GENTAUR Molecular Products.

 ITAD_HUMAN              Reviewed;        1161 AA.
 Q13349; Q15575; Q15576;
 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
 18-MAY-2010, sequence version 2.
 16-JAN-2019, entry version 170.
 RecName: Full=Integrin alpha-D;
 AltName: Full=ADB2;
 AltName: Full=CD11 antigen-like family member D;
 AltName: Full=Leukointegrin alpha D;
 AltName: CD_antigen=CD11d;
 Flags: Precursor;
 Name=ITGAD;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA].
 TISSUE=Spleen;
 PubMed=8777714; DOI=10.1016/1074-7613(95)90058-6;
 Van der Vieren M., Le Trong H., Wood C.L., Moore P.F., St John T.,
 Staunton D.E., Gallatin W.M.;
 "A novel leukointegrin, alpha d beta 2, binds preferentially to ICAM-
 3.";
 Immunity 3:683-690(1995).
 [2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-235.
 PubMed=10722744; DOI=10.1074/jbc.275.12.8959;
 Noti J.D., Johnson A.K., Dillon J.D.;
 "Structural and functional characterization of the leukocyte integrin
 gene CD11d. Essential role of Sp1 and Sp3.";
 J. Biol. Chem. 275:8959-8969(2000).
 [3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 467-536; 570-601; 632-665;
 787-833 AND 909-1124.
 PubMed=8666289; DOI=10.1016/0378-1119(95)00869-1;
 Wong D.A., Davis E.M., LeBeau M., Springer T.A.;
 "Cloning and chromosomal localization of a novel gene-encoding a human
 beta 2-integrin alpha subunit.";
 Gene 171:291-294(1996).
 [4]
 INTERACTION WITH VCAM1.
 PubMed=9841932; DOI=10.1084/jem.188.11.2187;
 Grayson M.H., Van der Vieren M., Sterbinsky S.A., Michael Gallatin W.,
 Hoffman P.A., Staunton D.E., Bochner B.S.;
 "Alphadbeta2 integrin is expressed on human eosinophils and functions
 as an alternative ligand for vascular cell adhesion molecule 1 (VCAM-
 1).";
 J. Exp. Med. 188:2187-2191(1998).
 [5]
 INTERACTION WITH VCAM1.
 PubMed=10438935;
 Van der Vieren M., Crowe D.T., Hoekstra D., Vazeux R., Hoffman P.A.,
 Grayson M.H., Bochner B.S., Gallatin W.M., Staunton D.E.;
 "The leukocyte integrin alpha D beta 2 binds VCAM-1: evidence for a
 binding interface between I domain and VCAM-1.";
 J. Immunol. 163:1984-1990(1999).
 -!- FUNCTION: Integrin alpha-D/beta-2 is a receptor for ICAM3 and
     VCAM1. May play a role in the atherosclerotic process such as
     clearing lipoproteins from plaques and in phagocytosis of blood-
     borne pathogens, particulate matter, and senescent erythrocytes
     from the blood.
 -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-D
     associates with beta-2.
 -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
     protein.
 -!- TISSUE SPECIFICITY: Expressed moderately on myelomonocytic cell
     lines and subsets of peripheral blood leukocytes and strongly on
     tissue-specialized cells, including macrophages foam cells within
     atherosclerotic plaques, and on splenic red pulp macrophages.
 -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins
     with I-domains do not undergo protease cleavage.
 -!- SIMILARITY: Belongs to the integrin alpha chain family.
     {ECO:0000305}.
 -!- SEQUENCE CAUTION:
     Sequence=AAB60634.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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 EMBL; U37028; AAB38547.1; -; mRNA.
 EMBL; AF187881; AAF62875.1; -; Genomic_DNA.
 EMBL; U40274; AAB60634.1; ALT_SEQ; Genomic_DNA.
 EMBL; U40275; AAB60635.1; -; Genomic_DNA.
 EMBL; U40276; AAB60636.1; -; Genomic_DNA.
 EMBL; U40277; AAB60637.1; -; Genomic_DNA.
 EMBL; U40279; AAB60638.1; -; Genomic_DNA.
 EMBL; U40278; AAB60638.1; JOINED; Genomic_DNA.
 CCDS; CCDS32438.1; -.
 RefSeq; NP_001305114.1; NM_001318185.1.
 RefSeq; NP_005344.2; NM_005353.2.
 UniGene; Hs.679163; -.
 ProteinModelPortal; Q13349; -.
 SMR; Q13349; -.
 BioGrid; 109887; 5.
 ComplexPortal; CPX-1828; Integrin alphaD-beta2 complex.
 IntAct; Q13349; 1.
 STRING; 9606.ENSP00000373854; -.
 iPTMnet; Q13349; -.
 PhosphoSitePlus; Q13349; -.
 BioMuta; ITGAD; -.
 DMDM; 296434544; -.
 jPOST; Q13349; -.
 PaxDb; Q13349; -.
 PeptideAtlas; Q13349; -.
 PRIDE; Q13349; -.
 ProteomicsDB; 59334; -.
 Ensembl; ENST00000389202; ENSP00000373854; ENSG00000156886.
 GeneID; 3681; -.
 KEGG; hsa:3681; -.
 UCSC; uc002ebv.1; human.
 CTD; 3681; -.
 DisGeNET; 3681; -.
 EuPathDB; HostDB:ENSG00000156886.11; -.
 GeneCards; ITGAD; -.
 H-InvDB; HIX0012989; -.
 H-InvDB; HIX0134372; -.
 HGNC; HGNC:6146; ITGAD.
 HPA; HPA026786; -.
 MIM; 602453; gene.
 neXtProt; NX_Q13349; -.
 OpenTargets; ENSG00000156886; -.
 PharmGKB; PA29946; -.
 eggNOG; ENOG410IPBA; Eukaryota.
 eggNOG; ENOG410ZFBE; LUCA.
 GeneTree; ENSGT00940000160953; -.
 HOGENOM; HOG000113114; -.
 HOVERGEN; HBG100530; -.
 InParanoid; Q13349; -.
 KO; K06594; -.
 OMA; ALPECPN; -.
 OrthoDB; 73876at2759; -.
 PhylomeDB; Q13349; -.
 TreeFam; TF105391; -.
 Reactome; R-HSA-216083; Integrin cell surface interactions.
 SIGNOR; Q13349; -.
 ChiTaRS; ITGAD; human.
 GeneWiki; ITGAD; -.
 GenomeRNAi; 3681; -.
 PRO; PR:Q13349; -.
 Proteomes; UP000005640; Chromosome 16.
 Bgee; ENSG00000156886; Expressed in 61 organ(s), highest expression level in spleen.
 CleanEx; HS_ITGAD; -.
 Genevisible; Q13349; HS.
 GO; GO:0009986; C:cell surface; IC:UniProtKB.
 GO; GO:0008305; C:integrin complex; TAS:UniProtKB.
 GO; GO:0005886; C:plasma membrane; TAS:Reactome.
 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
 GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB.
 GO; GO:0006955; P:immune response; NAS:UniProtKB.
 GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
 Gene3D; 2.130.10.130; -; 1.
 Gene3D; 3.40.50.410; -; 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.
 InterPro; IPR002035; VWF_A.
 InterPro; IPR036465; vWFA_dom_sf.
 Pfam; PF01839; FG-GAP; 1.
 Pfam; PF00357; Integrin_alpha; 1.
 Pfam; PF08441; Integrin_alpha2; 1.
 Pfam; PF00092; VWA; 1.
 PRINTS; PR01185; INTEGRINA.
 SMART; SM00191; Int_alpha; 5.
 SMART; SM00327; VWA; 1.
 SUPFAM; SSF53300; SSF53300; 1.
 SUPFAM; SSF69179; SSF69179; 3.
 PROSITE; PS51470; FG_GAP; 7.
 PROSITE; PS00242; INTEGRIN_ALPHA; 1.
 PROSITE; PS50234; VWFA; 1.
 1: Evidence at protein level;
 Calcium; Cell adhesion; Complete proteome; Disulfide bond;
 Glycoprotein; Integrin; Magnesium; Membrane; Metal-binding; Receptor;
 Reference proteome; Repeat; Signal; Transmembrane;
 Transmembrane helix.
 SIGNAL        1     17       {ECO:0000255}.
 CHAIN        18   1161       Integrin alpha-D.
                              /FTId=PRO_0000016296.
 TOPO_DOM     18   1099       Extracellular. {ECO:0000255}.
 TRANSMEM   1100   1120       Helical. {ECO:0000255}.
 TOPO_DOM   1121   1161       Cytoplasmic. {ECO:0000255}.
 REPEAT       19     76       FG-GAP 1. {ECO:0000255|PROSITE-
                              ProRule:PRU00803}.
 REPEAT       77    136       FG-GAP 2. {ECO:0000255|PROSITE-
                              ProRule:PRU00803}.
 DOMAIN      150    332       VWFA. {ECO:0000255|PROSITE-
                              ProRule:PRU00219}.
 REPEAT      339    390       FG-GAP 3. {ECO:0000255|PROSITE-
                              ProRule:PRU00803}.
 REPEAT      391    442       FG-GAP 4. {ECO:0000255|PROSITE-
                              ProRule:PRU00803}.
 REPEAT      443    503       FG-GAP 5. {ECO:0000255|PROSITE-
                              ProRule:PRU00803}.
 REPEAT      506    564       FG-GAP 6. {ECO:0000255|PROSITE-
                              ProRule:PRU00803}.
 REPEAT      569    629       FG-GAP 7. {ECO:0000255|PROSITE-
                              ProRule:PRU00803}.
 CA_BIND     465    473       {ECO:0000255}.
 CA_BIND     529    537       {ECO:0000255}.
 CA_BIND     592    600       {ECO:0000255}.
 MOTIF      1126   1130       GFFKR motif.
 CARBOHYD     59     59       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD     87     87       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD     99     99       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    391    391       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    690    690       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    732    732       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    872    872       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    956    956       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1045   1045       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 DISULFID     67     74       {ECO:0000250}.
 DISULFID    106    124       {ECO:0000250}.
 DISULFID    654    709       {ECO:0000250}.
 DISULFID    768    774       {ECO:0000250}.
 DISULFID    845    860       {ECO:0000250}.
 DISULFID    993   1017       {ECO:0000250}.
 DISULFID   1022   1027       {ECO:0000250}.
 CONFLICT    499    499       G -> GQ (in Ref. 1; AAB38547).
                              {ECO:0000305}.
 CONFLICT    824    824       L -> V (in Ref. 3; AAB60637).
                              {ECO:0000305}.
 CONFLICT    983    983       V -> A (in Ref. 3; AAB60638).
                              {ECO:0000305}.
 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

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