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Integrin alpha-4 (CD49 antigen-like family member D) (Integrin alpha-IV) (Lymphocyte Peyer patch adhesion molecules subunit alpha) (LPAM subunit alpha) (VLA-4 subunit alpha) (CD antigen CD49d)

 ITA4_MOUSE              Reviewed;        1039 AA.
Q00651;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
20-JUN-2018, entry version 153.
RecName: Full=Integrin alpha-4;
AltName: Full=CD49 antigen-like family member D;
AltName: Full=Integrin alpha-IV;
AltName: Full=Lymphocyte Peyer patch adhesion molecules subunit alpha;
Short=LPAM subunit alpha;
AltName: Full=VLA-4 subunit alpha;
AltName: CD_antigen=CD49d;
Flags: Precursor;
Name=Itga4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1840602; DOI=10.1083/jcb.115.4.1149;
Neuhaus H., Hu M.C.-T., Hemler M.E., Takada Y., Holzmann B.,
Weissman I.L.;
"Cloning and expression of cDNAs for the alpha subunit of the murine
lymphocyte-Peyer's patch adhesion molecule.";
J. Cell Biol. 115:1149-1158(1991).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1028, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1028, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Integrins alpha-4/beta-1 (VLA-4 or LPAM-2) and alpha-
4/beta-7 (LPAM-1) 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. 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.
{ECO:0000250|UniProtKB:P13612}.
-!- 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 (By similarity).
{ECO:0000250|UniProtKB:P13612}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Peyer patch homing cells.
-!- DOMAIN: The SG1 motif is involved in binding to chondroitin
sulfate glycosaminoglycan and cell adhesion. {ECO:0000250}.
-!- PTM: Phosphorylation on Ser-1028 inhibits PXN binding.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the integrin alpha chain family.
{ECO:0000305}.
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EMBL; X53176; CAA37316.1; -; mRNA.
PIR; A41131; A41131.
RefSeq; NP_034706.3; NM_010576.3.
UniGene; Mm.31903; -.
ProteinModelPortal; Q00651; -.
SMR; Q00651; -.
ComplexPortal; CPX-3077; integrin alpha4-beta7 complex.
ComplexPortal; CPX-3118; integrin alpha4-beta1 complex.
CORUM; Q00651; -.
STRING; 10090.ENSMUSP00000099718; -.
BindingDB; Q00651; -.
ChEMBL; CHEMBL2111481; -.
iPTMnet; Q00651; -.
PhosphoSitePlus; Q00651; -.
SwissPalm; Q00651; -.
EPD; Q00651; -.
MaxQB; Q00651; -.
PaxDb; Q00651; -.
PeptideAtlas; Q00651; -.
PRIDE; Q00651; -.
GeneID; 16401; -.
KEGG; mmu:16401; -.
CTD; 3676; -.
MGI; MGI:96603; Itga4.
eggNOG; ENOG410IPB2; Eukaryota.
eggNOG; ENOG410XTAR; LUCA.
HOGENOM; HOG000088626; -.
HOVERGEN; HBG004538; -.
InParanoid; Q00651; -.
KO; K06483; -.
PhylomeDB; Q00651; -.
ChiTaRS; Itga4; mouse.
PRO; PR:Q00651; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_ITGA4; -.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0034669; C:integrin alpha4-beta7 complex; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0003823; F:antigen binding; ISO:MGI.
GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
GO; GO:0001968; F:fibronectin binding; IMP:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:1990405; F:protein antigen binding; ISO:MGI.
GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
GO; GO:0007155; P:cell adhesion; IMP:MGI.
GO; GO:0016477; P:cell migration; IMP:MGI.
GO; GO:0098609; P:cell-cell adhesion; TAS:DFLAT.
GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
GO; GO:0003366; P:cell-matrix adhesion involved in ameboidal cell migration; ISO:MGI.
GO; GO:0060710; P:chorio-allantoic fusion; IMP:MGI.
GO; GO:1990771; P:clathrin-dependent extracellular exosome endocytosis; ISO:MGI.
GO; GO:0050904; P:diapedesis; ISO:MGI.
GO; GO:0060324; P:face development; IMP:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:MGI.
GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:MGI.
GO; GO:0098657; P:import into cell; ISO:MGI.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:MGI.
GO; GO:0050901; P:leukocyte tethering or rolling; ISO:MGI.
GO; GO:0060485; P:mesenchyme development; TAS:DFLAT.
GO; GO:0090074; P:negative regulation of protein homodimerization activity; ISS:UniProtKB.
GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; ISO:MGI.
GO; GO:1903039; P:positive regulation of leukocyte cell-cell adhesion; ISO:MGI.
GO; GO:0002687; P:positive regulation of leukocyte migration; ISO:MGI.
GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; ISO:MGI.
GO; GO:2000406; P:positive regulation of T cell migration; ISO:MGI.
GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; ISO:MGI.
GO; GO:0043113; P:receptor clustering; ISO:MGI.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:MGI.
GO; GO:0072678; P:T cell migration; IMP:MGI.
GO; GO:0061032; P:visceral serous pericardium development; TAS:DFLAT.
Gene3D; 2.130.10.130; -; 1.
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; IPR028994; Integrin_alpha_N.
InterPro; IPR032695; Integrin_dom_sf.
Pfam; PF01839; FG-GAP; 2.
Pfam; PF08441; Integrin_alpha2; 1.
PRINTS; PR01185; INTEGRINA.
SMART; SM00191; Int_alpha; 6.
SUPFAM; SSF69179; SSF69179; 3.
PROSITE; PS51470; FG_GAP; 7.
PROSITE; PS00242; INTEGRIN_ALPHA; 1.
1: Evidence at protein level;
Calcium; Cell adhesion; Complete proteome; Disulfide bond;
Glycoprotein; Integrin; Membrane; Metal-binding; Phosphoprotein;
Receptor; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 40 {ECO:0000255}.
CHAIN 41 1039 Integrin alpha-4.
/FTId=PRO_0000016245.
TOPO_DOM 41 983 Extracellular. {ECO:0000255}.
TRANSMEM 984 1007 Helical. {ECO:0000255}.
TOPO_DOM 1008 1039 Cytoplasmic. {ECO:0000255}.
REPEAT 42 107 FG-GAP 1. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 117 184 FG-GAP 2. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 193 244 FG-GAP 3. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 246 298 FG-GAP 4. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 299 358 FG-GAP 5. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 362 419 FG-GAP 6. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 423 485 FG-GAP 7. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
CA_BIND 321 329 {ECO:0000255}.
CA_BIND 384 392 {ECO:0000255}.
CA_BIND 446 454 {ECO:0000255}.
MOTIF 613 623 SG1.
MOTIF 1010 1014 GFFKR motif.
SITE 598 599 Cleavage.
MOD_RES 1028 1028 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 105 105 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 145 145 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 236 236 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 487 487 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 525 525 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 545 545 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 633 633 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 652 652 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 667 667 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 813 813 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 828 828 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 98 108 {ECO:0000250}.
DISULFID 151 172 {ECO:0000250}.
DISULFID 190 205 {ECO:0000250}.
DISULFID 493 502 {ECO:0000250}.
DISULFID 508 564 {ECO:0000250}.
DISULFID 629 634 {ECO:0000250}.
DISULFID 705 718 {ECO:0000250}.
DISULFID 859 897 {ECO:0000250}.
DISULFID 904 909 {ECO:0000250}.
SEQUENCE 1039 AA; 115696 MW; C8C0BC611F7E9847 CRC64;
MFSTKSAWLR NGGADQGPRG IALREAVMLL LYFGVPTGPS YNLDPENALL YQGPSGTLFG
YSVVLHSHGS KRWLIVGAPT ASWLSNASVV NPGAIYRCGI RKNPNQTCEQ LQSGSPSGEP
CGKTCLEERD NQWLGVTLSR QPGENGSIVT CGHRWKNIFY MKSDNKLPTG ICYVMPSDLR
TELSKRMAPC YKDYTRKFGE NFASCQAGIS SFYTQDLIVM GAPGSSYWTG TVFVYNITTN
QYKAFVDRQN QVKFGSYLGY SVGAGHFRSP HTTEVVGGAP QHEQIGKAYI FSIDENELNI
VYEMKGKKLG SYFGASVCAV DLNADGFSDL LVGAPMQSTI REEGRVFVYI NSGMGAVMVE
MERVLVGSDK YAARFGESIA NLGDIDNDGF EDIAIGAPQE DDLRGAVYIY NGRVDGISST
YSQRIEGQQI SKSLRMFGQS ISGQIDADNN GYVDVAVGAF QSDSAVLLRT RPVVIVEASL
SHPESVNRTK FDCTENGLPS VCMHLTLCFS YKGKEVPGYI VLFYNVSLDV HRKAESPSRF
YFFSNGTSDV ITGSIRVSSS GEKCRTHQAF MRKDVRDILT PIHVEATYHL GHHVITKRNT
EEFPPLQPIL QQKKEKDVIR KMINFARFCA YENCSADLQV SAKVGFLKPY ENKTYLAVGS
MKTIMLNVSL FNAGDDAYET TLNVQLPTGL YFIKILDLEE KQINCEVTES SGIVKLACSL
GYIYVDRLSR IDISFLLDVS SLSRAHEDLS ISVHASCENE GELDQVRDNR VTLTIPLRYE
VMLTVHGLVN PTSFVYGSSE ENEPETCMAE KLNLTFHVIN TGISMAPNVS VKIMVPNSFL
PQDDKLFNVL DVQTTTGQCH FKHYGRECTF AQQKGIAGTL TDIVKFLSKT DKRLLYCMKA
DQHCLDFLCN FGKMESGKEA SVHIQLEGRP SILEMDETSS LKFEIKATAF PEPHPKVIEL
NKDENVAHVF LEGLHHQRPK RHFTIIIITI SLLLGLIVLL LISCVMWKAG FFKRQYKSIL
QEENRRDSWS YVNSKSNDD


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