ID A0A3Q3VVW6_MOLML Unreviewed; 2129 AA.
AC A0A3Q3VVW6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Fibronectin {ECO:0000256|ARBA:ARBA00020368};
OS Mola mola (Ocean sunfish) (Tetraodon mola).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Molidae; Mola.
OX NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000007096.1, ECO:0000313|Proteomes:UP000261620};
RN [1] {ECO:0000313|Ensembl:ENSMMOP00000007096.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR STRING; 94237.ENSMMOP00000007096; -.
DR Ensembl; ENSMMOT00000007230.1; ENSMMOP00000007096.1; ENSMMOG00000005510.1.
DR OMA; VHWLAPQ; -.
DR Proteomes; UP000261620; Unplaced.
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; 1.
DR CDD; cd00063; FN3; 14.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 12.
DR Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 15.
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; 1.
DR Pfam; PF00041; fn3; 14.
DR PRINTS; PR00013; FNTYPEII.
DR SMART; SM00058; FN1; 12.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00060; FN3; 15.
DR SUPFAM; SSF49265; Fibronectin type III; 10.
DR SUPFAM; SSF57603; FnI-like domain; 12.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR PROSITE; PS01253; FN1_1; 4.
DR PROSITE; PS51091; FN1_2; 11.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 1.
DR PROSITE; PS50853; FN3; 13.
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:UP000261620};
KW Signal {ECO:0000256|SAM:SignalP};
KW Sulfation {ECO:0000256|ARBA:ARBA00022641}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..2129
FT /note="Fibronectin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018660395"
FT DOMAIN 47..86
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 91..134
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 135..178
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 180..224
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 225..269
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 379..427
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 432..476
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 481..523
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 524..567
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 575..668
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 681..768
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 769..858
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 865..956
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 957..1044
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1045..1132
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1133..1224
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1226..1320
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1321..1408
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1409..1499
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1503..1595
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1603..1694
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1778..1866
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1958..2002
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 2003..2045
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 2047..2085
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DISULFID 384..410
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 398..425
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 2129 AA; 233492 MW; 0185D088896BE92E CRC64;
ISMSSGSTIA RVLVALCIGS AVNCMPSGTH KNRRQAQQHR VPSVSQDGCL ENGQHYGVND
QWERPYLGSI LVCTCHGVAG IKCKSKPEAE ERCFDKTKQQ SYAVGETYER PKDGMIWDCT
CIGSGRGKIS CTIGNRCHEG GASYKIGDTW RRPHETGGYM LECVCLGNGK GEWTCKPVAE
RCYDNSAGTS YVVGETWEKP YQGWMVVDCT CLGEGSGRIT CTSRNRCNDQ DTLSSYRIGD
TWTKTDSQGH LLQCLCTGNG RGEWKCERHA SLHTTSTGSR VITNIQPAVY QPVGVPEHHQ
EGPCRTDSGL TYFIGQQWMK NQGSKQMICI CLGHGVSCEP WGKNFPLTPS LSTTVEYVCC
TWYFVFLFTV IVATRGGNSN GALCQFPFLY NGRNYTDCTA EGRRDGMKWC GTTTNYDAEQ
RFGFCPMAAH EEVCTTSEGV MYRVGDQWDK RHDVLGHMMR CTCVGNGRGE WSCVAYSQLK
DQCIVDGLTY EVNQTFTKLH EEGYTMNCSC FGQGRGRWKC DAIDQCQEPE TRAFYQIGES
WDKVIGGIMY KCYCYGNGIG ELSCEPQQSY HGGHRPVQVI ITESGNQPNS HPIQWNAPQS
AHITQYILKW RVKNTQSPWK EVAIPGHLNS YTISGLKPGI TYEGQLISVL QFGQQEVTRF
DFTTTYGSLA TSQGETTQPP PVVDTSESVT EITSSSFVIS WVSASDTVSG FRVEYELTEQ
GQDLPRTTTS VNINELLPGR KYTVKVYEVT DTGEDNIILT TSQTTAPDAP SEHELKDVGE
TSIVITWEKP LAPITGYRVV YTPSIEGEST ELTLPDTATS VTLSDLLPGK LYNISIYSVE
DSLESEPVFL QVNTAGDPLP EEVASPTDLQ FFEVSDKKIV LTWSGPAGSV SGYRVTVVAV
DEPSSPQREI TLPVSQNSYF EVTQLEPGTL YRFNVYTIDN GEESLPLIGE QTTKPDAPTD
IHFTDVTEDS AVIRWFAPRA KLTGYRLFLI VEGSSPKQLH LPAGLSQYTI LNLKPNTEYT
TTLHAEQENT LSKGETAVFT TNPPMGNTPH FSTDVTNTSI MISWTPVPRI GYKLTVRPSQ
GGEAPRDVTS EAGSIYISGL TPGVEYTYSV QPVINGHEQG TAVTRHVVTP LSPPTDLNLE
SNPGTGDLIV QWNGTSTPDI TGYKVTCTPT NGQEGNSVEE FVEAGQNSCT LDNLSPGVEY
NISVVTVKDD MESTPVSTTI TPAVPAPTNL GFGLVDSDSM EISWGSPRVP NPAEISEFLI
RYHPIDDEDD ITETSVTDGS NKVVLRNLLP DTEYLVSVVC VYEQRESSPV VGTQKTALDS
PAALSFSEIF TNSFTVHWLA PQSKITGYRI RYQMVSGGRA KDERLPPSRN HFTLTGLTPD
TEYLVSIFAV SRTEESMPLI GKQKTISDAP TDLEVLDSTP TSITVHWDAP PVTVRYYRIT
HGETGGHSNP KEFTVPGSQS TATITNLTPG TDYIITVYAV TGRGDSPASS TPIYVTHRTS
VNSPSEMEVM SVKDNSVTVR WSPAQGPIKG YRVTGVPRNG QGPSFTEVVA PDQTEITFSG
LMPTAEYILS VYALGQDGES SPVVVTALTT ISPPTNLQFS QVGPTSFTMS WAMPGQENRL
TGLKGLTGYR VVVNPKNKSG PTKEINLAPD ATQAHISGLM VATTYEVQVY ALKNSLTSRP
VQGEVTTQEN ISPPRRVRIA DVNDSAITLT WRSKTDIISG FLIEATPTSS PAGYIPIQKT
ISPNLRSYTI TGLEPGTNYK INIYTLKGNG RTKPLVIPPT NIRFTSLNTN SISFSWEPSR
SPGVTGYYVT YEQAGGLPQE LIPRPHATQS YAIINGLKPE TEYVIKIVAL QNALRSTPLV
GKLPQEAQTV TTISWQPIPQ TSEYEVSCNP ITHKEEGGFQ MRLPGTSNSA TLIGLTSGAS
YKVVVEAMRG GAKEKVLEEL VTVGNAVPGD IPITTNRDVC YDTFTQTYHD LGSEWERMSE
TGFKLWCRCL GLGSGHFRCD SSKWCHDNGN NYRIGEKWDR RAENGQMMSC TCLGNGKGEF
KCEPHESTCY DDGKMYQVGN HWQKEYLGAI CTCTCHGGQQ VCSCVVSSTF YVSVFKQITF
SSRPALQNIQ CPIECLRPEL LADALSPSD
//
