ID A0A3Q0S7Q8_AMPCI Unreviewed; 2407 AA.
AC A0A3Q0S7Q8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Fibronectin {ECO:0000256|ARBA:ARBA00020368};
OS Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC Cichlasomatinae; Heroini; Amphilophus.
OX NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000018842.1, ECO:0000313|Proteomes:UP000261340};
RN [1] {ECO:0000313|Ensembl:ENSACIP00000018842.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 Ensembl; ENSACIT00000019347.1; ENSACIP00000018842.1; ENSACIG00000013031.1.
DR GeneTree; ENSGT00940000155126; -.
DR Proteomes; UP000261340; 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; 8.
DR CDD; cd00062; FN2; 2.
DR CDD; cd00063; FN3; 16.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 10.
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:SF2; FIBRONECTIN TYPE-III DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46708; TENASCIN; 1.
DR Pfam; PF00039; fn1; 8.
DR Pfam; PF00040; fn2; 2.
DR Pfam; PF00041; fn3; 16.
DR PRINTS; PR00013; FNTYPEII.
DR PRINTS; PR00014; FNTYPEIII.
DR SMART; SM00058; FN1; 10.
DR SMART; SM00059; FN2; 2.
DR SMART; SM00060; FN3; 17.
DR SUPFAM; SSF49265; Fibronectin type III; 9.
DR SUPFAM; SSF57603; FnI-like domain; 10.
DR SUPFAM; SSF57440; Kringle-like; 2.
DR PROSITE; PS01253; FN1_1; 4.
DR PROSITE; PS51091; FN1_2; 8.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 2.
DR PROSITE; PS50853; FN3; 14.
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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..2407
FT /note="Fibronectin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018568027"
FT DOMAIN 87..130
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 131..174
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 176..220
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 221..265
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 350..398
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 410..458
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 463..507
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 512..554
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 555..598
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 604..697
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 710..800
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 802..894
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 901..992
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 993..1081
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1157..1246
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1249..1339
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1340..1434
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1435..1522
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1523..1613
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1617..1708
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1797..1898
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1899..1989
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1992..2088
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2294..2338
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT REGION 2096..2156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2113..2143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 355..381
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 369..396
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 415..441
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 429..456
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 2407 AA; 264594 MW; 01D350AB56FBFAAD CRC64;
MTGSTIARVL VALCIGTAVN XMPKGTHRNR RQALQHRATS VSQEGCMENG QFYGINDQWE
RQFLGNTLVC TCHGVAGVKC KSKPEVERCY DKVTEQFYTV GETYERPKEG MIWDCTCIGS
GRGKISCTIA NRCHEGGASY KIGDTWRRPH DTGGYMLECV CLGNGKGEWA CKPIAERCYD
NSAGTSYLVG ETWEKPYQGW MVVDCTCIGE GNGRITCTSR NRCNDQDTLS SYRIGDTWTK
TDARGNLLKC LCTGNGRGEW KCERHASLHT TGMGSGSRVI TNIQPVVYQP DTVPDHAQDG
TCQTETGLMY SVGQRWIKNQ GTKQMICTCL GTGVSCDQWD GPSPVYGGNS GGLPCVFPFV
YKGKIYHSCT SDGRADGQLW CSTSSDFETE QKYSFCTEKN AIVATRGGNS NGALCQFPFL
YNGRNYTDCT ADGRRDGMKW CGTTTNYDAE RRFGFCPMAA HDEVCTSSEG VMYHVGDQWD
KRHDVLGHMM RCTCVGNGRG EWSCIAYSQL NDQCNVDGFT YEVNQTFTKR HEEGYMMNCT
CFGQGRGRWK CDAIDQCQEP ETRAFYQIGE SWDKVIHGIM YKCYCYGNGV GELSCEPQST
HLGAPVQVII AESANQSNSH PIQWNVQQSA HITQYILKWR VKNSHSPWRE VTIPGHLNSY
TISGLKPGIT YEGQLISVLR YGRKEVTSFD FTTTYGSLAT THGLTTSPPP MVDISESVTE
ITSSSFVISW VSASDTVSGF RVEYELIEQG QGTGQPIVLD LPRTATSVNI NELLPGRKYT
VNVYAVTEGG EDLVLTTSQT TVPDAPKEHE VEEVGETSIV ISWEKPLAPI TGYRVVYTPS
EEGESTELTL PDTVTSVTLS DLRPGNLYNI SIYSVEDTLE SEPIFVQVRT SGDPLPDEVD
SPTNLQFFEV SDKKIVLTWS GPSSEVSGYR VTVVPVDESG SSHPEMNLPV SQNSYTEVTH
LQPGTLYRFS VYAIHNGEQS LPLIREQSTK PDAPTDIHFA NVTEDSAVML WFAPRAKITG
YRLFLMLEGS NPKQLRLPAR LTQYTLLNLK PDTEYTVTLH AEQDNTLSAG ETTLFTTTPP
MGNAPHFNAD VTDTSIIITW TPVPRIGYKL TVRPSQGGEA PRDVTSDSGS IYISGLTPGV
EYTYSVQPVI NGHEQGTPIT RRLDPFLTGE LVVQWNGAST PDITGYRVTC TPTNGQQGNS
VEEFVEAGEN SCTLENLSPG VEYNVSVVTV KDDMESTPVS TVIKPEIPQL TDLSFEDVSD
TTISLRWTPL NTTTITGYRV TVVAAGESVP IFEDMVQPTT GHYTVYGLEP GIDYDISVIT
VTENGESEPT TLTQQTSVPA PTNLGFGQVG PDSIEVTWVS PQVPNSADIN SFLIRYHPID
DEDEITETSV GGTTNSVVLR NLLPNTEYLV SVVCVYEQRE SSPLVGTQKT ALDSPVGLRF
SEIMTNSFTI HWYAPQSKIT GYRIRYQMVS GGRSKDERLP PSRNHFTLTG LHPDTEYLVN
IFAVSGIQES LPLSGTQKTI SDAPTDLEVL DSTPTSITVR WAAPPVTVRY YRITHGESGG
HSNPKEFTVP GSQSTATITN LKPGTDYTVT VYAVTGRGDS PASSIPIYVT HKTGVDSPSE
MEVTDVNDDS ITVRWSPAEG XIKGYRVTGA PRNGQGPSFT EVVAPDQTEF TFSGLMPTSE
YTFSVYAQGQ DGESSPQVVT ALTNVDRPKD LTFADIDSTS LRITWDSPEG TVTSYRVLYS
SSEEGERELL PAPRGDAEST VIYGLQPGRE RNLYSMFPLF PLTSFLFFFS LLTAISPPTN
LQFSQVTPTS FIMRWDMPSQ ENRLTGLTGL TGYRVVVNPK NKSGPTKEIN LAPDATQAHI
SGLMIATTYE VHVYALKNSL TSRPVQGEVT TLENISPPRR VRISDVNDST ITLTWRSKTE
TISGFLVEAT PTSFSSGYTP IQNTIGPELR SYTITGLEPG TSYKINIYTL KGNGRSVPLT
LTATTAQPLV IPPTNIRFTS LNPNSISFMW EPSRSPRVTG YYVTYEEAGG LPQEVIPRPH
AGQHFATING LKPGTEYVIK IVALQNALRS TSLVGKARTH SHLLVPELPQ LPVPHRPTTD
ILDVPDFDSN HVHLAGTSGQ NQPGQQGQHI YTEYQSLNPN NGFHGPYSGP KEGQRPTLKE
PLIYVPVTGP DGNRVPLVKV SDGPLPGLAF GFPDNETEFP QEAQTITTIS WKPIPHTTEY
EVSCNPITHL EEGGFLMRLP GTSSSATLIG LTSGASYNVI VEAMSGGAKE KVLEEVVTVG
NAVPGEIPIT PNRDMCYDTF TQTYHDVGSE WERMSETGFK LWCRCLGLGS GHFRCDSSSE
WLINSGWRCE NCRRPGGQTE MEVDLLQPVR SDVFDRYREN ALSKLNIQCP IECLRPELLA
DAHSPQE
//