ID   HA2B_RAT                Reviewed;         256 AA.
AC   P20037;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Rano class II histocompatibility antigen, B alpha chain;
DE   AltName: Full=RT1 class II antigen, Ba chain;
DE   Flags: Precursor;
GN   Name=RT1-Ba;
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 [GENOMIC DNA].
RX   PubMed=3610254; DOI=10.1007/bf00345455;
RA   Barran P.A., McMaster W.R.;
RT   "DNA sequence analysis of the rat RT1.B alpha gene.";
RL   Immunogenetics 26:56-62(1987).
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; M22366; AAA42083.1; -; Genomic_DNA.
DR   EMBL; M31014; AAA42083.1; JOINED; Genomic_DNA.
DR   PIR; S02855; S02855.
DR   AlphaFoldDB; P20037; -.
DR   SMR; P20037; -.
DR   GlyGen; P20037; 1 site.
DR   UCSC; RGD:1595867; rat.
DR   RGD; 1595867; RT1-Ba.
DR   InParanoid; P20037; -.
DR   PhylomeDB; P20037; -.
DR   Reactome; R-RNO-202424; Downstream TCR signaling.
DR   Reactome; R-RNO-202427; Phosphorylation of CD3 and TCR zeta chains.
DR   Reactome; R-RNO-202430; Translocation of ZAP-70 to Immunological synapse.
DR   Reactome; R-RNO-202433; Generation of second messenger molecules.
DR   Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR   Reactome; R-RNO-389948; PD-1 signaling.
DR   PRO; PR:P20037; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005764; C:lysosome; ISO:RGD.
DR   GO; GO:0042613; C:MHC class II protein complex; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0023026; F:MHC class II protein complex binding; IBA:GO_Central.
DR   GO; GO:0042605; F:peptide antigen binding; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0019882; P:antigen processing and presentation; ISO:RGD.
DR   GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; ISO:RGD.
DR   GO; GO:0048002; P:antigen processing and presentation of peptide antigen; ISO:RGD.
DR   GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEP:RGD.
DR   GO; GO:0042130; P:negative regulation of T cell proliferation; IDA:RGD.
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   GO; GO:0045582; P:positive regulation of T cell differentiation; ISO:RGD.
DR   GO; GO:0034341; P:response to interferon-gamma; ISO:RGD.
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; IPR001003; MHC_II_a_N.
DR   Pfam; PF07654; C1-set; 1.
DR   Pfam; PF00993; MHC_II_alpha; 1.
DR   SMART; SM00407; IGc1; 1.
DR   SMART; SM00920; MHC_II_alpha; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   SUPFAM; SSF54452; SSF54452; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00290; IG_MHC; 1.
PE   3: Inferred from homology;
KW   Adaptive immunity; Disulfide bond; Glycoprotein; Immunity; Membrane;
KW   MHC II; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT   CHAIN           24..256
FT                   /note="Rano class II histocompatibility antigen, B alpha
FT                   chain"
FT                   /id="PRO_0000018983"
FT   TOPO_DOM        24..218
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        219..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        245..256
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          108..206
FT                   /note="Ig-like C1-type"
FT   REGION          24..111
FT                   /note="Alpha-1"
FT   REGION          112..205
FT                   /note="Alpha-2"
FT   REGION          206..218
FT                   /note="Connecting peptide"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        134..190
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   256 AA;  28602 MW;  D09526BDA8950764 CRC64;
     MPLSRALILG VLALTTMLSP CGGQDDIEAD HVGSYGITVY QYHESKGQYT HEFDGDERFY
     VDLDKKETIW RIPEFGQLIS FDPQGALRNI AIIKHNLEIL MKRSNSTPAV NEVPEATVFS
     KSPVLLGQPN TLICFVDNIF PPVINITWLR NSKPLTEGVY ETSFLINSDY SFHKMAYLTF
     IPSNDDIYDC KVEHWSLDEP VLRHWEPEIP APMSELTETV VCALGLSVGL VGIVVGTIFI
     IQGLRSVAPS RHPGPL