ITAX_MOUSE
ID ITAX_MOUSE Reviewed; 1169 AA.
AC Q9QXH4;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Integrin alpha-X;
DE AltName: Full=CD11 antigen-like family member C;
DE AltName: Full=Leukocyte adhesion glycoprotein p150,95 alpha chain;
DE AltName: Full=Leukocyte adhesion receptor p150,95;
DE AltName: CD_antigen=CD11c;
DE Flags: Precursor;
GN Name=Itgax;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Dendritic cell;
RA Huang X., Gorski K., Tong C., Rattis F.-M., Tseng S.-Y., Pardoll D.,
RA Tsuchiya H.;
RT "Isolation of genes selectively expressed by dendritic cells.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Integrin alpha-X/beta-2 is a receptor for fibrinogen. It
CC recognizes the sequence G-P-R in fibrinogen. It mediates cell-cell
CC interaction during inflammatory responses. It is especially important
CC in monocyte adhesion and chemotaxis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-X associates
CC with beta-2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with
CC I-domains do not undergo protease cleavage.
CC -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF211864; AAF23492.1; -; mRNA.
DR CCDS; CCDS40150.1; -.
DR RefSeq; NP_067309.1; NM_021334.2.
DR AlphaFoldDB; Q9QXH4; -.
DR SMR; Q9QXH4; -.
DR BioGRID; 200825; 1.
DR ComplexPortal; CPX-3134; Integrin alphaX-beta2 complex.
DR CORUM; Q9QXH4; -.
DR STRING; 10090.ENSMUSP00000033053; -.
DR GlyGen; Q9QXH4; 7 sites.
DR PhosphoSitePlus; Q9QXH4; -.
DR MaxQB; Q9QXH4; -.
DR PaxDb; Q9QXH4; -.
DR PRIDE; Q9QXH4; -.
DR ProteomicsDB; 269005; -.
DR Antibodypedia; 1499; 2422 antibodies from 52 providers.
DR DNASU; 16411; -.
DR Ensembl; ENSMUST00000033053; ENSMUSP00000033053; ENSMUSG00000030789.
DR GeneID; 16411; -.
DR KEGG; mmu:16411; -.
DR UCSC; uc009jyc.1; mouse.
DR CTD; 3687; -.
DR MGI; MGI:96609; Itgax.
DR VEuPathDB; HostDB:ENSMUSG00000030789; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000154838; -.
DR HOGENOM; CLU_004111_3_0_1; -.
DR InParanoid; Q9QXH4; -.
DR OMA; YCETFTL; -.
DR OrthoDB; 73876at2759; -.
DR PhylomeDB; Q9QXH4; -.
DR TreeFam; TF105391; -.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 16411; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Itgax; mouse.
DR PRO; PR:Q9QXH4; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9QXH4; protein.
DR Bgee; ENSMUSG00000030789; Expressed in spleen and 55 other tissues.
DR ExpressionAtlas; Q9QXH4; baseline and differential.
DR Genevisible; Q9QXH4; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IDA:MGI.
DR GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:1905956; P:positive regulation of endothelial tube morphogenesis; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:ARUK-UCL.
DR GO; GO:0031643; P:positive regulation of myelination; IDA:ARUK-UCL.
DR Gene3D; 2.130.10.130; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR013649; Integrin_alpha-2.
DR InterPro; IPR018184; Integrin_alpha_C_CS.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF00357; Integrin_alpha; 1.
DR Pfam; PF08441; Integrin_alpha2; 1.
DR Pfam; PF00092; VWA; 1.
DR PRINTS; PR01185; INTEGRINA.
DR SMART; SM00191; Int_alpha; 5.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 3.
DR SUPFAM; SSF69318; SSF69318; 1.
DR PROSITE; PS51470; FG_GAP; 7.
DR PROSITE; PS00242; INTEGRIN_ALPHA; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Disulfide bond; Glycoprotein; Integrin; Magnesium;
KW Membrane; Metal-binding; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1169
FT /note="Integrin alpha-X"
FT /id="PRO_0000016295"
FT TOPO_DOM 20..1116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1117..1137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1138..1169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 23..78
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 79..138
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT DOMAIN 152..330
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REPEAT 341..392
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 393..444
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 445..505
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 508..566
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 571..631
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT MOTIF 1140..1144
FT /note="GFFKR motif"
FT BINDING 158
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 467
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 471
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 475
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 531
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 533
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 535
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 539
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 594
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 598
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 602
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 734
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 949
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1059
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1084
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 69..76
FT /evidence="ECO:0000250"
FT DISULFID 108..126
FT /evidence="ECO:0000250"
FT DISULFID 116..146
FT /evidence="ECO:0000250"
FT DISULFID 496..507
FT /evidence="ECO:0000250"
FT DISULFID 640..721
FT /evidence="ECO:0000250"
FT DISULFID 656..711
FT /evidence="ECO:0000250"
FT DISULFID 770..776
FT /evidence="ECO:0000250"
FT DISULFID 858..873
FT /evidence="ECO:0000250"
FT DISULFID 1007..1031
FT /evidence="ECO:0000250"
FT DISULFID 1036..1041
FT /evidence="ECO:0000250"
SQ SEQUENCE 1169 AA; 129151 MW; C616412033C219A6 CRC64;
MSCTWIAFLL LLGFVSCLGF NLDAEKLTHF HMDGAEFGHS VLQYDSSWVV VGAPKEIKAT
NQIGGLYKCG YHTGNCEPIS LQVPPEAVNI SLGLSLAAAT NPSWLLACGP TVHHTCRENI
YLTGLCFLLS SSFKQSQNFP TAQQECPKQD QDIVFLIDGS GSISSTDFEK MLDFVKAVMS
QLQRPSTRFS LMQFSDYFRV HFTFNNFIST SSPLSLLGSV RQLRGYTYTA SAIKHVITEL
FTTQSGARQD ATKVLIVITD GRKQGDNLSY DSVIPMAEAA SIIRYAIGVG KAFYNEHSKQ
ELKAIASMPS HEYVFSVENF DALKDIENQL KEKIFAIEGT ETPSSSTFEL EMSQEGFSAV
FTPDGPVLGA VGSFSWSGGA FLYPSNMRPT FINMSQENED MRDAYLGYST ALAFWKGVHS
LILGAPRHQH TGKVVIFTQE SRHWRPKSEV RGTQIGSYFG ASLCSVDMDR DGSTDLVLIG
VPHYYEHTRG GQVSVCPMPG VGSRWHCGTT LHGEQGHPWG RFGAALTVLG DVNGDSLADV
AIGAPGEEEN RGAVYIFHGA SRQDIAPSPS QRISASQIPS RIQYFGQSLS GGQDLTRDGL
VDLAVGSKGR VLLLRTRPIL RVSPTVHFTP AEISRSVFEC QEQVAPEQTL SDATVCLHIH
ESPKTQLGDL RSTVTFDLAL DHGRLSTRAI FKETKTRALT RVKTLGLNKH CESVKLLLPA
CVEDSVTPIT LRLNFSLVGV PISSLQNLQP MLAVDDQTYF TASLPFEKNC GADHICQDDL
SVVFGFPDLK TLVVGSDLEL NVDVTVSNDG EDSYGTTVTL FYPVGLSFRR VAEGQVFLRK
KEDQQWQRRG QHSLHLMCDS TPDRSQGLWS TSCSSRHVIF RGGSQMTFLV TFDVSPKAEL
GDRLLLRARV GSENNVPGTP KTTFQLELPV KYAVYTMISS HDQFTKYLNF STSEKEKTSV
VEHRFQVNNL GQRDVPVSIN FWVPIELKGE AVWTVMVSHP QNPLTQCYRN RLKPTQFDLL
THMQKSPVLD CSIADCLHLR CDIPSLGILD ELYFILKGNL SFGWISQTLQ KKVLLLSEAE
ITFNTSVYSQ LPGQEAFLRA QTKTVLEMYK VHNPVPLIVG SSVGGLLLLA IITAILYKAG
FFKRQYKEML EEANGQFVSD GTPTPQVAQ
