B2MG_RAT
ID B2MG_RAT Reviewed; 119 AA.
AC P07151;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Beta-2-microglobulin;
DE Flags: Precursor;
GN Name=B2m;
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 [MRNA].
RC STRAIN=Wistar;
RX PubMed=3309895; DOI=10.1093/nar/15.18.7638;
RA Mauxion F., Kress M.;
RT "Nucleotide sequence of rat beta 2-microglobulin cDNA.";
RL Nucleic Acids Res. 15:7638-7638(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=RT10 stock; TISSUE=Splenocyte;
RA le Rolle A.F., Butcher G.W., Joly E.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 21-39.
RC STRAIN=Wistar;
RX PubMed=2911353; DOI=10.1038/337184a0;
RA Simister N.E., Mostov K.E.;
RT "An Fc receptor structurally related to MHC class I antigens.";
RL Nature 337:184-187(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 65-119.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2689174; DOI=10.1111/j.1432-1033.1989.tb15174.x;
RA Cole T., Dickson P.W., Esnard F., Averill F., Risbridger G., Gauthier F.,
RA Schreiber G.;
RT "The cDNA structure and expression analysis of the genes for the cysteine
RT proteinase inhibitor cystatin C and for beta 2-microglobulin in rat
RT brain.";
RL Eur. J. Biochem. 186:35-42(1989).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=7969498; DOI=10.1038/372379a0;
RA Burmeister W.P., Huber A.H., Bjorkman P.J.;
RT "Crystal structure of the complex of rat neonatal Fc receptor with Fc.";
RL Nature 372:379-383(1994).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=9493268; DOI=10.1016/s0969-2126(98)00008-2;
RA Vaughn D.E., Bjorkman P.J.;
RT "Structural basis of pH-dependent antibody binding by the neonatal Fc
RT receptor.";
RL Structure 6:63-73(1998).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS).
RX PubMed=11163232; DOI=10.1016/s1074-7613(01)00091-7;
RA Speir J.A., Stevens J., Joly E., Butcher G.W., Wilson I.A.;
RT "Two different, highly exposed, bulged structures for an unusually long
RT peptide bound to rat MHC class I RT1-A(a).";
RL Immunity 14:81-92(2001).
CC -!- FUNCTION: Component of the class I major histocompatibility complex
CC (MHC). Involved in the presentation of peptide antigens to the immune
CC system.
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. Forms a heterotrimer with MR1 and a metabolite
CC antigen. {ECO:0000250|UniProtKB:P61769}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the beta-2-microglobulin family. {ECO:0000305}.
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DR EMBL; Y00441; CAA68498.1; -; mRNA.
DR EMBL; Y08531; CAA69847.1; -; mRNA.
DR EMBL; X16956; CAA34830.1; -; mRNA.
DR PIR; A26842; A26842.
DR RefSeq; NP_036644.1; NM_012512.2.
DR PDB; 1ED3; X-ray; 2.55 A; B/E=21-119.
DR PDB; 1FRT; X-ray; 4.50 A; B=21-119.
DR PDB; 1I1A; X-ray; 2.80 A; B=21-119.
DR PDB; 1KJM; X-ray; 2.35 A; B=21-119.
DR PDB; 1KJV; X-ray; 1.48 A; B=21-119.
DR PDB; 3FRU; X-ray; 2.20 A; B/D/F=21-119.
DR PDB; 6NF7; X-ray; 2.90 A; B/E/H/K/N=21-119.
DR PDBsum; 1ED3; -.
DR PDBsum; 1FRT; -.
DR PDBsum; 1I1A; -.
DR PDBsum; 1KJM; -.
DR PDBsum; 1KJV; -.
DR PDBsum; 3FRU; -.
DR PDBsum; 6NF7; -.
DR AlphaFoldDB; P07151; -.
DR SMR; P07151; -.
DR BioGRID; 246411; 2.
DR IntAct; P07151; 3.
DR MINT; P07151; -.
DR STRING; 10116.ENSRNOP00000023017; -.
DR iPTMnet; P07151; -.
DR PhosphoSitePlus; P07151; -.
DR PaxDb; P07151; -.
DR PRIDE; P07151; -.
DR Ensembl; ENSRNOT00000023017; ENSRNOP00000023017; ENSRNOG00000017123.
DR GeneID; 24223; -.
DR KEGG; rno:24223; -.
DR UCSC; RGD:2189; rat.
DR CTD; 567; -.
DR RGD; 2189; B2m.
DR eggNOG; ENOG502S8GM; Eukaryota.
DR GeneTree; ENSGT00690000102227; -.
DR HOGENOM; CLU_163066_0_0_1; -.
DR InParanoid; P07151; -.
DR OMA; FHPPKID; -.
DR OrthoDB; 1556447at2759; -.
DR PhylomeDB; P07151; -.
DR TreeFam; TF334167; -.
DR Reactome; R-RNO-1236974; ER-Phagosome pathway.
DR Reactome; R-RNO-1236977; Endosomal/Vacuolar pathway.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-RNO-2172127; DAP12 interactions.
DR Reactome; R-RNO-2424491; DAP12 signaling.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR EvolutionaryTrace; P07151; -.
DR PRO; PR:P07151; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000017123; Expressed in lung and 19 other tissues.
DR Genevisible; P07151; RN.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:1990712; C:HFE-transferrin receptor complex; ISO:RGD.
DR GO; GO:0042824; C:MHC class I peptide loading complex; ISO:RGD.
DR GO; GO:0042612; C:MHC class I protein complex; IEA:UniProtKB-KW.
DR GO; GO:0042613; C:MHC class II protein complex; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0023026; F:MHC class II protein complex binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:1990000; P:amyloid fibril formation; ISO:RGD.
DR GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; ISO:RGD.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IBA:GO_Central.
DR GO; GO:0002481; P:antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent; ISO:RGD.
DR GO; GO:0071281; P:cellular response to iron ion; ISO:RGD.
DR GO; GO:0071283; P:cellular response to iron(III) ion; ISO:RGD.
DR GO; GO:0071316; P:cellular response to nicotine; ISO:RGD.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0055072; P:iron ion homeostasis; ISO:RGD.
DR GO; GO:0006826; P:iron ion transport; ISO:RGD.
DR GO; GO:0007611; P:learning or memory; ISO:RGD.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:RGD.
DR GO; GO:2000978; P:negative regulation of forebrain neuron differentiation; ISO:RGD.
DR GO; GO:0050768; P:negative regulation of neurogenesis; ISO:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:RGD.
DR GO; GO:1900121; P:negative regulation of receptor binding; ISO:RGD.
DR GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IBA:GO_Central.
DR GO; GO:2000774; P:positive regulation of cellular senescence; ISO:RGD.
DR GO; GO:1904434; P:positive regulation of ferrous iron binding; ISO:RGD.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:RGD.
DR GO; GO:1900122; P:positive regulation of receptor binding; ISO:RGD.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISO:RGD.
DR GO; GO:0050870; P:positive regulation of T cell activation; IBA:GO_Central.
DR GO; GO:0002726; P:positive regulation of T cell cytokine production; ISO:RGD.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; ISO:RGD.
DR GO; GO:1904437; P:positive regulation of transferrin receptor binding; ISO:RGD.
DR GO; GO:0051289; P:protein homotetramerization; ISO:RGD.
DR GO; GO:0042026; P:protein refolding; ISO:RGD.
DR GO; GO:0045646; P:regulation of erythrocyte differentiation; ISO:RGD.
DR GO; GO:0034756; P:regulation of iron ion transport; ISO:RGD.
DR GO; GO:0046686; P:response to cadmium ion; IEP:RGD.
DR GO; GO:0002237; P:response to molecule of bacterial origin; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007608; P:sensory perception of smell; ISO:RGD.
DR GO; GO:0033077; P:T cell differentiation in thymus; ISO:RGD.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Immunity;
KW Immunoglobulin domain; MHC I; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:2911353"
FT CHAIN 21..119
FT /note="Beta-2-microglobulin"
FT /id="PRO_0000018790"
FT DOMAIN 25..114
FT /note="Ig-like C1-type"
FT DISULFID 45..100
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:1KJV"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1KJM"
FT STRAND 41..53
FT /evidence="ECO:0007829|PDB:1KJV"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:1KJV"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:1KJV"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:1KJV"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1KJV"
SQ SEQUENCE 119 AA; 13720 MW; 3BE0A869E236DDFB CRC64;
MARSVTVIFL VLVSLAVVLA IQKTPQIQVY SRHPPENGKP NFLNCYVSQF HPPQIEIELL
KNGKKIPNIE MSDLSFSKDW SFYILAHTEF TPTETDVYAC RVKHVTLKEP KTVTWDRDM
