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Integrin alpha-D (CD antigen CD11d)

 ITAD_MOUSE              Reviewed;        1168 AA.
Q3V0T4;
07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
11-OCT-2005, sequence version 1.
22-NOV-2017, entry version 84.
RecName: Full=Integrin alpha-D;
AltName: CD_antigen=CD11d;
Flags: Precursor;
Name=Itgad;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-D
associates with beta-2 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
membrane protein {ECO:0000250}.
-!- 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}.
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EMBL; AK132915; BAE21419.1; -; mRNA.
UniGene; Mm.334257; -.
ProteinModelPortal; Q3V0T4; -.
SMR; Q3V0T4; -.
STRING; 10090.ENSMUSP00000033051; -.
iPTMnet; Q3V0T4; -.
PhosphoSitePlus; Q3V0T4; -.
MaxQB; Q3V0T4; -.
PaxDb; Q3V0T4; -.
PRIDE; Q3V0T4; -.
Ensembl; ENSMUST00000106237; ENSMUSP00000101844; ENSMUSG00000070369.
UCSC; uc009jyd.2; mouse.
MGI; MGI:3578624; Itgad.
eggNOG; KOG3637; Eukaryota.
eggNOG; ENOG410XPVZ; LUCA.
GeneTree; ENSGT00760000118782; -.
HOGENOM; HOG000113114; -.
HOVERGEN; HBG100530; -.
InParanoid; Q3V0T4; -.
PhylomeDB; Q3V0T4; -.
Reactome; R-MMU-216083; Integrin cell surface interactions.
PRO; PR:Q3V0T4; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000070369; -.
CleanEx; MM_ITGAD; -.
ExpressionAtlas; Q3V0T4; baseline and differential.
GO; GO:0008305; C:integrin complex; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050798; P:activated T cell proliferation; IMP:MGI.
GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:MGI.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
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; IPR032695; Integrin_dom_sf.
InterPro; IPR002035; VWF_A.
InterPro; IPR036465; vWFA_dom_sf.
Pfam; PF01839; FG-GAP; 2.
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 26 {ECO:0000255}.
CHAIN 27 1168 Integrin alpha-D.
/FTId=PRO_0000045902.
TOPO_DOM 27 1107 Extracellular. {ECO:0000255}.
TRANSMEM 1108 1128 Helical. {ECO:0000255}.
TOPO_DOM 1129 1168 Cytoplasmic. {ECO:0000255}.
REPEAT 28 85 FG-GAP 1. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 86 145 FG-GAP 2. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
DOMAIN 159 341 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
REPEAT 348 399 FG-GAP 3. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 400 451 FG-GAP 4. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 452 512 FG-GAP 5. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 515 573 FG-GAP 6. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
REPEAT 578 638 FG-GAP 7. {ECO:0000255|PROSITE-
ProRule:PRU00803}.
CA_BIND 474 482 {ECO:0000255}.
CA_BIND 538 546 {ECO:0000255}.
CA_BIND 601 609 {ECO:0000255}.
MOTIF 1133 1137 GFFKR motif.
CARBOHYD 68 68 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 96 96 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 108 108 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 400 400 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 703 703 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 741 741 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 791 791 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 943 943 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1052 1052 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1077 1077 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 76 83 {ECO:0000250}.
DISULFID 115 133 {ECO:0000250}.
DISULFID 663 718 {ECO:0000250}.
DISULFID 776 782 {ECO:0000250}.
DISULFID 852 867 {ECO:0000250}.
DISULFID 1000 1024 {ECO:0000250}.
DISULFID 1029 1034 {ECO:0000250}.
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


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