HB21_SPAEH
ID HB21_SPAEH Reviewed; 258 AA.
AC P15464;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=SMH class II histocompatibility antigen, beta-1 chain;
DE Flags: Precursor;
OS Spalax ehrenbergi (Middle East blind mole rat) (Nannospalax ehrenbergi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Spalacidae; Spalacinae; Nannospalax.
OX NCBI_TaxID=30637;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2833671; DOI=10.1093/oxfordjournals.molbev.a040439;
RA Schopfer R., Figueroa F., Nizetic D., Nevo E., Klein J.;
RT "Evolutionary diversification of class II P loci in the Mhc of the mole-rat
RT Spalax ehrenbergi.";
RL Mol. Biol. Evol. 4:287-299(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; M16685; AAA42354.1; -; Genomic_DNA.
DR EMBL; M16683; AAA42354.1; JOINED; Genomic_DNA.
DR EMBL; M16684; AAA42354.1; JOINED; Genomic_DNA.
DR PIR; A29088; A29088.
DR AlphaFoldDB; P15464; -.
DR SMR; P15464; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Adaptive immunity; Disulfide bond; Glycoprotein; Immunity; Membrane;
KW MHC II; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT CHAIN 30..258
FT /note="SMH class II histocompatibility antigen, beta-1
FT chain"
FT /id="PRO_0000019007"
FT TOPO_DOM 30..225
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 124..212
FT /note="Ig-like C1-type"
FT REGION 30..121
FT /note="Beta-1"
FT REGION 122..215
FT /note="Beta-2"
FT REGION 216..225
FT /note="Connecting peptide"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 144..200
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 258 AA; 29454 MW; CFB3CA0228D5D1A1 CRC64;
MMVLPVPVAP WTAALTVLLM VLNKSVVQGR TTPENYLFRA WQECHLTHGR YRYVERYIYN
QEEYVRFDSD VGVFRAVTEL GRSWADDFNS RKEALEQKRA APDTGCRHNH ELNQRLSQSL
IAQPKVHVSP SKGGTLNHHN LLVCQVTDFY PGNIQVRWFR NNQEETTGIS TTNPIRNGDW
TFQILVTLEM TPQRGDVYTC HVEHPSLDRP ITVEWRAQSD SARNKTLTGV GGLVLGLIFL
AVGLIMHVRS KKAQRGSR
