DOB_PANTR
ID DOB_PANTR Reviewed; 273 AA.
AC P18467;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Patr class II histocompatibility antigen, DO beta chain;
DE AltName: Full=ChLa class II histocompatibility antigen, DO beta chain;
DE AltName: Full=MHC class II antigen DOB;
DE Flags: Precursor;
GN Name=Patr-DOB;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2744808; DOI=10.1007/bf02421475;
RA Kasahara M., Klein D., Klein J.;
RT "Nucleotide sequence of a chimpanzee DOB cDNA clone.";
RL Immunogenetics 30:66-68(1989).
CC -!- FUNCTION: Important modulator in the HLA class II restricted antigen
CC presentation pathway by interaction with the HLA-DM molecule in B-
CC cells. Modifies peptide exchange activity of HLA-DM.
CC -!- SUBUNIT: Heterodimer of an alpha chain (DOA) and a beta chain (DOB).
CC Forms a heterotetrameric complex with an HLA-DM molecule during
CC intracellular transport in endosomal/lysosomal compartments in B-cells.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Single-pass type
CC I membrane protein {ECO:0000250}. Lysosome membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}. Note=Complexes with
CC HLA-DM molecule during intracellular transport and in
CC endosomal/lysosomal compartments. Heterotetramerization is necessary to
CC exit the ER.
CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
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DR EMBL; M24358; AAA35409.1; -; mRNA.
DR PIR; A45879; A45879.
DR RefSeq; NP_001123943.1; NM_001130471.1.
DR AlphaFoldDB; P18467; -.
DR SMR; P18467; -.
DR STRING; 9598.ENSPTRP00000030772; -.
DR PaxDb; P18467; -.
DR GeneID; 471977; -.
DR KEGG; ptr:471977; -.
DR CTD; 471977; -.
DR eggNOG; ENOG502RWX2; Eukaryota.
DR InParanoid; P18467; -.
DR OrthoDB; 1249505at2759; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042613; C:MHC class II protein complex; IBA:GO_Central.
DR GO; GO:0023026; F:MHC class II protein complex binding; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IBA:GO_Central.
DR GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IBA:GO_Central.
DR GO; GO:0050870; P:positive regulation of T cell activation; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.10.320.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR InterPro; IPR014745; MHC_II_a/b_N.
DR InterPro; IPR000353; MHC_II_b_N.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF00969; MHC_II_beta; 1.
DR SMART; SM00407; IGc1; 1.
DR SMART; SM00921; MHC_II_beta; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF54452; SSF54452; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
PE 2: Evidence at transcript level;
KW Adaptive immunity; Disulfide bond; Endosome; Glycoprotein; Immunity;
KW Lysosome; Membrane; MHC II; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT CHAIN 27..273
FT /note="Patr class II histocompatibility antigen, DO beta
FT chain"
FT /id="PRO_0000018964"
FT TOPO_DOM 27..224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 123..213
FT /note="Ig-like C1-type"
FT REGION 27..120
FT /note="Beta-1"
FT REGION 121..214
FT /note="Beta-2"
FT REGION 215..224
FT /note="Connecting peptide"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 143..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 273 AA; 30922 MW; 8AC0A1F56A06D30D CRC64;
MGSGWVPWVV ALLVNLTRLD SSMTQGTDSP EDFVIQAKAD CYFTNGTEKV QFVVRFIFNL
EEYVRFDSDV GMFVALTKLG QPDAEQWNSR LDLLERSRQA VDGVCRHNYR LGAPFTVGRK
VQPEVTVYPE RTPLLHQHNL LHCSVTGFYP GDIKIRWFLN GQEERARVMS TGPIRNGDWT
FQTVVMLEMT PELGHVYTCL VDHSSLLSPV SVEWRAQSEY SWKKMLSGIA AFLLGLIFLL
VGIVIQLRAQ KGYVRTQMSG NEVSRAVLLP QSC