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HB21_BOVIN
ID   HB21_BOVIN              Reviewed;         261 AA.
AC   Q9TVC8; O77825; Q95541;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=BoLa class II histocompatibility antigen, DQB*0101 beta chain;
DE            Short=DQB1*1A;
DE   Flags: Precursor;
GN   Name=BoLA-DQB {ECO:0000312|EMBL:CAA77078.1};
GN   Synonyms=DQB1 {ECO:0000312|EMBL:AAB21511.1};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1] {ECO:0000312|EMBL:CAA77078.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Blood {ECO:0000312|EMBL:CAA77078.1};
RX   PubMed=11132144; DOI=10.1007/s002510000257;
RA   Russell G.C.;
RT   "Sequence duplication at the 3' end of BoLA-DQB genes suggests multiple
RT   allelic lineages.";
RL   Immunogenetics 52:101-106(2000).
RN   [2] {ECO:0000312|EMBL:AAB21511.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-121.
RX   PubMed=1537611; DOI=10.1007/bf00185115;
RA   Sigurdardottir S., Borsch C., Gustafsson K., Andersson L.;
RT   "Gene duplications and sequence polymorphism of bovine class II DQB
RT   genes.";
RL   Immunogenetics 35:205-213(1992).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000255}.
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DR   EMBL; Y18201; CAA77078.1; -; mRNA.
DR   EMBL; S83910; AAB21511.1; -; Genomic_DNA.
DR   PIR; I47060; I47060.
DR   AlphaFoldDB; Q9TVC8; -.
DR   SMR; Q9TVC8; -.
DR   STRING; 9913.ENSBTAP00000026100; -.
DR   PRIDE; Q9TVC8; -.
DR   eggNOG; ENOG502RYBQ; Eukaryota.
DR   InParanoid; Q9TVC8; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..261
FT                   /note="BoLa class II histocompatibility antigen, DQB*0101
FT                   beta chain"
FT                   /id="PRO_5000147334"
FT   TOPO_DOM        33..230
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        252..261
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          129..233
FT                   /note="Ig-like C1-type"
FT                   /evidence="ECO:0000255"
FT   REGION          33..126
FT                   /note="Beta-1"
FT                   /evidence="ECO:0000255"
FT   REGION          127..220
FT                   /note="Beta-2"
FT                   /evidence="ECO:0000255"
FT   REGION          221..230
FT                   /note="Connecting peptide"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        47..111
FT                   /evidence="ECO:0000250|UniProtKB:P06343,
FT                   ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        149..205
FT                   /evidence="ECO:0000250|UniProtKB:P06343,
FT                   ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   261 AA;  30122 MW;  9BB83ABA7CCC49F8 CRC64;
     MSGMVALWIP RGLWTAVVMV TLVMLSTPGA EGRDSPKDFV YQFKGLCYFT NGTERVRYVT
     RYIYNQEENV RFDSDWDEYR AVTPLGRPDA EYFNSQKDFL EQTRAEADTV CRHNYQVEAP
     FTWQRQVEPT VTIFLSRTEA LNHHNLLVCS VTDFYPGQIK VRWFRNDQEE TAGVVATPLI
     RNGDWTFQLF MMLEMTPQRG DVYTCRVEHP SLQSPIMVEW RAQSESAQSK MLSGIGGFVL
     GLIFLGLGLI VHHRSQKGLM R
 
 
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