ITAD_MOUSE
ID ITAD_MOUSE Reviewed; 1168 AA.
AC Q3V0T4;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Integrin alpha-D;
DE AltName: CD_antigen=CD11d;
DE Flags: Precursor;
GN Name=Itgad;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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-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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-D 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}.
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DR EMBL; AK132915; BAE21419.1; -; mRNA.
DR AlphaFoldDB; Q3V0T4; -.
DR SMR; Q3V0T4; -.
DR ComplexPortal; CPX-3126; Integrin alphaD-beta2 complex.
DR STRING; 10090.ENSMUSP00000033051; -.
DR GlyGen; Q3V0T4; 10 sites.
DR iPTMnet; Q3V0T4; -.
DR PhosphoSitePlus; Q3V0T4; -.
DR MaxQB; Q3V0T4; -.
DR PaxDb; Q3V0T4; -.
DR PRIDE; Q3V0T4; -.
DR ProteomicsDB; 268892; -.
DR Antibodypedia; 27846; 125 antibodies from 20 providers.
DR Ensembl; ENSMUST00000106237; ENSMUSP00000101844; ENSMUSG00000070369.
DR UCSC; uc009jyd.2; mouse.
DR MGI; MGI:3578624; Itgad.
DR VEuPathDB; HostDB:ENSMUSG00000070369; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000160953; -.
DR InParanoid; Q3V0T4; -.
DR OMA; WEIIQTV; -.
DR PhylomeDB; Q3V0T4; -.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR ChiTaRS; Itgad; mouse.
DR PRO; PR:Q3V0T4; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3V0T4; protein.
DR Bgee; ENSMUSG00000070369; Expressed in spleen and 37 other tissues.
DR ExpressionAtlas; Q3V0T4; baseline and differential.
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:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0050798; P:activated T cell proliferation; IMP: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:0034113; P:heterotypic cell-cell adhesion; ISO:MGI.
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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1168
FT /note="Integrin alpha-D"
FT /id="PRO_0000045902"
FT TOPO_DOM 27..1107
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1108..1128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1129..1168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 28..85
FT /note="FG-GAP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 86..145
FT /note="FG-GAP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT DOMAIN 159..341
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REPEAT 348..399
FT /note="FG-GAP 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 400..451
FT /note="FG-GAP 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 452..512
FT /note="FG-GAP 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 515..573
FT /note="FG-GAP 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REPEAT 578..638
FT /note="FG-GAP 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT REGION 1146..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1133..1137
FT /note="GFFKR motif"
FT BINDING 474
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 476
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 478
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 482
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 538
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 540
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 542
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 546
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 601
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 605
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT BINDING 609
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P08648"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 703
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 791
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 943
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1052
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1077
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 76..83
FT /evidence="ECO:0000250"
FT DISULFID 115..133
FT /evidence="ECO:0000250"
FT DISULFID 663..718
FT /evidence="ECO:0000250"
FT DISULFID 776..782
FT /evidence="ECO:0000250"
FT DISULFID 852..867
FT /evidence="ECO:0000250"
FT DISULFID 1000..1024
FT /evidence="ECO:0000250"
FT DISULFID 1029..1034
FT /evidence="ECO:0000250"
SQ SEQUENCE 1168 AA; 127829 MW; 15FCDF2618AD05C3 CRC64;
MVFKTIWIER YRKLINLFRA LASCHGSNLD VEKPVVFKED AASFGQTVVQ FGGSRLVVGA
PLEAVAVNQT GQLYDCAPAT GVCQPILLHI PLEAVNMSLG LSLVADTNNS QLLACGPTAQ
RACAKNMYAK GSCLLLGSSL QFIQAIPATM PECPGQEMDI AFLIDGSGSI DQSDFTQMKD
FVKALMGQLA STSTSFSLMQ YSNILKTHFT FTEFKSSLSP QSLVDAIVQL QGLTYTASGI
QKVVKELFHS KNGARKSAKK ILIVITDGQK FRDPLEYRHV IPEAEKAGII RYAIGVGDAF
REPTALQELN TIGSAPSQDH VFKVGNFVAL RSIQRQIQEK IFAIEGTESR SSSSFQHEMS
QEGFSSALSM DGPVLGAVGS FSWSGGAFLY PSNMRSTFIN MSQENEDMRD AYLGYSTALA
FWKGVHSLIL GAPRHQHTGK VVIFTQESRH WRPKSEVRGT QIGSYFGASL CSVDMDRDGS
TDLVLIGVPH YYEHTRGGQV SVCPMPGVRS RWHCGTTLHG EQGHPWGRFG AALTVLGDVN
GDSLADVAIG APGEEENRGA VYIFHGASRQ DIAPSPSQRV TGSQLFLRLQ YFGQSLSGGQ
DLTQDGLVDL AVGAQGHVLL LRSLPLLKVG ISIRFAPSEV AKTVYQCWGR TPTVLEAGEA
TVCLTVRKGS PDLLGDVQSS VRYDLALDPG RLISRAIFDE TKNCTLTRRK TLGLGDHCET
MKLLLPDCVE DAVTPIILRL NLSLAGDSAP SRNLRPVLAV GSQDHVTASF PFEKNCKQEL
LCEGNLGVSF NFSGLQVLEV GSSPELTVTV TVWNEGEDSY GTLIKFYYPA ELSYRRVTRA
QQPHPYPLRL ACEAEPTGQE SLRSSSCSIN HPIFREGAKA TFMITFDVSY KAFLGDRLLL
RASASSENNK PETSKTAFQL ELPVKYTVYT VISRQEDSTK HFNFSSSHGE RQKEAEHRYR
VNNLSPLTLA ISVNFWVPIL LNGVAVWDVT LRSPAQGVSC VSQREPPQHS DLLTQIQGRS
VLDCAIADCL HLRCDIPSLG TLDELDFILK GNLSFGWISQ TLQKKVLLLS EAEITFNTSV
YSQLPGQEAF LRAQVSTMLE EYVVYEPVFL MVFSSVGGLL LLALITVALY KLGFFKRQYK
EMLDLPSADP DPAGQADSNH ETPPHLTS
