ID   B2MG_PAPAN              Reviewed;         119 AA.
AC   Q6T672;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Beta-2-microglobulin;
DE   Flags: Precursor;
GN   Name=B2M;
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Term placenta;
RA   Langat D.K., Morales P.J., Fazleabas A.T., Hunt J.S.;
RT   "Sequence of the olive baboon (Papio anubis) beta-2-microglobulin.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the class I major histocompatibility complex
CC       (MHC). Involved in the presentation of peptide antigens to the immune
CC       system (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain. Beta-2-
CC       microglobulin is the beta-chain of major histocompatibility complex
CC       class I molecules (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the beta-2-microglobulin family. {ECO:0000305}.
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DR   EMBL; AY434098; AAR12070.1; -; mRNA.
DR   RefSeq; NP_001167006.1; NM_001173535.1.
DR   AlphaFoldDB; Q6T672; -.
DR   SMR; Q6T672; -.
DR   STRING; 9555.ENSPANP00000013995; -.
DR   Ensembl; ENSPANT00000026151; ENSPANP00000013995; ENSPANG00000018027.
DR   GeneID; 100381194; -.
DR   KEGG; panu:100381194; -.
DR   CTD; 567; -.
DR   eggNOG; ENOG502S8GM; Eukaryota.
DR   GeneTree; ENSGT00690000102227; -.
DR   HOGENOM; CLU_163066_0_0_1; -.
DR   OMA; FHPPKID; -.
DR   OrthoDB; 1556447at2759; -.
DR   Proteomes; UP000028761; Chromosome 7.
DR   Bgee; ENSPANG00000018027; Expressed in perirenal fat and 65 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:1990712; C:HFE-transferrin receptor complex; IEA:Ensembl.
DR   GO; GO:0042824; C:MHC class I peptide loading complex; IEA:Ensembl.
DR   GO; GO:0042612; C:MHC class I protein complex; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:1990000; P:amyloid fibril formation; IEA:Ensembl.
DR   GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; IEA:Ensembl.
DR   GO; GO:0002481; P:antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent; IEA:Ensembl.
DR   GO; GO:0071283; P:cellular response to iron(III) ion; IEA:Ensembl.
DR   GO; GO:0071316; P:cellular response to nicotine; IEA:Ensembl.
DR   GO; GO:0055072; P:iron ion homeostasis; IEA:Ensembl.
DR   GO; GO:0006826; P:iron ion transport; IEA:Ensembl.
DR   GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:2000978; P:negative regulation of forebrain neuron differentiation; IEA:Ensembl.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; IEA:Ensembl.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR   GO; GO:1900121; P:negative regulation of receptor binding; IEA:Ensembl.
DR   GO; GO:2000774; P:positive regulation of cellular senescence; IEA:Ensembl.
DR   GO; GO:1904434; P:positive regulation of ferrous iron binding; IEA:Ensembl.
DR   GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IEA:Ensembl.
DR   GO; GO:0002726; P:positive regulation of T cell cytokine production; IEA:Ensembl.
DR   GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:Ensembl.
DR   GO; GO:1904437; P:positive regulation of transferrin receptor binding; IEA:Ensembl.
DR   GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
DR   GO; GO:0042026; P:protein refolding; IEA:Ensembl.
DR   GO; GO:0045646; P:regulation of erythrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0034756; P:regulation of iron ion transport; IEA:Ensembl.
DR   GO; GO:0002237; P:response to molecule of bacterial origin; IEA:Ensembl.
DR   GO; GO:0007608; P:sensory perception of smell; IEA:Ensembl.
DR   GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
DR   GO; GO:0001913; P:T cell mediated cytotoxicity; IEA:Ensembl.
DR   CDD; cd05770; IgC_beta2m; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR015707; B2Microglobulin.
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   PANTHER; PTHR19944:SF62; PTHR19944:SF62; 1.
DR   Pfam; PF07654; C1-set; 1.
DR   SMART; SM00407; IGc1; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00290; IG_MHC; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Immunity; Immunoglobulin domain; MHC I; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..119
FT                   /note="Beta-2-microglobulin"
FT                   /id="PRO_0000018786"
FT   DOMAIN          25..114
FT                   /note="Ig-like C1-type"
FT   DISULFID        45..100
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   119 AA;  13626 MW;  511F59EF5FB64D71 CRC64;
     MSRSVALAVL ALLSLSGLEA IQRTPKIQVY SRHPPENGKP NFLNCYVSGF HPSDIEVDLL
     KNGEKMGKVE HSDLSFSKDW SFYLLYYTEF TPNEKDEYAC RVNHVTLSGP RTVKWDRDM