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Integrin alpha-4 (CD49 antigen-like family member D) (Integrin alpha-IV) (VLA-4 subunit alpha) (CD antigen CD49d)

 ITA4_HUMAN              Reviewed;        1032 AA.
P13612; D3DPG4; Q7Z4L6;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 3.
27-SEP-2017, entry version 185.
RecName: Full=Integrin alpha-4;
AltName: Full=CD49 antigen-like family member D;
AltName: Full=Integrin alpha-IV;
AltName: Full=VLA-4 subunit alpha;
AltName: CD_antigen=CD49d;
Flags: Precursor;
Name=ITGA4; Synonyms=CD49D;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2788572;
Takada Y., Elices M.J., Crouse C., Hemler M.E.;
"The primary structure of the alpha 4 subunit of VLA-4: homology to
other integrins and a possible cell-cell adhesion function.";
EMBO J. 8:1361-1368(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1551405; DOI=10.1002/eji.1830220434;
Rubio M., Nueda A., Vara A., Corbi-Lopez A.L.;
"A single mRNA encodes the alpha 150 and alpha 80/70 forms of the
alpha subunit of VLA4.";
Eur. J. Immunol. 22:1099-1102(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLN-878.
PubMed=8643114; DOI=10.1016/0161-5890(96)00001-6;
Szabo M.C., McIntyre B.W.;
"Identification of two variants of the human integrin alpha 4
subunit.";
Mol. Immunol. 32:1453-1454(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-878.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-87 (ISOFORM 1).
PubMed=2034655; DOI=10.1073/pnas.88.10.4094;
Rosen G.D., Birkenmeier T.M., Dean D.C.;
"Characterization of the alpha 4 integrin gene promoter.";
Proc. Natl. Acad. Sci. U.S.A. 88:4094-4098(1991).
[8]
PROTEIN SEQUENCE OF 34-47.
PubMed=3033641; DOI=10.1073/pnas.84.10.3239;
Takada Y., Strominger J.L., Hemler M.E.;
"The very late antigen family of heterodimers is part of a superfamily
of molecules involved in adhesion and embryogenesis.";
Proc. Natl. Acad. Sci. U.S.A. 84:3239-3243(1987).
[9]
PROTEIN SEQUENCE OF 592-601, PROTEOLYTIC PROCESSING, AND MUTAGENESIS
OF LYS-590 AND ARG-591.
PubMed=1730718;
Teixido J., Parker C.M., Kassner P.D., Hemler M.E.;
"Functional and structural analysis of VLA-4 integrin alpha 4 subunit
cleavage.";
J. Biol. Chem. 267:1786-1791(1992).
[10]
DOMAIN, AND INTERACTION WITH CSPG4.
PubMed=9488735; DOI=10.1074/jbc.273.10.5955;
Iida J., Meijne A.M.L., Oegema T.R. Jr., Yednock T.A., Kovach N.L.,
Furcht L.T., McCarthy J.B.;
"A role of chondroitin sulfate glycosaminoglycan binding site in
alpha4beta1 integrin-mediated melanoma cell adhesion.";
J. Biol. Chem. 273:5955-5962(1998).
[11]
INTERACTION WITH PXN; LPXN AND TGFB1I1, AND MUTAGENESIS OF TYR-1024.
PubMed=10604475; DOI=10.1038/45264;
Liu S., Thomas S.M., Woodside D.G., Rose D.M., Kiosses W.B., Pfaff M.,
Ginsberg M.H.;
"Binding of paxillin to alpha4 integrins modifies integrin-dependent
biological responses.";
Nature 402:676-681(1999).
[12]
PHOSPHORYLATION AT SER-1021, AND MUTAGENESIS OF SER-1021.
PubMed=11533025; DOI=10.1074/jbc.M102665200;
Han J., Liu S., Rose D.M., Schlaepfer D.D., McDonald H.,
Ginsberg M.H.;
"Phosphorylation of the integrin alpha 4 cytoplasmic domain regulates
paxillin binding.";
J. Biol. Chem. 276:40903-40909(2001).
[13]
FUNCTION, AND MUTAGENESIS OF THR-222 AND GLY-223.
PubMed=18635536; DOI=10.1074/jbc.M804835200;
Saegusa J., Akakura N., Wu C.Y., Hoogland C., Ma Z., Lam K.S.,
Liu F.T., Takada Y.K., Takada Y.;
"Pro-inflammatory secretory phospholipase A2 type IIA binds to
integrins alphavbeta3 and alpha4beta1 and induces proliferation of
monocytic cells in an integrin-dependent manner.";
J. Biol. Chem. 283:26107-26115(2008).
[14]
FUNCTION IN LEUKOCYTE TO ENDOTHELIAL CELLS ADHESION, AND INTERACTION
WITH JAML.
PubMed=19064666; DOI=10.1083/jcb.200805061;
Luissint A.C., Lutz P.G., Calderwood D.A., Couraud P.O.,
Bourdoulous S.;
"JAM-L-mediated leukocyte adhesion to endothelial cells is regulated
in cis by alpha4beta1 integrin activation.";
J. Cell Biol. 183:1159-1173(2008).
[15]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-480; ASN-518; ASN-538 AND
ASN-645.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1021, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
FUNCTION, BINDING TO CX3CL1, AND IDENTIFICATION IN A COMPLEX WITH
CX3CR1 AND CX3CL1.
PubMed=23125415; DOI=10.4049/jimmunol.1200889;
Fujita M., Takada Y.K., Takada Y.;
"Integrins alphavbeta3 and alpha4beta1 act as coreceptors for
fractalkine, and the integrin-binding defective mutant of fractalkine
is an antagonist of CX3CR1.";
J. Immunol. 189:5809-5819(2012).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1021, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
FUNCTION.
PubMed=25398877; DOI=10.1074/jbc.M114.579946;
Fujita M., Zhu K., Fujita C.K., Zhao M., Lam K.S., Kurth M.J.,
Takada Y.K., Takada Y.;
"Proinflammatory secreted phospholipase A2 type IIA (sPLA-IIA) induces
integrin activation through direct binding to a newly identified
binding site (site 2) in integrins alphavbeta3, alpha4beta1, and
alpha5beta1.";
J. Biol. Chem. 290:259-271(2015).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Integrins alpha-4/beta-1 (VLA-4) and alpha-4/beta-7 are
receptors for fibronectin. They recognize one or more domains
within the alternatively spliced CS-1 and CS-5 regions of
fibronectin. They are also receptors for VCAM1. Integrin alpha-
4/beta-1 recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-
4/beta-7 is also a receptor for MADCAM1. It recognizes the
sequence L-D-T in MADCAM1. On activated endothelial cells integrin
VLA-4 triggers homotypic aggregation for most VLA-4-positive
leukocyte cell lines. It may also participate in cytolytic T-cell
interactions with target cells. ITGA4:ITGB1 binds to fractalkine
(CX3CL1) and may act as its coreceptor in CX3CR1-dependent
fractalkine signaling (PubMed:23125415). ITGA4:ITGB1 binds to
PLA2G2A via a site (site 2) which is distinct from the classical
ligand-binding site (site 1) and this induces integrin
conformational changes and enhanced ligand binding to site 1
(PubMed:18635536, PubMed:25398877). {ECO:0000269|PubMed:18635536,
ECO:0000269|PubMed:19064666, ECO:0000269|PubMed:23125415,
ECO:0000269|PubMed:25398877}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha
subunit can sometimes be cleaved into two non-covalently
associated fragments. Alpha-4 associates with either beta-1 or
beta-7. Alpha-4 interacts with PXN, LPXN, and TGFB1I1/HIC5.
Interacts with CSPG4 through CSPG4 chondroitin sulfate
glycosaminoglycan. Interacts with JAML; integrin alpha-4/beta-1
may regulate leukocyte to endothelial cells adhesion by
controlling JAML homodimerization. ITGA4:ITGB1 is found in a
ternary complex with CX3CR1 and CX3CL1 (PubMed:23125415).
{ECO:0000269|PubMed:10604475, ECO:0000269|PubMed:19064666,
ECO:0000269|PubMed:23125415, ECO:0000269|PubMed:9488735}.
-!- INTERACTION:
P05556:ITGB1; NbExp=4; IntAct=EBI-703044, EBI-703066;
P26010:ITGB7; NbExp=6; IntAct=EBI-703044, EBI-702932;
P49023:PXN; NbExp=3; IntAct=EBI-703044, EBI-702209;
O43294:TGFB1I1; NbExp=2; IntAct=EBI-703044, EBI-1051449;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P13612-1; Sequence=Displayed;
Name=2;
IsoId=P13612-2; Sequence=VSP_056612, VSP_056613;
Note=No experimental confirmation available.;
-!- DOMAIN: The SG1 motif is involved in binding to chondroitin
sulfate glycosaminoglycan and cell adhesion.
{ECO:0000269|PubMed:9488735}.
-!- PTM: Phosphorylation on Ser-1027 inhibits PXN binding.
{ECO:0000269|PubMed:11533025}.
-!- SIMILARITY: Belongs to the integrin alpha chain family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB59613.1; Type=Frameshift; Positions=13; Evidence={ECO:0000305};
Sequence=CAA34852.1; Type=Frameshift; Positions=13; Evidence={ECO:0000305};
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EMBL; X16983; CAA34852.1; ALT_FRAME; mRNA.
EMBL; L12002; AAB59613.1; ALT_FRAME; mRNA.
EMBL; AC020595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471058; EAX10985.1; -; Genomic_DNA.
EMBL; CH471058; EAX10987.1; -; Genomic_DNA.
EMBL; BC055419; AAH55419.1; -; mRNA.
CCDS; CCDS42788.1; -. [P13612-1]
CCDS; CCDS82540.1; -. [P13612-2]
PIR; S06046; S06046.
RefSeq; NP_000876.3; NM_000885.5. [P13612-1]
RefSeq; NP_001303241.1; NM_001316312.1. [P13612-2]
UniGene; Hs.440955; -.
UniGene; Hs.72981; -.
PDB; 3V4P; X-ray; 3.15 A; A/C=34-620.
PDB; 3V4V; X-ray; 3.10 A; A/C=34-620.
PDB; 4HKC; X-ray; 2.20 A; B=1003-1032.
PDB; 5C7Z; X-ray; 2.77 A; B=1008-1015.
PDB; 5FPI; X-ray; 2.77 A; B=1008-1015.
PDBsum; 3V4P; -.
PDBsum; 3V4V; -.
PDBsum; 4HKC; -.
PDBsum; 5C7Z; -.
PDBsum; 5FPI; -.
ProteinModelPortal; P13612; -.
SMR; P13612; -.
BioGrid; 109883; 517.
CORUM; P13612; -.
DIP; DIP-34971N; -.
IntAct; P13612; 11.
MINT; MINT-4098849; -.
STRING; 9606.ENSP00000380227; -.
BindingDB; P13612; -.
ChEMBL; CHEMBL278; -.
DrugBank; DB04997; ATL1102.
DrugBank; DB05092; CDP323.
DrugBank; DB05802; MLN-02.
DrugBank; DB00108; Natalizumab.
DrugBank; DB05122; R1295.
DrugBank; DB05468; R411.
DrugBank; DB06822; Tinzaparin.
DrugBank; DB09033; Vedolizumab.
GuidetoPHARMACOLOGY; 2443; -.
iPTMnet; P13612; -.
PhosphoSitePlus; P13612; -.
BioMuta; ITGA4; -.
DMDM; 311033436; -.
EPD; P13612; -.
MaxQB; P13612; -.
PaxDb; P13612; -.
PeptideAtlas; P13612; -.
PRIDE; P13612; -.
DNASU; 3676; -.
Ensembl; ENST00000339307; ENSP00000340149; ENSG00000115232. [P13612-2]
Ensembl; ENST00000397033; ENSP00000380227; ENSG00000115232. [P13612-1]
GeneID; 3676; -.
KEGG; hsa:3676; -.
UCSC; uc002unu.4; human. [P13612-1]
CTD; 3676; -.
DisGeNET; 3676; -.
EuPathDB; HostDB:ENSG00000115232.13; -.
GeneCards; ITGA4; -.
HGNC; HGNC:6140; ITGA4.
HPA; HPA064041; -.
MIM; 192975; gene.
neXtProt; NX_P13612; -.
OpenTargets; ENSG00000115232; -.
PharmGKB; PA29940; -.
eggNOG; ENOG410IPB2; Eukaryota.
eggNOG; ENOG410XTAR; LUCA.
GeneTree; ENSGT00760000118782; -.
HOGENOM; HOG000088626; -.
HOVERGEN; HBG004538; -.
InParanoid; P13612; -.
KO; K06483; -.
OMA; NRRDSWS; -.
OrthoDB; EOG091G011V; -.
PhylomeDB; P13612; -.
TreeFam; TF105391; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-8949275; RUNX3 Regulates Immune Response and Cell Migration.
SignaLink; P13612; -.
SIGNOR; P13612; -.
ChiTaRS; ITGA4; human.
GeneWiki; CD49d; -.
GenomeRNAi; 3676; -.
PRO; PR:P13612; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115232; -.
CleanEx; HS_ITGA4; -.
ExpressionAtlas; P13612; baseline and differential.
Genevisible; P13612; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0034669; C:integrin alpha4-beta7 complex; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0050839; F:cell adhesion molecule binding; IMP:UniProtKB.
GO; GO:0015026; F:coreceptor activity; TAS:UniProtKB.
GO; GO:0001968; F:fibronectin binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:1990405; F:protein antigen binding; IEA:Ensembl.
GO; GO:0030183; P:B cell differentiation; IC:BHF-UCL.
GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
GO; GO:0003366; P:cell-matrix adhesion involved in ameboidal cell migration; IMP:UniProtKB.
GO; GO:0071345; P:cellular response to cytokine stimulus; IEA:Ensembl.
GO; GO:1990771; P:clathrin-dependent extracellular exosome endocytosis; IEA:Ensembl.
GO; GO:0050904; P:diapedesis; IEA:Ensembl.
GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB.
GO; GO:0098657; P:import into cell; IEA:Ensembl.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0050901; P:leukocyte tethering or rolling; IMP:UniProtKB.
GO; GO:0090074; P:negative regulation of protein homodimerization activity; IDA:UniProtKB.
GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; IEA:Ensembl.
GO; GO:2000406; P:positive regulation of T cell migration; IEA:Ensembl.
GO; GO:0043113; P:receptor clustering; IMP:UniProtKB.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:UniProtKB.
InterPro; IPR013517; FG-GAP.
InterPro; IPR013519; Int_alpha_beta-p.
InterPro; IPR000413; Integrin_alpha.
InterPro; IPR013649; Integrin_alpha-2.
InterPro; IPR018184; Integrin_alpha_C_CS.
InterPro; IPR032695; Integrin_dom.
Pfam; PF01839; FG-GAP; 2.
Pfam; PF08441; Integrin_alpha2; 1.
PRINTS; PR01185; INTEGRINA.
SMART; SM00191; Int_alpha; 5.
SUPFAM; SSF69179; SSF69179; 3.
PROSITE; PS51470; FG_GAP; 7.
PROSITE; PS00242; INTEGRIN_ALPHA; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell adhesion;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Integrin; Membrane; Metal-binding; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 33 {ECO:0000269|PubMed:3033641}.
CHAIN 34 1032 Integrin alpha-4.
/FTId=PRO_0000016244.
TOPO_DOM 35 977 Extracellular. {ECO:0000255}.
TRANSMEM 978 1001 Helical. {ECO:0000255}.
TOPO_DOM 1002 1032 Cytoplasmic. {ECO:0000255}.
REPEAT 35 100 FG-GAP 1. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 110 177 FG-GAP 2. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 185 237 FG-GAP 3. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 238 291 FG-GAP 4. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 292 351 FG-GAP 5. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 355 412 FG-GAP 6. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 416 478 FG-GAP 7. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
CA_BIND 314 322 {ECO:0000255}.
CA_BIND 377 385 {ECO:0000255}.
CA_BIND 439 447 {ECO:0000255}.
MOTIF 606 616 SG1.
MOTIF 1003 1007 GFFKR motif.
SITE 591 592 Cleavage.
MOD_RES 1021 1021 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:11533025}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 138 138 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 229 229 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 480 480 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 518 518 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 538 538 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 626 626 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 645 645 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 660 660 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 806 806 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 821 821 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 91 101 {ECO:0000250}.
DISULFID 144 165 {ECO:0000250}.
DISULFID 183 198 {ECO:0000250}.
DISULFID 486 495 {ECO:0000250}.
DISULFID 501 557 {ECO:0000250}.
DISULFID 622 627 {ECO:0000250}.
DISULFID 698 711 {ECO:0000250}.
DISULFID 852 890 {ECO:0000250}.
DISULFID 897 902 {ECO:0000250}.
VAR_SEQ 186 195 DYVKKFGENF -> GSISKYRART (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056612.
VAR_SEQ 196 1032 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056613.
VARIANT 634 634 S -> T (in dbSNP:rs35322532).
/FTId=VAR_047423.
VARIANT 824 824 V -> A (in dbSNP:rs1143675).
/FTId=VAR_047424.
VARIANT 878 878 R -> Q (in dbSNP:rs1143676).
{ECO:0000269|PubMed:8643114,
ECO:0000269|Ref.5}.
/FTId=VAR_003978.
MUTAGEN 222 222 T->A: Blocks binding to PLA2G2A.
{ECO:0000269|PubMed:18635536}.
MUTAGEN 223 223 G->A: Blocks binding to PLA2G2A.
{ECO:0000269|PubMed:18635536}.
MUTAGEN 590 590 K->Q: Abolishes almost completely
cleavage. {ECO:0000269|PubMed:1730718}.
MUTAGEN 591 591 R->L: Abolishes completely cleavage.
{ECO:0000269|PubMed:1730718}.
MUTAGEN 1021 1021 S->A: Abolishes phosphorylation.
{ECO:0000269|PubMed:11533025}.
MUTAGEN 1021 1021 S->D: Reduces PXN binding.
{ECO:0000269|PubMed:11533025}.
MUTAGEN 1024 1024 Y->A: Disrupts PXN binding.
{ECO:0000269|PubMed:10604475}.
STRAND 42 45 {ECO:0000244|PDB:3V4V}.
STRAND 54 61 {ECO:0000244|PDB:3V4V}.
STRAND 64 71 {ECO:0000244|PDB:3V4V}.
STRAND 87 95 {ECO:0000244|PDB:3V4V}.
STRAND 102 104 {ECO:0000244|PDB:3V4V}.
STRAND 127 133 {ECO:0000244|PDB:3V4V}.
STRAND 141 145 {ECO:0000244|PDB:3V4V}.
TURN 152 156 {ECO:0000244|PDB:3V4V}.
STRAND 165 168 {ECO:0000244|PDB:3V4V}.
HELIX 174 176 {ECO:0000244|PDB:3V4V}.
STRAND 178 180 {ECO:0000244|PDB:3V4V}.
TURN 193 197 {ECO:0000244|PDB:3V4V}.
STRAND 202 206 {ECO:0000244|PDB:3V4V}.
STRAND 208 215 {ECO:0000244|PDB:3V4V}.
HELIX 218 221 {ECO:0000244|PDB:3V4V}.
STRAND 223 229 {ECO:0000244|PDB:3V4V}.
TURN 230 233 {ECO:0000244|PDB:3V4V}.
STRAND 234 237 {ECO:0000244|PDB:3V4P}.
STRAND 253 258 {ECO:0000244|PDB:3V4V}.
STRAND 267 272 {ECO:0000244|PDB:3V4V}.
HELIX 275 277 {ECO:0000244|PDB:3V4V}.
STRAND 280 286 {ECO:0000244|PDB:3V4V}.
STRAND 288 298 {ECO:0000244|PDB:3V4V}.
STRAND 308 313 {ECO:0000244|PDB:3V4V}.
STRAND 318 320 {ECO:0000244|PDB:3V4V}.
STRAND 322 327 {ECO:0000244|PDB:3V4V}.
STRAND 332 334 {ECO:0000244|PDB:3V4V}.
STRAND 338 344 {ECO:0000244|PDB:3V4V}.
STRAND 346 349 {ECO:0000244|PDB:3V4V}.
STRAND 351 353 {ECO:0000244|PDB:3V4P}.
STRAND 381 383 {ECO:0000244|PDB:3V4V}.
STRAND 386 390 {ECO:0000244|PDB:3V4V}.
HELIX 393 396 {ECO:0000244|PDB:3V4V}.
STRAND 398 403 {ECO:0000244|PDB:3V4V}.
STRAND 415 419 {ECO:0000244|PDB:3V4V}.
HELIX 420 422 {ECO:0000244|PDB:3V4V}.
STRAND 429 438 {ECO:0000244|PDB:3V4V}.
STRAND 440 445 {ECO:0000244|PDB:3V4V}.
STRAND 447 452 {ECO:0000244|PDB:3V4V}.
HELIX 453 455 {ECO:0000244|PDB:3V4V}.
STRAND 457 461 {ECO:0000244|PDB:3V4V}.
STRAND 466 474 {ECO:0000244|PDB:3V4V}.
STRAND 495 505 {ECO:0000244|PDB:3V4V}.
STRAND 511 522 {ECO:0000244|PDB:3V4V}.
STRAND 532 534 {ECO:0000244|PDB:3V4V}.
STRAND 536 538 {ECO:0000244|PDB:3V4V}.
STRAND 542 554 {ECO:0000244|PDB:3V4V}.
STRAND 556 564 {ECO:0000244|PDB:3V4V}.
STRAND 575 583 {ECO:0000244|PDB:3V4V}.
STRAND 610 617 {ECO:0000244|PDB:3V4V}.
SEQUENCE 1032 AA; 114900 MW; 73EC1204DE78CD35 CRC64;
MAWEARREPG PRRAAVRETV MLLLCLGVPT GRPYNVDTES ALLYQGPHNT LFGYSVVLHS
HGANRWLLVG APTANWLANA SVINPGAIYR CRIGKNPGQT CEQLQLGSPN GEPCGKTCLE
ERDNQWLGVT LSRQPGENGS IVTCGHRWKN IFYIKNENKL PTGGCYGVPP DLRTELSKRI
APCYQDYVKK FGENFASCQA GISSFYTKDL IVMGAPGSSY WTGSLFVYNI TTNKYKAFLD
KQNQVKFGSY LGYSVGAGHF RSQHTTEVVG GAPQHEQIGK AYIFSIDEKE LNILHEMKGK
KLGSYFGASV CAVDLNADGF SDLLVGAPMQ STIREEGRVF VYINSGSGAV MNAMETNLVG
SDKYAARFGE SIVNLGDIDN DGFEDVAIGA PQEDDLQGAI YIYNGRADGI SSTFSQRIEG
LQISKSLSMF GQSISGQIDA DNNGYVDVAV GAFRSDSAVL LRTRPVVIVD ASLSHPESVN
RTKFDCVENG WPSVCIDLTL CFSYKGKEVP GYIVLFYNMS LDVNRKAESP PRFYFSSNGT
SDVITGSIQV SSREANCRTH QAFMRKDVRD ILTPIQIEAA YHLGPHVISK RSTEEFPPLQ
PILQQKKEKD IMKKTINFAR FCAHENCSAD LQVSAKIGFL KPHENKTYLA VGSMKTLMLN
VSLFNAGDDA YETTLHVKLP VGLYFIKILE LEEKQINCEV TDNSGVVQLD CSIGYIYVDH
LSRIDISFLL DVSSLSRAEE DLSITVHATC ENEEEMDNLK HSRVTVAIPL KYEVKLTVHG
FVNPTSFVYG SNDENEPETC MVEKMNLTFH VINTGNSMAP NVSVEIMVPN SFSPQTDKLF
NILDVQTTTG ECHFENYQRV CALEQQKSAM QTLKGIVRFL SKTDKRLLYC IKADPHCLNF
LCNFGKMESG KEASVHIQLE GRPSILEMDE TSALKFEIRA TGFPEPNPRV IELNKDENVA
HVLLEGLHHQ RPKRYFTIVI ISSSLLLGLI VLLLISYVMW KAGFFKRQYK SILQEENRRD
SWSYINSKSN DD


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