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Database: UniProt
Entry: K7GDA6_PELSI
LinkDB: K7GDA6_PELSI
Original site: K7GDA6_PELSI 
ID   K7GDA6_PELSI            Unreviewed;      2389 AA.
AC   K7GDA6;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Fibronectin {ECO:0000256|ARBA:ARBA00020368};
GN   Name=FN1 {ECO:0000313|Ensembl:ENSPSIP00000018267.1};
OS   Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC   Trionychidae; Pelodiscus.
OX   NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000018267.1, ECO:0000313|Proteomes:UP000007267};
RN   [1] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG   Soft-shell Turtle Genome Consortium;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX   PubMed=23624526; DOI=10.1038/ng.2615;
RA   Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA   White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA   Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA   Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA   Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT   "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT   into the development and evolution of the turtle-specific body plan.";
RL   Nat. Genet. 45:701-706(2013).
RN   [3] {ECO:0000313|Ensembl:ENSPSIP00000018267.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AGCU01115502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01115503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01115504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01115505; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01115506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AGCU01115507; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 13735.ENSPSIP00000018267; -.
DR   Ensembl; ENSPSIT00000018353.1; ENSPSIP00000018267.1; ENSPSIG00000015987.1.
DR   eggNOG; ENOG502QPTS; Eukaryota.
DR   GeneTree; ENSGT00940000155126; -.
DR   HOGENOM; CLU_000916_0_0_1; -.
DR   OMA; VHWLAPQ; -.
DR   TreeFam; TF329915; -.
DR   Proteomes; UP000007267; Unassembled WGS sequence.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0005577; C:fibrinogen complex; IEA:Ensembl.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR   GO; GO:0016504; F:peptidase activator activity; IEA:Ensembl.
DR   GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR   GO; GO:0043394; F:proteoglycan binding; IEA:Ensembl.
DR   GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR   GO; GO:0051702; P:biological process involved in interaction with symbiont; IEA:Ensembl.
DR   GO; GO:0007161; P:calcium-independent cell-matrix adhesion; IEA:Ensembl.
DR   GO; GO:0007044; P:cell-substrate junction assembly; IEA:Ensembl.
DR   GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR   GO; GO:0033622; P:integrin activation; IEA:Ensembl.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0150102; P:negative regulation of monocyte activation; IEA:Ensembl.
DR   GO; GO:0071635; P:negative regulation of transforming growth factor beta production; IEA:Ensembl.
DR   GO; GO:1901166; P:neural crest cell migration involved in autonomic nervous system development; IEA:Ensembl.
DR   GO; GO:0045773; P:positive regulation of axon extension; IEA:Ensembl.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:1904237; P:positive regulation of substrate-dependent cell migration, cell attachment to substrate; IEA:Ensembl.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR   GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR   CDD; cd00061; FN1; 12.
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; 16.
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; 16.
DR   SUPFAM; SSF49265; Fibronectin type III; 9.
DR   SUPFAM; SSF57603; FnI-like domain; 12.
DR   SUPFAM; SSF57440; Kringle-like; 2.
DR   PROSITE; PS01253; FN1_1; 4.
DR   PROSITE; PS51091; FN1_2; 11.
DR   PROSITE; PS00023; FN2_1; 1.
DR   PROSITE; PS51092; FN2_2; 2.
DR   PROSITE; PS50853; FN3; 16.
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:UP000007267};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Sulfation {ECO:0000256|ARBA:ARBA00022641}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..2389
FT                   /note="Fibronectin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003906418"
FT   DOMAIN          49..89
FT                   /note="Fibronectin type-I"
FT                   /evidence="ECO:0000259|PROSITE:PS51091"
FT   DOMAIN          94..142
FT                   /note="Fibronectin type-I"
FT                   /evidence="ECO:0000259|PROSITE:PS51091"
FT   DOMAIN          137..180
FT                   /note="Fibronectin type-I"
FT                   /evidence="ECO:0000259|PROSITE:PS51091"
FT   DOMAIN          182..226
FT                   /note="Fibronectin type-I"
FT                   /evidence="ECO:0000259|PROSITE:PS51091"
FT   DOMAIN          227..271
FT                   /note="Fibronectin type-I"
FT                   /evidence="ECO:0000259|PROSITE:PS51091"
FT   DOMAIN          353..401
FT                   /note="Fibronectin type-II"
FT                   /evidence="ECO:0000259|PROSITE:PS51092"
FT   DOMAIN          413..461
FT                   /note="Fibronectin type-II"
FT                   /evidence="ECO:0000259|PROSITE:PS51092"
FT   DOMAIN          466..509
FT                   /note="Fibronectin type-I"
FT                   /evidence="ECO:0000259|PROSITE:PS51091"
FT   DOMAIN          514..556
FT                   /note="Fibronectin type-I"
FT                   /evidence="ECO:0000259|PROSITE:PS51091"
FT   DOMAIN          557..600
FT                   /note="Fibronectin type-I"
FT                   /evidence="ECO:0000259|PROSITE:PS51091"
FT   DOMAIN          608..701
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          719..809
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          810..901
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          908..997
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          998..1087
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1088..1174
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1175..1266
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1268..1360
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1361..1448
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1449..1542
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1543..1634
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1635..1722
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1723..1816
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1817..1903
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1904..1994
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2108..2200
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2207..2251
FT                   /note="Fibronectin type-I"
FT                   /evidence="ECO:0000259|PROSITE:PS51091"
FT   DOMAIN          2252..2294
FT                   /note="Fibronectin type-I"
FT                   /evidence="ECO:0000259|PROSITE:PS51091"
FT   DOMAIN          2296..2336
FT                   /note="Fibronectin type-I"
FT                   /evidence="ECO:0000259|PROSITE:PS51091"
FT   REGION          23..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1392..1412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1392..1406
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        358..384
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT   DISULFID        372..399
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT   DISULFID        418..444
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT   DISULFID        432..459
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ   SEQUENCE   2389 AA;  263051 MW;  6503C7B2932B0150 CRC64;
     MPSSPGWPLL LLALVVGAGA HGEQPRTTKA RRQAQQIAQP PVPSSQNKQG CYDNGRHYQI
     NQQWERTYLG RMLVCTCYGG SRGFNCESKP ELEETCFDKY TGSTHRVGET YERPKDSMIW
     DCTCIGAGRG RIATVAYRCH EGGQSYKIGD TWRRPHETGG YMLECVCLGN GKGEWTCKPV
     AERCYDNTAG TSYVVGETWE KPYQGWMMVD CTCLGEGSGR ITCTSRNRCN DQDTTTSYRI
     GDTWSKKDNR GNLLQCICTG NGRGEWKCER HSAVQTTGIG SGSPTFTDVR TALYQPQPQP
     PPYGHCVTDS GVVYSIGMKW LKTQGSQQML CTCLGNGVSC QETAVTQTYG GNSNGEPCVL
     PFTYGGRTFY SCTTEGRSDG HLWCSTTSNF EQDNKYSFCT EQNVLVQTRG GNSNGALCHF
     PFLYNNRNYT DCTSEGRRDN MKWCGTTQNY DADQKFGFCP MAAHEEICTT NEGVMYRVGD
     HWDKQHDMGH MMKCTCVGNG RGEWTCIAYS QLRDQCIVDG ITYDVNQTFH KRHEEGHMLN
     CTCFGQGRGR WKCDPVDQCQ DSESRTFYQI GDSWEKHVHG VRYQCYCYGR GIGEWHCQPL
     QAFPGATGPV QVIITESGSH PNSHPIQWNA PETSHISQYI LRWRPKNKRA LWKEAIIPGH
     LNSYTISGLK PGVQYEGQLV SVQQYGPKEV TRFDFTTTHI TPISTNTLSG ETTPFSPVVA
     TSESVTEITA SSFVVSWVSA SDTVSGFRVE YELSEEGAEP QYLDLPSTAT SVNIPDLLPG
     RKYIVNVYQI SEEGEQNLIL STSQTTETAP DAPPEHNVDR VDDTSIVVSW SRPQAPITGY
     RIVYTPSMEG SSTELNLPDT ATSVTLSDLM PGVQYNITIY AVEENQESTP VFIQQETTGV
     PQKDDVPSPK DLQFVEVSDV KITIIWTPPS STVSGYRVDV IPVNRPGVHG QKLPVTRNYF
     AEVTDLLPGT TYLFKVFTVL QGRESKPLTG EHTTKLDAPT NLRFENLTDS AVLVAWTPPR
     APITGYQLTA GPTRGGQPKQ YNVVPSATNY QLKNLQPGSE YTVYLVALKG NQQSNRQTGI
     FTTLQPMSSI PPYSTEVTET SIVVTWTPAP RIGFKLGVRP SQGGEAPREV TSESGSIVIS
     GLTPGVEYVY SISVLMDGQD RDTPIVKRVT TPLSPPTNLH LEPNPDTGIL TVSWDRSTTP
     GVTGYRVTTV PTSGQQGYTL EEVVSAEQTS CIFENLSPGL EYNVSVYSVQ DNKESIPISK
     TITQAVPAPT DLRFTNVRPD TMRVTWTPPV SIELTSFLVR YSPVKKEDDV AELTISPSDN
     MVVLTNLLPG TEYLVKVYSV YEQHESTALT GVQKTGLDSP TGIDFSDITA NSFTVHWIAP
     RAAITGSKIR HHLEQGGGRP KEDRVPPSRN SITLTNLVPG SEYVVSIIAV NGKEESLPLV
     GQQTTVSDVP RDVEVTATGP TSLVISWDAP AVTVRYYRIT YGETGGSGPI QEFTVPGTSS
     TATISDLKPG ADYTITMYAV TGRGDSPASS KPVTVTYKTE IDTPSQLQVT DVQDNSISVR
     WLPSTSPVTG YRVTTVPKDG HGPVKSKNVP ADQTQTTIEG LQPTVEYVVS VYAQSQNGES
     LPLVETAITN IDRPRGLTFT EVDVDSIKIA WESPQGQVTS YRVTYSSPED GIRELVPAPD
     GEDDTAELHG LRPGSEYTVT IVALHDDLES QPLTGTQSTA IPPPTNLQFV QVTPTSLKVN
     WNAPSVRLTG YRVRVNPKEK TGPMKEINLS PDSTFAVVSG LMVATKYEVS VYALKDSLTS
     TPAHGVVTTL ENISPPRRAR VTDATETTIT ITWRTKTETI TGFQVEAVPA DGQSPIQRTI
     TPDVRTYTIT GLQPGTDYKI YLYTMNENAR SSPFVIDAST AIDAPSNLRF LTTTSNSQLI
     TWQPPRAQIT GYIIKYERPG AQPKELIPRP RAGTTEATLT GLEPGIEYTI YIIAVKNAQK
     SEPLVGRKKT DELPKLVTLP HPNQGGPEIL DVPSTVERTP YLTNRFDNGN GIQLPGTSGQ
     QTLGNQGQQV FFEEHGFRRT TAPTTATPIR HRPGLQTPDV DEEIDLGNRY SIQRVDLVQP
     SFPHSLGPRR NDTTGQEALS QTTISWRPLL ESTEYVISCQ PVGTDEEPLQ FRVPGTSSSA
     TLTGLTRGAT YNIIVEALKD RRRHKVLEEV VTVGNAVSEG VNQPSDDTCY DTYTGSFYSI
     GEEWERLSDT GFKLWCQCLG FGSGHFRCDS SKWCHDNGVS YKIGEKWDRQ GETGQMMSCT
     CLGNGKGEFK CDPHEATCYD DGKMYHVGEQ WQKEYLGAIC SCTCYGGQQG WRCDNCRRPG
     AEAAPDGTAG HSYTQFSQRY HQSTNTNVNC PIECFMPLDV QADRQHRPG
//
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