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 27-MAR-2024, entry version 155. 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 GlyCosmos; Q9QXH4; 7 sites, No reported glycans. DR GlyGen; Q9QXH4; 7 sites. DR PhosphoSitePlus; Q9QXH4; -. DR MaxQB; Q9QXH4; -. DR PaxDb; 10090-ENSMUSP00000033053; -. DR ProteomicsDB; 269005; -. DR Antibodypedia; 1499; 2764 antibodies from 52 providers. DR DNASU; 16411; -. DR Ensembl; ENSMUST00000033053.8; ENSMUSP00000033053.7; ENSMUSG00000030789.10. DR GeneID; 16411; -. DR KEGG; mmu:16411; -. DR UCSC; uc009jyc.1; mouse. DR AGR; MGI:96609; -. 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; KGEAVWT; -. DR OrthoDB; 3816176at2759; -. 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 81 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 56 other cell types or tissues. DR ExpressionAtlas; Q9QXH4; baseline and differential. 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 CDD; cd01469; vWA_integrins_alpha_subunit; 1. DR Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1. DR Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 1. DR Gene3D; 2.60.40.1460; Integrin domains. Chain A, domain 2; 1. DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1. DR Gene3D; 2.60.40.1530; ntegrin, alpha v. Chain A, domain 4; 1. DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1. DR InterPro; IPR013517; FG-GAP. DR InterPro; IPR013519; Int_alpha_beta-p. DR InterPro; IPR000413; Integrin_alpha. DR InterPro; IPR018184; Integrin_alpha_C_CS. DR InterPro; IPR013649; Integrin_alpha_Ig-like_1. DR InterPro; IPR048285; Integrin_alpha_Ig-like_2. DR InterPro; IPR028994; Integrin_alpha_N. DR InterPro; IPR032695; Integrin_dom_sf. DR InterPro; IPR048633; ITGAX-like_Ig_3. DR InterPro; IPR002035; VWF_A. DR InterPro; IPR036465; vWFA_dom_sf. DR PANTHER; PTHR23220; INTEGRIN ALPHA; 1. DR PANTHER; PTHR23220:SF118; INTEGRIN ALPHA-X; 1. DR Pfam; PF01839; FG-GAP; 2. DR Pfam; PF08441; Integrin_A_Ig_1; 1. DR Pfam; PF20805; Integrin_A_Ig_2; 1. DR Pfam; PF00357; Integrin_alpha; 1. DR Pfam; PF21520; ITGAX-like_Ig_3; 1. DR Pfam; PF00092; VWA; 1. DR PRINTS; PR01185; INTEGRINA. DR PRINTS; PR00453; VWFADOMAIN. DR SMART; SM00191; Int_alpha; 5. DR SMART; SM00327; VWA; 1. DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1. DR SUPFAM; SSF69179; Integrin domains; 3. DR SUPFAM; SSF53300; vWA-like; 1. DR PROSITE; PS51470; FG_GAP; 7. DR PROSITE; PS00242; INTEGRIN_ALPHA; 1. DR PROSITE; PS50234; VWFA; 1. DR Genevisible; Q9QXH4; MM. 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 //