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FINC_RAT
ID   FINC_RAT                Reviewed;        2477 AA.
AC   P04937; Q6LDX9;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   03-AUG-2022, entry version 188.
DE   RecName: Full=Fibronectin {ECO:0000305};
DE            Short=FN;
DE   Contains:
DE     RecName: Full=Anastellin;
DE   Flags: Precursor;
GN   Name=Fn1 {ECO:0000312|RGD:2624};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Fischer; TISSUE=Liver;
RX   PubMed=2445560; DOI=10.1002/j.1460-2075.1987.tb02547.x;
RA   Scwarzbauer J.E., Patel R.S., Fonda D., Hynes R.O.;
RT   "Multiple sites of alternative splicing of the rat fibronectin gene
RT   transcript.";
RL   EMBO J. 6:2573-2580(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-139 AND 2382-2477.
RC   STRAIN=Fischer; TISSUE=Liver;
RX   PubMed=3119323; DOI=10.1002/j.1460-2075.1987.tb02545.x;
RA   Patel R.S., Odermatt E., Schwarzbauer J.E., Hynes R.O.;
RT   "Organization of the fibronectin gene provides evidence for exon shuffling
RT   during evolution.";
RL   EMBO J. 6:2565-2572(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1586-2477.
RX   PubMed=6317187; DOI=10.1016/0092-8674(83)90175-7;
RA   Schwarzbauer J.E., Tamkun J.W., Lemischka I.R., Hynes R.O.;
RT   "Three different fibronectin mRNAs arise by alternative splicing within the
RT   coding region.";
RL   Cell 35:421-431(1983).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1722-1810, AND ALTERNATIVE SPLICING.
RX   PubMed=3863113; DOI=10.1073/pnas.82.19.6571;
RA   Odermatt E., Tamkun J.W., Hynes R.O.;
RT   "Repeating modular structure of the fibronectin gene: relationship to
RT   protein structure and subunit variation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:6571-6575(1985).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2052-2237, AND ALTERNATIVE SPLICING.
RX   PubMed=6089177; DOI=10.1073/pnas.81.16.5140;
RA   Tamkun J.W., Schwarzbauer J.E., Hynes R.O.;
RT   "A single rat fibronectin gene generates three different mRNAs by
RT   alternative splicing of a complex exon.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:5140-5144(1984).
RN   [6]
RP   PROTEIN SEQUENCE OF 1183-1192; 1385-1399 AND 2287-2300, AND INTERACTION
RP   WITH AMBP.
RX   PubMed=7519849; DOI=10.1042/bj3010745;
RA   Falkenberg C., Enghild J.J., Thoegersen I.B., Salvesen G., Aakerstroem B.;
RT   "Isolation and characterization of fibronectin-alpha 1-microglobulin
RT   complex in rat plasma.";
RL   Biochem. J. 301:745-751(1994).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285 AND SER-2475, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [8]
RP   CLEAVAGE OF SIGNAL PEPTIDE AFTER CYS-24, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=26479776; DOI=10.1021/acs.jproteome.5b00820;
RA   Tsuchiya T., Osaki T., Minamino N., Sasaki K.;
RT   "Peptidomics for studying limited proteolysis.";
RL   J. Proteome Res. 14:4921-4931(2015).
CC   -!- FUNCTION: Fibronectins bind cell surfaces and various compounds
CC       including collagen, fibrin, heparin, DNA, and actin. Fibronectins are
CC       involved in cell adhesion, cell motility, opsonization, wound healing,
CC       and maintenance of cell shape (By similarity). Involved in osteoblast
CC       compaction through the fibronectin fibrillogenesis cell-mediated matrix
CC       assembly process, essential for osteoblast mineralization. Participates
CC       in the regulation of type I collagen deposition by osteoblasts (By
CC       similarity). {ECO:0000250|UniProtKB:P02751,
CC       ECO:0000250|UniProtKB:P11276}.
CC   -!- FUNCTION: [Anastellin]: Binds fibronectin and induces fibril formation.
CC       This fibronectin polymer, named superfibronectin, exhibits enhanced
CC       adhesive properties. Both anastellin and superfibronectin inhibit tumor
CC       growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and
CC       inhibits lysophospholipid signaling. {ECO:0000250|UniProtKB:P02751}.
CC   -!- SUBUNIT: Mostly heterodimers or multimers of alternatively spliced
CC       variants, connected by 2 disulfide bonds near the carboxyl ends; to a
CC       lesser extent homodimers. Interacts with FBLN1, AMBP, TNR, LGALS3BP and
CC       COL13A1. Interacts with FBLN7 (By similarity). Interacts with COMP.
CC       Interacts (via type III repeats 9-14) with TNFAIP6 (via CUB domain);
CC       this interaction enhances fibronectin fibril assembly. TNFAIP6 may act
CC       as a bridging molecule between FN1 and THBS1 (By similarity). Interacts
CC       with TNR; the interaction inhibits cell adhesion and neurite outgrowth
CC       (By similarity). Interacts with FST3 and MYOC (By similarity).
CC       {ECO:0000250, ECO:0000250|UniProtKB:P02751}.
CC   -!- INTERACTION:
CC       P04937; P34901: Sdc4; NbExp=2; IntAct=EBI-6127274, EBI-1173182;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=A number of isoforms are produced. The diversity of isoforms
CC         depends on the V region and either of the two extra domain which can
CC         be either included or excluded (partially or completely for the V
CC         region). {ECO:0000305};
CC       Name=1;
CC         IsoId=P04937-1; Sequence=Displayed;
CC       Name=2; Synonyms=FNIII-13-less;
CC         IsoId=P04937-2; Sequence=VSP_003258;
CC       Name=3; Synonyms=Lambda-RLF4-5;
CC         IsoId=P04937-3; Sequence=VSP_003259;
CC       Name=4; Synonyms=Lambda-RLF6;
CC         IsoId=P04937-4; Sequence=VSP_003260;
CC   -!- TISSUE SPECIFICITY: Plasma FN (soluble dimeric form) is secreted by
CC       hepatocytes. Cellular FN (dimeric or cross-linked multimeric forms),
CC       made by fibroblasts, epithelial and other cell types, is deposited as
CC       fibrils in the extracellular matrix.
CC   -!- PTM: Sulfated. {ECO:0000250|UniProtKB:P02751}.
CC   -!- PTM: Forms covalent cross-links mediated by a transglutaminase, such as
CC       F13A or TGM2, between a glutamine and the epsilon-amino group of a
CC       lysine residue, forming homopolymers and heteropolymers (e.g.
CC       fibrinogen-fibronectin, collagen-fibronectin heteropolymers).
CC       {ECO:0000250|UniProtKB:P11276}.
CC   -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC       {ECO:0000250|UniProtKB:P02751}.
CC   -!- PTM: Proteolytic processing produces the C-terminal NC1 peptide,
CC       anastellin. {ECO:0000250|UniProtKB:P02751}.
CC   -!- PTM: Some lysine residues are oxidized to allysine by LOXL3, promoting
CC       fibronectin activation and matrix formation.
CC       {ECO:0000250|UniProtKB:P11276}.
CC   -!- PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia.
CC       {ECO:0000250|UniProtKB:P07589}.
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DR   EMBL; X15906; CAA34020.1; -; mRNA.
DR   EMBL; L29191; AAA41166.1; -; Genomic_DNA.
DR   EMBL; L00191; AAA41166.1; JOINED; Genomic_DNA.
DR   EMBL; L29191; AAA41167.1; -; Genomic_DNA.
DR   EMBL; L00191; AAA41167.1; JOINED; Genomic_DNA.
DR   EMBL; L29191; AAA41168.1; -; Genomic_DNA.
DR   EMBL; L00191; AAA41168.1; JOINED; Genomic_DNA.
DR   EMBL; M11750; AAA41170.1; -; Genomic_DNA.
DR   EMBL; X05831; CAA29278.1; -; Genomic_DNA.
DR   EMBL; X05832; CAA29279.1; -; Genomic_DNA.
DR   EMBL; X05833; CAA29280.1; -; Genomic_DNA.
DR   EMBL; X05834; CAA29281.1; -; Genomic_DNA.
DR   PIR; S14428; S14428.
DR   AlphaFoldDB; P04937; -.
DR   SMR; P04937; -.
DR   IntAct; P04937; 3.
DR   MINT; P04937; -.
DR   STRING; 10116.ENSRNOP00000019772; -.
DR   CarbonylDB; P04937; -.
DR   GlyGen; P04937; 9 sites.
DR   iPTMnet; P04937; -.
DR   PhosphoSitePlus; P04937; -.
DR   jPOST; P04937; -.
DR   PaxDb; P04937; -.
DR   PeptideAtlas; P04937; -.
DR   PRIDE; P04937; -.
DR   ABCD; P04937; 2 sequenced antibodies.
DR   UCSC; RGD:2624; rat. [P04937-1]
DR   RGD; 2624; Fn1.
DR   eggNOG; ENOG502QPTS; Eukaryota.
DR   InParanoid; P04937; -.
DR   PhylomeDB; P04937; -.
DR   Reactome; R-RNO-114608; Platelet degranulation.
DR   Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-RNO-1474244; Extracellular matrix organization.
DR   Reactome; R-RNO-1566977; Fibronectin matrix formation.
DR   Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR   Reactome; R-RNO-2129379; Molecules associated with elastic fibres.
DR   Reactome; R-RNO-216083; Integrin cell surface interactions.
DR   Reactome; R-RNO-3000170; Syndecan interactions.
DR   Reactome; R-RNO-3000171; Non-integrin membrane-ECM interactions.
DR   Reactome; R-RNO-3000178; ECM proteoglycans.
DR   Reactome; R-RNO-354192; Integrin signaling.
DR   Reactome; R-RNO-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR   Reactome; R-RNO-372708; p130Cas linkage to MAPK signaling for integrins.
DR   Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-RNO-5674135; MAP2K and MAPK activation.
DR   Reactome; R-RNO-8874081; MET activates PTK2 signaling.
DR   Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR   Reactome; R-RNO-9634597; GPER1 signaling.
DR   PRO; PR:P04937; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR   GO; GO:0005604; C:basement membrane; IDA:RGD.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:RGD.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISO:RGD.
DR   GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR   GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0005577; C:fibrinogen complex; ISO:RGD.
DR   GO; GO:0051087; F:chaperone binding; ISO:RGD.
DR   GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
DR   GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; TAS:RGD.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0005178; F:integrin binding; ISO:RGD.
DR   GO; GO:0045340; F:mercury ion binding; IDA:RGD.
DR   GO; GO:0016504; F:peptidase activator activity; ISO:RGD.
DR   GO; GO:0002020; F:protease binding; IPI:RGD.
DR   GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR   GO; GO:0043394; F:proteoglycan binding; ISO:RGD.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR   GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0051702; P:biological process involved in interaction with symbiont; ISO:RGD.
DR   GO; GO:0072378; P:blood coagulation, fibrin clot formation; IBA:GO_Central.
DR   GO; GO:0007161; P:calcium-independent cell-matrix adhesion; ISO:RGD.
DR   GO; GO:0001775; P:cell activation; IMP:RGD.
DR   GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR   GO; GO:0007160; P:cell-matrix adhesion; IMP:RGD.
DR   GO; GO:0007044; P:cell-substrate junction assembly; ISO:RGD.
DR   GO; GO:1904646; P:cellular response to amyloid-beta; IEP:RGD.
DR   GO; GO:1904385; P:cellular response to angiotensin; IEP:RGD.
DR   GO; GO:0071773; P:cellular response to BMP stimulus; IEP:RGD.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR   GO; GO:0071347; P:cellular response to interleukin-1; IMP:RGD.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:0071288; P:cellular response to mercury ion; IDA:RGD.
DR   GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEP:RGD.
DR   GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IEP:RGD.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD.
DR   GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IEP:RGD.
DR   GO; GO:0035987; P:endodermal cell differentiation; ISO:RGD.
DR   GO; GO:0030198; P:extracellular matrix organization; IMP:RGD.
DR   GO; GO:0008347; P:glial cell migration; IDA:RGD.
DR   GO; GO:0007507; P:heart development; IBA:GO_Central.
DR   GO; GO:0033622; P:integrin activation; ISO:RGD.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:RGD.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR   GO; GO:0032966; P:negative regulation of collagen biosynthetic process; IMP:RGD.
DR   GO; GO:0150102; P:negative regulation of monocyte activation; ISO:RGD.
DR   GO; GO:0071635; P:negative regulation of transforming growth factor beta production; ISO:RGD.
DR   GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR   GO; GO:1901166; P:neural crest cell migration involved in autonomic nervous system development; ISO:RGD.
DR   GO; GO:0001503; P:ossification; TAS:RGD.
DR   GO; GO:0018149; P:peptide cross-linking; ISO:RGD.
DR   GO; GO:0070527; P:platelet aggregation; IBA:GO_Central.
DR   GO; GO:0045773; P:positive regulation of axon extension; ISO:RGD.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:0050921; P:positive regulation of chemotaxis; IDA:RGD.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:RGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR   GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR   GO; GO:1904237; P:positive regulation of substrate-dependent cell migration, cell attachment to substrate; ISO:RGD.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:RGD.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
DR   GO; GO:0014823; P:response to activity; IEP:RGD.
DR   GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR   GO; GO:0010039; P:response to iron ion; IEP:RGD.
DR   GO; GO:0002931; P:response to ischemia; IEP:RGD.
DR   GO; GO:0010193; P:response to ozone; IEP:RGD.
DR   GO; GO:0009611; P:response to wounding; IEP:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:RGD.
DR   GO; GO:0042060; P:wound healing; ISO:RGD.
DR   CDD; cd00061; FN1; 12.
DR   CDD; cd00062; FN2; 2.
DR   CDD; cd00063; FN3; 17.
DR   Gene3D; 2.10.10.10; -; 2.
DR   Gene3D; 2.60.40.10; -; 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   Pfam; PF00039; fn1; 11.
DR   Pfam; PF00040; fn2; 2.
DR   Pfam; PF00041; fn3; 17.
DR   SMART; SM00058; FN1; 12.
DR   SMART; SM00059; FN2; 2.
DR   SMART; SM00060; FN3; 17.
DR   SUPFAM; SSF49265; SSF49265; 11.
DR   SUPFAM; SSF57440; SSF57440; 2.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01253; FN1_1; 12.
DR   PROSITE; PS51091; FN1_2; 12.
DR   PROSITE; PS00023; FN2_1; 2.
DR   PROSITE; PS51092; FN2_2; 2.
DR   PROSITE; PS50853; FN3; 17.
PE   1: Evidence at protein level;
KW   Acute phase; Alternative splicing; Angiogenesis; Cell adhesion; Cell shape;
KW   Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW   Glycoprotein; Heparin-binding; Isopeptide bond; Oxidation; Phosphoprotein;
KW   Reference proteome; Repeat; Secreted; Signal; Sulfation.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:26479776"
FT   CHAIN           25..2477
FT                   /note="Fibronectin"
FT                   /id="PRO_0000019237"
FT   CHAIN           627..701
FT                   /note="Anastellin"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000390481"
FT   DOMAIN          51..91
FT                   /note="Fibronectin type-I 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          96..139
FT                   /note="Fibronectin type-I 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          140..183
FT                   /note="Fibronectin type-I 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          185..229
FT                   /note="Fibronectin type-I 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          230..274
FT                   /note="Fibronectin type-I 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          306..345
FT                   /note="Fibronectin type-I 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          355..403
FT                   /note="Fibronectin type-II 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478,
FT                   ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DOMAIN          415..463
FT                   /note="Fibronectin type-II 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478,
FT                   ECO:0000255|PROSITE-ProRule:PRU00479"
FT   DOMAIN          468..511
FT                   /note="Fibronectin type-I 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          516..558
FT                   /note="Fibronectin type-I 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          559..602
FT                   /note="Fibronectin type-I 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          610..717
FT                   /note="Fibronectin type-III 1"
FT   DOMAIN          721..811
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT                   ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT                   ProRule:PRU00479"
FT   DOMAIN          812..901
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT                   ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT                   ProRule:PRU00479"
FT   DOMAIN          908..997
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT                   ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT                   ProRule:PRU00479"
FT   DOMAIN          998..1087
FT                   /note="Fibronectin type-III 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT                   ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT                   ProRule:PRU00479"
FT   DOMAIN          1088..1174
FT                   /note="Fibronectin type-III 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT                   ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT                   ProRule:PRU00479"
FT   DOMAIN          1175..1269
FT                   /note="Fibronectin type-III 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT                   ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT                   ProRule:PRU00479"
FT   DOMAIN          1270..1358
FT                   /note="Fibronectin type-III 8; extra domain B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT                   ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT                   ProRule:PRU00479"
FT   DOMAIN          1359..1451
FT                   /note="Fibronectin type-III 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT                   ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT                   ProRule:PRU00479"
FT   DOMAIN          1452..1539
FT                   /note="Fibronectin type-III 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1540..1633
FT                   /note="Fibronectin type-III 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1634..1725
FT                   /note="Fibronectin type-III 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1726..1813
FT                   /note="Fibronectin type-III 13; extra domain A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316,
FT                   ECO:0000255|PROSITE-ProRule:PRU00478, ECO:0000255|PROSITE-
FT                   ProRule:PRU00479"
FT   DOMAIN          1814..1907
FT                   /note="Fibronectin type-III 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1908..1994
FT                   /note="Fibronectin type-III 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1995..2085
FT                   /note="Fibronectin type-III 16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          2193..2286
FT                   /note="Fibronectin type-III 17"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          2294..2338
FT                   /note="Fibronectin type-I 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          2339..2381
FT                   /note="Fibronectin type-I 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DOMAIN          2383..2426
FT                   /note="Fibronectin type-I 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT   DNA_BIND        906..1171
FT   REGION          53..273
FT                   /note="Fibrin- and heparin-binding 1"
FT   REGION          308..608
FT                   /note="Collagen-binding"
FT   REGION          1357..1630
FT                   /note="Cell-attachment"
FT   REGION          1661..1685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1811..2081
FT                   /note="Heparin-binding 2"
FT   REGION          2082..2201
FT                   /note="V region (type III connecting segment, IIICS)"
FT   REGION          2296..2427
FT                   /note="Fibrin-binding 2"
FT   MOTIF           1614..1616
FT                   /note="Cell attachment site"
FT   MOTIF           2181..2183
FT                   /note="Cell attachment site"
FT   MOD_RES         285
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         875
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         880
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2392
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2454
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P02751"
FT   MOD_RES         2475
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CARBOHYD        430
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        528
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        542
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        876
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1006
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1243
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1290
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2154
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        2198
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        53..79
FT                   /evidence="ECO:0000250"
FT   DISULFID        77..88
FT                   /evidence="ECO:0000250"
FT   DISULFID        98..126
FT                   /evidence="ECO:0000250"
FT   DISULFID        124..136
FT                   /evidence="ECO:0000250"
FT   DISULFID        142..170
FT                   /evidence="ECO:0000250"
FT   DISULFID        168..180
FT                   /evidence="ECO:0000250"
FT   DISULFID        187..216
FT                   /evidence="ECO:0000250"
FT   DISULFID        214..226
FT                   /evidence="ECO:0000250"
FT   DISULFID        232..261
FT                   /evidence="ECO:0000250"
FT   DISULFID        259..271
FT                   /evidence="ECO:0000250"
FT   DISULFID        308..335
FT                   /evidence="ECO:0000250"
FT   DISULFID        333..342
FT                   /evidence="ECO:0000250"
FT   DISULFID        360..386
FT                   /evidence="ECO:0000250"
FT   DISULFID        374..401
FT                   /evidence="ECO:0000250"
FT   DISULFID        420..446
FT                   /evidence="ECO:0000250"
FT   DISULFID        434..461
FT                   /evidence="ECO:0000250"
FT   DISULFID        470..498
FT                   /evidence="ECO:0000250"
FT   DISULFID        496..508
FT                   /evidence="ECO:0000250"
FT   DISULFID        518..545
FT                   /evidence="ECO:0000250"
FT   DISULFID        543..555
FT                   /evidence="ECO:0000250"
FT   DISULFID        561..589
FT                   /evidence="ECO:0000250"
FT   DISULFID        587..599
FT                   /evidence="ECO:0000250"
FT   DISULFID        2296..2325
FT                   /evidence="ECO:0000250"
FT   DISULFID        2323..2335
FT                   /evidence="ECO:0000250"
FT   DISULFID        2341..2368
FT                   /evidence="ECO:0000250"
FT   DISULFID        2366..2378
FT                   /evidence="ECO:0000250"
FT   DISULFID        2385..2411
FT                   /evidence="ECO:0000250"
FT   DISULFID        2409..2420
FT                   /evidence="ECO:0000250"
FT   DISULFID        2458
FT                   /note="Interchain (with C-2462)"
FT   DISULFID        2462
FT                   /note="Interchain (with C-2458)"
FT   CROSSLNK        35
FT                   /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT                   with K-?)"
FT                   /evidence="ECO:0000250|UniProtKB:P11276"
FT   CROSSLNK        36
FT                   /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT                   with K-?)"
FT                   /evidence="ECO:0000250|UniProtKB:P11276"
FT   CROSSLNK        48
FT                   /note="Isoglutamyl lysine isopeptide (Gln-Lys) (interchain
FT                   with K-?)"
FT                   /evidence="ECO:0000250|UniProtKB:P11276"
FT   VAR_SEQ         1720..1809
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003258"
FT   VAR_SEQ         2082..2200
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003260"
FT   VAR_SEQ         2082..2106
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_003259"
FT   CONFLICT        2318
FT                   /note="G -> A (in Ref. 3; AAA41166/AAA41167/AAA41168)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2477 AA;  272511 MW;  B4391A472ECEDEB5 CRC64;
     MLRGPGPGRL LLLAVLCLGT SVRCTETGKS KRQAQQIVQP PSPVAVSQSK PGCFDNGKHY
     QINQQWERTY LGNALVCTCY GGSRGFNCES KPEPEETCFD KYTGNTYKVG DTYERPKDSM
     IWDCTCIGAG RGRISCTIAN RCHEGGQSYK IGDKWRRPHE TGGYMLECLC LGNGKGEWTC
     KPIAEKCFDH AAGTSYVVGE TWEKPYQGWM MVDCTCLGEG NGRITCTSRN RCNDQDTRTS
     YRIGDTWSKK DNRGNLLQCV CTGNGRGEWK CERHVLQSAS AGSGSFTDVR TAIYQPQTHP
     QPAPYGHCVT DSGVVYSVGM QWLKSQGDKQ MLCTCLGNGV SCQETAVTQT YGGNSNGEPC
     VLPFHYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF CTDHAVLVQT RGGNSNGALC
     HFPFLYSNRN YSDCTSEGRR DNMKWCGTTQ NYDADQKFGF CPMAAHEEIC TTNEGVMYRI
     GDQWDKQHDL GHMMRCTCVG NGRGQWACIP YSQLRDQCIV DDITYNVNDT FHKRHEEGHM
     LNCTCFGQGR GRWKCDPIDR CQDSETRTFY QIGDSWEKFV HGVRYQCYCY GRGIGEWHCQ
     PLQTYPGTTG PVQVIITETP SQPNSHPIQW NAPEPSHITK YILRWRPKTS TGRWKEATIP
     GHLNSYTIKG LTPGVIYEGQ LISIQQYGHQ EVTRFDFTTS ASTPVTSNTV TGETAPFSPV
     VATSESVTEI TASSFVVSWV SASDTVSGFR VEYELSEEGD EPQYLDLPST ATSVNIPDLL
     PGRKYIVNVY QISEEGKQSL ILSTSQTTAP DAPPDPTVDQ VDDTSIVVRW SRPQAPITGY
     RIVYSPSVEG SSTELNLPET ANSVTLSDLQ PGVQYNITIY AVEENQESTP VFIQQETTGV
     PRSDDVPAPK DLQFVEVTDV KVTIMWTPPN SAVTGYRVDV LPVNLPGEHG QRLPVNRNTF
     AEVTGLSPGV TYLFKVFAVH QGRESKPLTA QQTTKLDAPT NLQFVNETDR TVLVTWTPPR
     ARIAGYRLTV GLTRGGQPKQ YNVGPMASKY PLRNLQPGSE YTVTLMAVKG NQQSPKATGV
     FTTLQPLRSI PPYNTEVTET TIVITWTPAP RIGFKLGVRP SQGGEAPREV TSDSGSIVVS
     GLTPGVEYTY TIQVLRDGQE RDAPIVNRVV TPLSPPTNLH LEANPDTGVL TVSWERSTTP
     DITGYRITTT PTNGQQGTAL EEVVHADQSS CTFENRNPGL EYNVSVYTVK DDKESAPISD
     TVIPEVPQLT DLSFVDITDS SIGLRWTPLN SSTIIGYRIT VVAAGEGIPI FEDFVDSSVG
     YYTVTGLEPG IDYDISVITL INGGESAPTT LTQQTAVPPP TDLRFTNIGP DTMRVTWAPP
     PSIELTNLLV RYSPVKNEED VAELSISPSD NAVVLTNLLP GTEYLVSVSS VYEQHESIPL
     RGRQKTGLDS PTGFDSSDVT ANSFTVHWVA PRAPITGYII RHHAEHSAGR PRQDRVPPSR
     NSITLTNLNP GTEYIVTIIA VNGREESPPL IGQQSTVSDV PRDLEVIAST PTSLLISWEP
     PAVSVRYYRI TYGETGGNSP VQEFTVPGSK STATINNIKP GADYTITLYA VTGRGDSPAS
     SKPVSINYQT EIDKPSQMQV TDVQDNSISV RWLPSTSPVT GYRVTTAPKN GLGPTKSQTV
     SPDQTEMTIE GLQPTVEYVV SVYAQNRNGE SQPLVQTAVT NIDRPKGLAF TDVDVDSIKI
     AWESPQGQVS RYRVTYSSPE DGIHELFPAP DGDEDTAELH GLRPGSEYTV SVVALHGGME
     SQPLIGVQST AIPAPTNLKF TQVSPTTLTA QWTAPSVKLT GYRVRVTPKE KTGPMKEINL
     SPDSTSVIVS GLMVATKYEV SVYALKDTLT SRPAQGVVTT LENVSPPRRA RVTDATETTI
     TISWRTKTET ITGFQVDAIP ANGQTPVQRT ISPDVRSYTI TGLQPGTDYK IHLYTLNDNA
     RSSPVVIDAS TAIDAPSNLR FLTTTPNSLL VSWQAPRARI TGYIIKYEKP GSPPREVVPR
     PRPGVTEATI TGLEPGTEYT IYVIALKNNQ KSEPLIGRKK TDELPQLVTL PHPNLHGPEI
     LDVPSTVQKT PFVTNPGYDT ENGIQLPGTS HQQPSVGQQM IFEEHGFRRT TPPTAATPVR
     LRPRPYLPNV DEEVQIGHVP RGDVDYHLYP HVPGLNPNAS TGQEALSQTT ISWTPFQESS
     EYIISCQPVG TDEEPLQFQV PGTSTSATLT GLTRGVTYNI IVEALHNQRR HKVREEVVTV
     GNTVNEGLNQ PTDDSCFDPY TVSHYAVGEE WERLSDSGFK LTCQCLGFGS GHFRCDSSKW
     CHDNGVNYKI GEKWDRQGEN GQRMSCTCLG NGKGEFKCDP HEATCYDDGK TYHVGEQWQK
     EYLGAICSCT CFGGQRGWRC DNCRRPGAAE PSPDGTTGHT YNQYTQRYHQ RTNTNVNCPI
     ECFMPLDVQA DRDDSRE
 
 
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