ID A0A2D0Q5W0_ICTPU Unreviewed; 2476 AA.
AC A0A2D0Q5W0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Fibronectin {ECO:0000256|ARBA:ARBA00020368};
GN Name=fn1b {ECO:0000313|RefSeq:XP_017312740.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017312740.1};
RN [1] {ECO:0000313|RefSeq:XP_017312740.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017312740.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_017312740.1; XM_017457251.3.
DR GeneID; 108258550; -.
DR CTD; 334613; -.
DR OrthoDB; 5399734at2759; -.
DR Proteomes; UP000221080; Chromosome 26.
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; 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; 16.
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; 12.
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 Signal {ECO:0000256|SAM:SignalP};
KW Sulfation {ECO:0000256|ARBA:ARBA00022641}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..2476
FT /note="Fibronectin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012406719"
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 358..406
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 418..466
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 471..514
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 519..561
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 562..605
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 609..701
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 717..807
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 808..897
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 904..996
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 997..1086
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1087..1173
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1174..1268
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1269..1359
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1360..1454
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1455..1541
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1542..1632
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1639..1729
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1731..1821
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1822..1911
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1914..2004
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2007..2097
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2198..2291
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2298..2342
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 2343..2385
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 2387..2427
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT REGION 1343..1363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 363..389
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 377..404
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 423..449
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 437..464
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 2476 AA; 272343 MW; D7E867915FF1E70F CRC64;
MRRLVLLALC ACSAVVCVPK SGRNKRQQQQ QVLPGIPVEE LAYTRQAVCT ENGRFYQVND
QWERPYMGST LLCTCKGSAG IQCESKPAGE EMCFDKVNAR SYRVGETYER PKDGMIWDCT
CIGSGRGKIS CTIANRCHEG GRSYRIGETW TRPHDTGDYM LECVCLGNGK GEWTCKPIAE
RCYDTSVGAS YVVGQTWEKP YQGWMIVDCT CLGEGNGRIT CTSRNRCNDQ DMRKSYRIGE
TWTKVDSQGR AQQCVCTGNG RGEWKCESHT SAQTALGECD TGSGSGLSTQ VKPVTHQLNI
LPVLAEIGTC QTRSGTIYYD GMRWVQTQGS QQMICTCVNG GIGCEEWDGQ SHVYGGNSNG
QPCVFPFTFG GKTHYSCISE GRTDGQLWCS TTSDYDTDRQ YSFCTQRNLM VTTRGGNSNG
ALCQFPFLYN GRNYTDCTAD GRRDGMKWCG TTANYDDERR YGFCPMAAHE EICTVNDVMY
RLGDEWDKRH DTMGHMMRCK CVGNGRGEWS CVAHSQIRDQ CIVDGLTYEV DQTFDKRHNE
GYMMNCTCFG QGRGRWKCDA IDQCQEAETK VFYQIGETWD KVSHGVRYRC TCYGNGIGEH
ACEPLESRVP VRVTITETGN QPNSHPIQWN PPASAHITQY ILKWKVKNTR TPWREVIIPS
HINSYTISGL KPGLTYEGQL ISILNYGHRE VTRFDFTTSS GSLVPTEGVT TQNTRVLDTS
ESITEITSSS FVVSWTSASE TISGFRVQYE LSEEGAEPTV IDLPRTSTSV NIDRLLPGRT
YHVQVYEVEP EGDTNLILTT TQTTAPDTPS DHRVTEVRET SIVISWTKPH APITGYRVVY
TPSVEGSSTE LNLPETVTSV TLVDLQPGQS YNVSIFAVEG NLESEAVVLQ VRTAGESQPE
EVQAPTELQF YEVTDVKITI TWTGPPSEVS GYRVTYEPVS SDGHSTQRPL ALPTTPNAYA
EITHLQPGTL YRFYVYAVYG GAESQPLVGE KSTRPDAPTD LRFPDVTEDT VLVVWSAPQA
RITGYRLYIT TEDSTSPTLL RIRPEETQYT VPNLQPDTMY TVTLHSEHGS TLSEGVSGTV
TTTVPIGNAP RFSTDVTDSS IIISWTPVPR FSYRMSVKPS QGGEAPRVVT SDSGSIYISG
LTPGVEYTYS LQPIINGRKQ GNAITRNVVT PLSPPSDLNL VSNPNTGDLS VRWRESTTPD
ITGYRVTCTP TLGQRANSLE EFVRGQQTSC TLENLSPGVE YNVSVYTVKN HIESEPISSV
ITQDVPKVSD LGYVNVTDTT IGIQWTLLNH PAVTGYRVTV LAAGESLPIL EDSLDSGTGF
YTVRGLEPGV DYHISVITLT EESESEPTTI TQQTQAGVPA PTNLKFGEVG PDSMRLSWTR
PSVRQSEISR FVIRYHPSND DDNIQEVNVG GATSTYLLQH LLPVTEYVVS VSCVYGQRES
TPVTGRQTTN LDSPSGLVFS DVFTHSFTAN WQAPRAPITG YRLAYEATSG GRRQEERLPP
SRTRYALNNL QPNTLYTLRI YAVSGRQESQ PLTGTQATIS DAPTDLEVTS STPNSITISW
DAPAIPVRYY RIKHEQTGER GSGQEFTVPG TESTATIGGL QPGTDYTVTI YAVTGRGDSP
ASSTPTIITH RTGSHGVPSP SDLDVTDIQD QAIVVRWSPA RGPITGYRVT GSPKNGVGPT
FSKEVGPDQT ELRITGLVPT VEYVISVYAI GRDGKSTPVV ERATTIKPTD SPTDLTFSDV
DSSSVRVSWR PPQGRVTSYR VFYSSPETGE REWSPAPSRN DDNVLLQHLR PGTEYSVRVI
ATTDRGATAE LAGTHTTVVP APTNIQFGDV GPSSFVVLWR APGIRLNGYR VLVKPKNNIA
QPKELNVAPD SMQVTVTGLL VSTVYEVYVY ALKDSVSSPP LVGEVTTTGE DISPPRRPRV
NEVKDTSITL NWRAKIEPIT GFLIEATPIS GNYPTIRKEI PGEHRSAVIT GLHPGTAYKI
NIYTLNGDRR SAPFTLSTNT IGSSLQPPTD LRFQALSPTS ISFNWQPPTS HITGYYITYE
EEGSSPRELT PRPHAGTNYA TITGLKPATV YIIKIIALQN TLRSPPLVGK ARTQESLLLP
LPIPPRHNTL GPLDVPETDI LVNVVGPTVQ PGPGEGGQGM EYTEYNNQPT LPHSGHRPNP
YVPGTGQTLI YVPAPGPDGS RVPKVVQLSD RNAHGFTFPE NKTGTPQEAQ TQTTVSWQPF
RQSKAYLVTC HPVTQRNEKM FQLQLPSTST SATLIGLTSG ASYRVLVEAL KDALKYKILD
EVITAGNTDP AGVPASDDSC YDTLTATHHN IGDEWERMSE TGFKLWCRCL GLGSGHFRCD
SSKWCHDNGH NYLIGERWER RAENGHMMSC TCLGNGKGEF KCEPHESTCY DEGKTYQVGN
QWQKEYLGAI CTCICYGGQQ GWRCENCKKP GTEINTHLLK PVRYGDGIAK VNIHCPIECL
RPDILADAVA NPNPLE
//