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Entry: A0A3Q0S7Q8_AMPCI
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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.
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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
//
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