ITAD_RAT
ID ITAD_RAT Reviewed; 1161 AA.
AC Q9QYE7;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Integrin alpha-D;
DE AltName: CD_antigen=CD11d;
DE Flags: Precursor;
GN Name=Itgad; Synonyms=Itgax;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA O'Brien M.M., VanderVieren M., Kilgannon P.D., Dietsch G., Gallatin W.M.;
RT "Cloning of rat alpha D, a novel beta 2 integrin.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
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; AF021334; AAF21241.1; -; mRNA.
DR RefSeq; NP_113879.1; NM_031691.1.
DR AlphaFoldDB; Q9QYE7; -.
DR SMR; Q9QYE7; -.
DR STRING; 10116.ENSRNOP00000026855; -.
DR GlyGen; Q9QYE7; 10 sites.
DR PaxDb; Q9QYE7; -.
DR PRIDE; Q9QYE7; -.
DR GeneID; 64350; -.
DR KEGG; rno:64350; -.
DR UCSC; RGD:71075; rat.
DR CTD; 3681; -.
DR RGD; 71075; Itgad.
DR eggNOG; KOG3637; Eukaryota.
DR InParanoid; Q9QYE7; -.
DR OrthoDB; 73876at2759; -.
DR PhylomeDB; Q9QYE7; -.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR PRO; PR:Q9QYE7; -.
DR Proteomes; UP000002494; Unplaced.
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; IPI:RGD.
DR GO; GO:0050798; P:activated T cell proliferation; ISO:RGD.
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:RGD.
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 2: Evidence at transcript 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..1161
FT /note="Integrin alpha-D"
FT /id="PRO_0000016297"
FT TOPO_DOM 20..1100
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1101..1121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1122..1161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 21..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..334
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 1126..1130
FT /note="GFFKR motif"
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 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
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 696
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 784
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 907
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 936
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 69..76
FT /evidence="ECO:0000250"
FT DISULFID 108..126
FT /evidence="ECO:0000250"
FT DISULFID 656..711
FT /evidence="ECO:0000250"
FT DISULFID 769..775
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"
SQ SEQUENCE 1161 AA; 126600 MW; 2258491A984A705E CRC64;
MAGGVVILLC GWVLASCHGS NLDVEEPIVF REDAASFGQT VVQFGGSRLV VGAPLEAVAV
NQTGRLYDCA PATGMCQPIV LRSPLEAVNM SLGLSLVTAT NNAQLLACGP TAQRACVKNM
YAKGSCLLLG SSLQFIQAVP ASMPECPRQE MDIAFLIDGS GSINQRDFAQ MKDFVKALMG
EFASTSTLFS LMQYSNILKT HFTFTEFKNI LDPQSLVDPI VQLQGLTYTA TGIRTVMEEL
FHSKNGSRKS AKKILLVITD GQKYRDPLEY SDVIPAADKA GIIRYAIGVG DAFQEPTALK
ELNTIGSAPP QDHVFKVGNF AALRSIQRQL QEKIFAIEGT QSRSSSSFQH EMSQEGFSSA
LTSDGPVLGA VGSFSWSGGA FLYPPNTRPT FINMSQENVD MRDSYLGYST AVAFWKGVHS
LILGAPRHQH TGKVVIFTQE ARHWRPKSEV RGTQIGSYFG ASLCSVDVDR DGSTDLVLIG
APHYYEQTRG GQVSVFPVPG VRGRWQCEAT LHGEQGHPWG RFGVALTVLG DVNGDNLADV
AIGAPGEEES RGAVYIFHGA SRLEIMPSPS QRVTGSQLSL RLQYFGQSLS GGQDLTQDGL
VDLAVGAQGH VLLLRSLPLL KVELSIRFAP MEVAKAVYQC WERTPTVLEA GEATVCLTVH
KGSPDLLGNV QGSVRYDLAL DPGRLISRAI FDETKNCTLT GRKTLGLGDH CETVKLLLPD
CVEDAVSPII LRLNFSLVRD SASPRNLHPV LAVGSQDHIT ASLPFEKNCK QELLCEGDLG
ISFNFSGLQV LVVGGSPELT VTVTVWNEGE DSYGTLVKFY YPAGLSYRRV TGTQQPHQYP
LRLACEAEPA AQEDLRSSSC SINHPIFREG AKTTFMITFD VSYKAFLGDR LLLRAKASSE
NNKPDTNKTA FQLELPVKYT VYTLISRQED STNHVNFSSS HGGRRQEAAH RYRVNNLSPL
KLAVRVNFWV PVLLNGVAVW DVTLSSPAQG VSCVSQMKPP QNPDFLTQIQ RRSVLDCSIA
DCLHFRCDIP SLDIQDELDF ILRGNLSFGW VSQTLQEKVL LVSEAEITFD TSVYSQLPGQ
EAFLRAQVET TLEEYVVYEP IFLVAGSSVG GLLLLALITV VLYKLGFFKR QYKEMLDGKA
ADPVTAGQAD FGCETPPYLV S
