ID V8P062_OPHHA Unreviewed; 2386 AA.
AC V8P062;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Fibronectin {ECO:0000256|ARBA:ARBA00020368};
DE Flags: Fragment;
GN Name=FN1 {ECO:0000313|EMBL:ETE67561.1};
GN ORFNames=L345_06652 {ECO:0000313|EMBL:ETE67561.1};
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE67561.1, ECO:0000313|Proteomes:UP000018936};
RN [1] {ECO:0000313|EMBL:ETE67561.1, ECO:0000313|Proteomes:UP000018936}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Blood {ECO:0000313|EMBL:ETE67561.1};
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETE67561.1}.
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DR EMBL; AZIM01001254; ETE67561.1; -; Genomic_DNA.
DR Proteomes; UP000018936; Unassembled WGS sequence.
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; 11.
DR CDD; cd00062; FN2; 2.
DR CDD; cd00063; FN3; 16.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 11.
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; 10.
DR Pfam; PF00040; fn2; 2.
DR Pfam; PF00041; fn3; 17.
DR PRINTS; PR00013; FNTYPEII.
DR SMART; SM00058; FN1; 11.
DR SMART; SM00059; FN2; 2.
DR SMART; SM00060; FN3; 17.
DR SUPFAM; SSF49265; Fibronectin type III; 11.
DR SUPFAM; SSF57603; FnI-like domain; 11.
DR SUPFAM; SSF57440; Kringle-like; 2.
DR PROSITE; PS01253; FN1_1; 5.
DR PROSITE; PS51091; FN1_2; 10.
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 Reference proteome {ECO:0000313|Proteomes:UP000018936};
KW Sulfation {ECO:0000256|ARBA:ARBA00022641}.
FT DOMAIN 11..51
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 56..99
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 145..189
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 190..234
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 316..364
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 376..424
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 429..472
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 477..519
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 520..563
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 570..662
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 677..768
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 770..861
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 868..957
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 958..1047
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1048..1134
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1135..1229
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1230..1318
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1319..1411
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1412..1499
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1500..1593
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1594..1685
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1686..1773
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1774..1864
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1866..1954
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1955..2045
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2154..2242
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2251..2295
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 2298..2338
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT REGION 1611..1640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 321..347
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 335..362
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 381..407
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 395..422
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ETE67561.1"
SQ SEQUENCE 2386 AA; 263076 MW; F9B8AB47AD00F871 CRC64;
MTGWLHSLSH KGCYDNGQHY QINQQWERIY LGNTLVCTCY GGSRGFNCES KPEPEETCFD
KYTGTTYRVG ETYERPKDSM IWDCTCIGAG RGRISCTIAN RCHEGGQSYK IGDTWRRPHE
TGGYMLECVC LGNGKGEWTC KPVAERCYDN TAGTSYVVGE VWEKPYQGWM MVDCTCLGEG
SGRITCTSRN RCNDQDTKTS YRIGETWSKK DNRGNLLQCI CTGNGRGEWK CERHSSLQAT
GVGSASATIT DVRTALYQPQ PQPAPYGHCV TDSGMMYILG MQWLKAQGSQ HMLCTCLGNG
ISCQETAVTQ TYGGNSNGEP CVFPFTYDER TFYSCTSEGR NDGNLWCSTT SNFNQDKSYS
FCTEQNVVVQ TRGGNSNGAL CHFPFLYNNR NYTDCTSEGR RDNMKWCGTT SNYDVDQKFG
FCPMAAHEEI CTTNDGVMYR VGDQWDKQHD MGHMMRCTCV GNGRGEWTCV AYSQLRDQCI
VDGITYDVNQ TFHKRHEEGH MLNCTCFGQG RGRWKCDPID QCQDSESQTF YQIGDSWEKH
AHGVRYQCYC YGRGIGEWHC QPLNTGSPGH PVQVIITDVP IQPDSHPIQW IVPESSHISN
YILRWKPKNS RVQWKEARIP GYLNSYTISG LKPGVLYEGQ LISVQHYGQR EITRFEFTTS
STTAISSSRV AGETTALPSV VSISESVTEI TANSFVVSWV SASDTVSGFR VEYELSEDGD
EPKYLDLPNT VNSVSIPNLL PGRNYIIKVY QISEEGEQNL ILSTTQTTAP DAPPDHLVEN
VDDTSILVSW RRPEAPITGY RIVYTPSLEG SSTELNLPES ATSVTLSDLM PGVQYNISIY
AVEENQESSP IFIQQKTTGV PVADDIHPPQ HLQFLEVASD KITIMWSPPD SAVIGYRVEV
IPVNRPGEHG QRLPVSRYTF AEITELLPGT TYLFKIYAIG QNTESEPLTG EQTTKLDGPT
NLRLVSETPS TALVTWKSPR ARITGYQLTV QPVTDGHPKQ YTVGPSATKY LLKNLQPGSE
YTVSLVAVKD NQKSNPEEGT FTTLQSTGSV PPYNTEVTET SIVVTWIPAP RLGFKLGVRP
SQGGEAPREV ISESGSIVIS GLTPGVEYIY SINVIKDGQE GTTPIVKTVI TPPSPPTNLH
LDSNPDTGIL TVSWGKSTTP DITGYRITTI PTNGQEGYTL EEQVQAEVTS CTFENLSPGM
EYNVSVYTLK DNQESLPISE TITQEVPQLT DLNFVDVSDT SIGLKWTPIN TSAIIGYRIK
VIATGETVPI FEDFVDSSVG YYMVTGLEPG IDYEISVITL INGGESAPTT LIQQTAVPPP
TDLRFTNVGP DTIRVTWTPP ASIELTSFLV RFSPMKNKED VAELSISPSD NAVVLTNLLP
GTAYLIKVYS VYEQHESKPL SGEQKTGLDS PTGLDFSEIT AHSFIVHWIA PRAPISGYKI
RHHLEQGGSR PKEVRVAPSR NFITLTDLIP GSEYVVSVSA FYGKEESLPL IGQQSTVSDV
PRDLHVTATG PTSLVVSWDA PAVTVRYYRI TYGETGGSGP VQEFTVPGHV STATIPGLKP
GVDYTITVYA VTGRGDSPAS SKPVSINYRI EVDTPSQLQV TDVQDNSLTV QWQPSSSPVT
GYRVTATPKD NHSPTKSRVL SAEQTEVTID ELQPTIEYVV SVYAQGPNGE SQPLVEKVVT
NIDRPKGLAF TAVDVDSIKI AWESPQGQVT GYRVTYSTPE DGIQELFPAP DGEDDTAELH
GLRPGSEYTV YIVALHNDLE SLPLIGTQTT AIPPPTNLKF IQVAPTSLTL TWTAPNVKLT
GYRVRVNPKE KNGPMKEINL APDSTSAVIS GLMVATKYEV SVYALKDSLT SRPTQGVVNT
LENVSAPRRA RVTDVTERTI TITWRTKTEA ITGFQIDAIP AGGQNPVQRT IGPDVRTYTI
TGLQPGTDYK IFIYALNENA RSSPAELDAS TAIDAPSNLR FLTTTSNSLL ISWQPPRAKI
TDYIIKYEQV GGPTRELFPR PRSGITEATI TGLEPGTEYI IYITAVKNNQ KSEPLIGRKK
TDELPRLVTP PHPGERVTEI LDVPSVLENV PYLTNNPYDN GNGIPIPGSS GQQSILINPG
QQVIVEEFGS RTPTTPATPG RAKPNKEEQP VVVIHHPIQV PEVDKPSYHH TLLSKDNYTR
PQEALSQTTI SWTPYTDSSE YIISCQPVSA EEEPTEIKVP GMYSSATLTG LTRGATYNII
VEAVKNQRRH RVLEEMVTVG NDVSGRLPTD DVCYDTFTGS FYSIGDEWER MSETGFKLWC
QCLGLGSGHF RCDSSNEATC YDDGKMYRVG QQWQKEYLGA ICSCTCYGGQ QGWRCDNCRR
PGASEGSPSQ TYLQREQQSP NTNIQCPIEC FYPLHLHSDA QIQRGD
//
