HB2D_CANLF
ID HB2D_CANLF Reviewed; 266 AA.
AC P18470;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=DLA class II histocompatibility antigen, DR-1 beta chain;
DE Flags: Precursor;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2370085; DOI=10.1007/bf02115018;
RA Sarmiento U.M., Storb R.;
RT "Nucleotide sequence of a dog DRB cDNA clone.";
RL Immunogenetics 31:396-399(1990).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}.
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DR EMBL; M29611; AAA30874.1; -; mRNA.
DR PIR; A45844; A45844.
DR RefSeq; NP_001014768.1; NM_001014768.1.
DR AlphaFoldDB; P18470; -.
DR SMR; P18470; -.
DR STRING; 9612.ENSCAFP00000001156; -.
DR PaxDb; P18470; -.
DR GeneID; 474860; -.
DR KEGG; cfa:474860; -.
DR CTD; 3123; -.
DR eggNOG; ENOG502RYBQ; Eukaryota.
DR OrthoDB; 1249505at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
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; Glycoprotein; Immunity; Membrane;
KW MHC II; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT CHAIN 30..266
FT /note="DLA class II histocompatibility antigen, DR-1 beta
FT chain"
FT /id="PRO_0000019010"
FT TOPO_DOM 30..227
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 126..214
FT /note="Ig-like C1-type"
FT REGION 30..124
FT /note="Beta-1"
FT REGION 125..227
FT /note="Beta-2"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 146..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 266 AA; 30151 MW; 4E8297BBF1ACDD67 CRC64;
MVCLCFLGGS WMTALMLILM VLNPPFAWAR DTPPHFLEVA KSECYFTNGT ERVRFVERYI
HNREEFVRFD SDVGEFRAVT ELGRPVAESW NGQKEILEQE RATVDTYCRH NYGVIESFTV
QRRVEPTVTV YPTKTQTLQH HNLLVCSVNG FYPGHIEVRW LRNGQEEEAG VVSTGLIRNG
DWTFQILVML EIVPQSGEVY TCQVEHPSLT SPVTVEWRAQ SDSAQSKMLS GIGGFVLGLL
FLAVGLFIYF RNQKGHSGLQ PTGLLS