRYHQR
TNTNVNCPIE CFMPLDVQAD RDDSRE
//
