B2MG_CALJA
ID B2MG_CALJA Reviewed; 119 AA.
AC P63061; O77522;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Beta-2-microglobulin;
DE Flags: Precursor;
GN Name=B2M;
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10380996;
RX DOI=10.1002/(sici)1098-2345(1999)48:3<225::aid-ajp4>3.0.co;2-4;
RA Canavez F.C., Moreira M.A.M., Simon F., Parham P., Seuanez H.N.;
RT "Phylogenetic relationships of the Callitrichinae (Platyrrhini, primates)
RT based on beta2-microglobulin DNA sequences.";
RL Am. J. Primatol. 48:225-236(1999).
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; AF084624; AAF21790.1; -; Genomic_DNA.
DR EMBL; AF084622; AAF21790.1; JOINED; Genomic_DNA.
DR EMBL; AF084623; AAF21790.1; JOINED; Genomic_DNA.
DR RefSeq; XP_002753457.2; XM_002753411.4.
DR AlphaFoldDB; P63061; -.
DR SMR; P63061; -.
DR STRING; 9483.ENSCJAP00000004290; -.
DR Ensembl; ENSCJAT00000053960; ENSCJAP00000048032; ENSCJAG00000002377.
DR GeneID; 100404307; -.
DR KEGG; cjc:100404307; -.
DR CTD; 567; -.
DR eggNOG; ENOG502S8GM; Eukaryota.
DR GeneTree; ENSGT00690000102227; -.
DR HOGENOM; CLU_163066_0_0_1; -.
DR InParanoid; P63061; -.
DR Proteomes; UP000008225; Chromosome 10.
DR Bgee; ENSCJAG00000002377; Expressed in kidney and 6 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_0000018764"
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; 13552 MW; BB40481BF10DECEB CRC64;
MASSVVVALL VLLSLSGLEA IQHAPKIQVY SRHPAENGKP NFLNCYVSGF HPSDIEVDLL
KNGKKIEKVE HSDLSFSKDW SFYLLYYTEF TPSEKDEYAC RVSHVTFSTP KTVKWDRNI
