ITAD_HUMAN
ID ITAD_HUMAN Reviewed; 1161 AA.
AC Q13349; Q15575; Q15576;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Integrin alpha-D;
DE AltName: Full=ADB2;
DE AltName: Full=CD11 antigen-like family member D;
DE AltName: Full=Leukointegrin alpha D;
DE AltName: CD_antigen=CD11d;
DE Flags: Precursor;
GN Name=ITGAD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RX PubMed=8777714; DOI=10.1016/1074-7613(95)90058-6;
RA Van der Vieren M., Le Trong H., Wood C.L., Moore P.F., St John T.,
RA Staunton D.E., Gallatin W.M.;
RT "A novel leukointegrin, alpha d beta 2, binds preferentially to ICAM-3.";
RL Immunity 3:683-690(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-235.
RX PubMed=10722744; DOI=10.1074/jbc.275.12.8959;
RA Noti J.D., Johnson A.K., Dillon J.D.;
RT "Structural and functional characterization of the leukocyte integrin gene
RT CD11d. Essential role of Sp1 and Sp3.";
RL J. Biol. Chem. 275:8959-8969(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 467-536; 570-601; 632-665; 787-833 AND
RP 909-1124.
RX PubMed=8666289; DOI=10.1016/0378-1119(95)00869-1;
RA Wong D.A., Davis E.M., LeBeau M., Springer T.A.;
RT "Cloning and chromosomal localization of a novel gene-encoding a human beta
RT 2-integrin alpha subunit.";
RL Gene 171:291-294(1996).
RN [4]
RP INTERACTION WITH VCAM1.
RX PubMed=9841932; DOI=10.1084/jem.188.11.2187;
RA Grayson M.H., Van der Vieren M., Sterbinsky S.A., Michael Gallatin W.,
RA Hoffman P.A., Staunton D.E., Bochner B.S.;
RT "Alphadbeta2 integrin is expressed on human eosinophils and functions as an
RT alternative ligand for vascular cell adhesion molecule 1 (VCAM-1).";
RL J. Exp. Med. 188:2187-2191(1998).
RN [5]
RP INTERACTION WITH VCAM1.
RX PubMed=10438935;
RA Van der Vieren M., Crowe D.T., Hoekstra D., Vazeux R., Hoffman P.A.,
RA Grayson M.H., Bochner B.S., Gallatin W.M., Staunton D.E.;
RT "The leukocyte integrin alpha D beta 2 binds VCAM-1: evidence for a binding
RT interface between I domain and VCAM-1.";
RL J. Immunol. 163:1984-1990(1999).
CC -!- FUNCTION: Integrin alpha-D/beta-2 is a receptor for ICAM3 and VCAM1.
CC May play a role in the atherosclerotic process such as clearing
CC lipoproteins from plaques and in phagocytosis of blood-borne pathogens,
CC particulate matter, and senescent erythrocytes from the blood.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-D associates
CC with beta-2.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed moderately on myelomonocytic cell lines
CC and subsets of peripheral blood leukocytes and strongly on tissue-
CC specialized cells, including macrophages foam cells within
CC atherosclerotic plaques, and on splenic red pulp macrophages.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAB60634.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR EMBL; U37028; AAB38547.1; -; mRNA.
DR EMBL; AF187881; AAF62875.1; -; Genomic_DNA.
DR EMBL; U40274; AAB60634.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U40275; AAB60635.1; -; Genomic_DNA.
DR EMBL; U40276; AAB60636.1; -; Genomic_DNA.
DR EMBL; U40277; AAB60637.1; -; Genomic_DNA.
DR EMBL; U40279; AAB60638.1; -; Genomic_DNA.
DR EMBL; U40278; AAB60638.1; JOINED; Genomic_DNA.
DR CCDS; CCDS32438.1; -.
DR RefSeq; NP_001305114.1; NM_001318185.1.
DR RefSeq; NP_005344.2; NM_005353.2.
DR AlphaFoldDB; Q13349; -.
DR SMR; Q13349; -.
DR BioGRID; 109887; 54.
DR ComplexPortal; CPX-1828; Integrin alphaD-beta2 complex.
DR IntAct; Q13349; 1.
DR STRING; 9606.ENSP00000373854; -.
DR GlyGen; Q13349; 9 sites.
DR iPTMnet; Q13349; -.
DR PhosphoSitePlus; Q13349; -.
DR BioMuta; ITGAD; -.
DR DMDM; 296434544; -.
DR jPOST; Q13349; -.
DR MassIVE; Q13349; -.
DR PaxDb; Q13349; -.
DR PeptideAtlas; Q13349; -.
DR PRIDE; Q13349; -.
DR Antibodypedia; 27846; 125 antibodies from 20 providers.
DR DNASU; 3681; -.
DR Ensembl; ENST00000389202.3; ENSP00000373854.2; ENSG00000156886.12.
DR GeneID; 3681; -.
DR KEGG; hsa:3681; -.
DR MANE-Select; ENST00000389202.3; ENSP00000373854.2; NM_005353.3; NP_005344.2.
DR UCSC; uc002ebv.1; human.
DR CTD; 3681; -.
DR DisGeNET; 3681; -.
DR GeneCards; ITGAD; -.
DR HGNC; HGNC:6146; ITGAD.
DR HPA; ENSG00000156886; Tissue enriched (lymphoid).
DR MIM; 602453; gene.
DR neXtProt; NX_Q13349; -.
DR OpenTargets; ENSG00000156886; -.
DR PharmGKB; PA29946; -.
DR VEuPathDB; HostDB:ENSG00000156886; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000160953; -.
DR HOGENOM; CLU_004111_3_0_1; -.
DR InParanoid; Q13349; -.
DR OMA; WEIIQTV; -.
DR OrthoDB; 73876at2759; -.
DR PhylomeDB; Q13349; -.
DR TreeFam; TF105391; -.
DR PathwayCommons; Q13349; -.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR SignaLink; Q13349; -.
DR SIGNOR; Q13349; -.
DR BioGRID-ORCS; 3681; 9 hits in 1064 CRISPR screens.
DR ChiTaRS; ITGAD; human.
DR GeneWiki; ITGAD; -.
DR GenomeRNAi; 3681; -.
DR Pharos; Q13349; Tbio.
DR PRO; PR:Q13349; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q13349; protein.
DR Bgee; ENSG00000156886; Expressed in granulocyte and 91 other tissues.
DR Genevisible; Q13349; HS.
DR GO; GO:0009986; C:cell surface; IC:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0006955; P:immune response; NAS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..1161
FT /note="Integrin alpha-D"
FT /id="PRO_0000016296"
FT TOPO_DOM 18..1099
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1100..1120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1121..1161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 19..76
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 77..136
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT DOMAIN 150..332
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REPEAT 339..390
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 391..442
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 443..503
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 506..564
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 569..629
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT MOTIF 1126..1130
FT /note="GFFKR motif"
FT BINDING 465
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
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 473
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 529
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 537
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 592
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 596
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 600
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 690
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 732
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 872
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 956
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1045
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 67..74
FT /evidence="ECO:0000250"
FT DISULFID 106..124
FT /evidence="ECO:0000250"
FT DISULFID 654..709
FT /evidence="ECO:0000250"
FT DISULFID 768..774
FT /evidence="ECO:0000250"
FT DISULFID 845..860
FT /evidence="ECO:0000250"
FT DISULFID 993..1017
FT /evidence="ECO:0000250"
FT DISULFID 1022..1027
FT /evidence="ECO:0000250"
FT CONFLICT 499
FT /note="G -> GQ (in Ref. 1; AAB38547)"
FT /evidence="ECO:0000305"
FT CONFLICT 824
FT /note="L -> V (in Ref. 3; AAB60637)"
FT /evidence="ECO:0000305"
FT CONFLICT 983
FT /note="V -> A (in Ref. 3; AAB60638)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1161 AA; 126758 MW; 769D658010CE5823 CRC64;
MTFGTVLLLS VLASYHGFNL DVEEPTIFQE DAGGFGQSVV QFGGSRLVVG APLEVVAANQ
TGRLYDCAAA TGMCQPIPLH IRPEAVNMSL GLTLAASTNG SRLLACGPTL HRVCGENSYS
KGSCLLLGSR WEIIQTVPDA TPECPHQEMD IVFLIDGSGS IDQNDFNQMK GFVQAVMGQF
EGTDTLFALM QYSNLLKIHF TFTQFRTSPS QQSLVDPIVQ LKGLTFTATG ILTVVTQLFH
HKNGARKSAK KILIVITDGQ KYKDPLEYSD VIPQAEKAGI IRYAIGVGHA FQGPTARQEL
NTISSAPPQD HVFKVDNFAA LGSIQKQLQE KIYAVEGTQS RASSSFQHEM SQEGFSTALT
MDGLFLGAVG SFSWSGGAFL YPPNMSPTFI NMSQENVDMR DSYLGYSTEL ALWKGVQNLV
LGAPRYQHTG KAVIFTQVSR QWRKKAEVTG TQIGSYFGAS LCSVDVDSDG STDLILIGAP
HYYEQTRGGQ VSVCPLPRGR VQWQCDAVLR GEQGHPWGRF GAALTVLGDV NEDKLIDVAI
GAPGEQENRG AVYLFHGASE SGISPSHSQR IASSQLSPRL QYFGQALSGG QDLTQDGLMD
LAVGARGQVL LLRSLPVLKV GVAMRFSPVE VAKAVYRCWE EKPSALEAGD ATVCLTIQKS
SLDQLGDIQS SVRFDLALDP GRLTSRAIFN ETKNPTLTRR KTLGLGIHCE TLKLLLPDCV
EDVVSPIILH LNFSLVREPI PSPQNLRPVL AVGSQDLFTA SLPFEKNCGQ DGLCEGDLGV
TLSFSGLQTL TVGSSLELNV IVTVWNAGED SYGTVVSLYY PAGLSHRRVS GAQKQPHQSA
LRLACETVPT EDEGLRSSRC SVNHPIFHEG SNGTFIVTFD VSYKATLGDR MLMRASASSE
NNKASSSKAT FQLELPVKYA VYTMISRQEE STKYFNFATS DEKKMKEAEH RYRVNNLSQR
DLAISINFWV PVLLNGVAVW DVVMEAPSQS LPCVSERKPP QHSDFLTQIS RSPMLDCSIA
DCLQFRCDVP SFSVQEELDF TLKGNLSFGW VRETLQKKVL VVSVAEITFD TSVYSQLPGQ
EAFMRAQMEM VLEEDEVYNA IPIIMGSSVG ALLLLALITA TLYKLGFFKR HYKEMLEDKP
EDTATFSGDD FSCVAPNVPL S
