B2MG_BOVIN
ID B2MG_BOVIN Reviewed; 118 AA.
AC P01888; Q148G6; Q56K05;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Beta-2-microglobulin;
DE AltName: Full=Lactollin;
DE Flags: Precursor;
GN Name=B2M;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8319984; DOI=10.1007/bf00188812;
RA Ellis S.A., Braem K.A., Payne L.;
RT "Nucleotide sequence of cattle beta 2-microglobulin cDNA.";
RL Immunogenetics 38:310-310(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymphoid epithelium;
RA Yu J., Meng Y., Wang Z., Hansen C., Li C., Moore S.S.;
RT "Analysis of sequences obtained from constructed full-length bovine cDNA
RT libraries.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 21-118.
RX PubMed=6174509; DOI=10.1016/s0021-9258(18)34969-x;
RA Groves M.L., Greenberg R.;
RT "Complete amino acid sequence of bovine beta 2-microglobulin.";
RL J. Biol. Chem. 257:2619-2626(1982).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX PubMed=3889925; DOI=10.1073/pnas.82.12.4225;
RA Becker J.W., Reeke G.N. Jr.;
RT "Three-dimensional structure of beta 2-microglobulin.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:4225-4229(1985).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) OF 21-118 IN COMPLEX WITH MR1, AND
RP DISULFIDE BOND.
RX PubMed=23613577; DOI=10.1073/pnas.1222678110;
RA Lopez-Sagaseta J., Dulberger C.L., Crooks J.E., Parks C.D., Luoma A.M.,
RA McFedries A., Van Rhijn I., Saghatelian A., Adams E.J.;
RT "The molecular basis for Mucosal-Associated Invariant T cell recognition of
RT MR1 proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E1771-E1778(2013).
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 (PubMed:23613577). Forms a heterotrimer with MR1 and
CC a metabolite antigen (By similarity). {ECO:0000250|UniProtKB:P61769,
CC ECO:0000269|PubMed:23613577}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the beta-2-microglobulin family. {ECO:0000305}.
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DR EMBL; X69084; CAA48828.1; -; mRNA.
DR EMBL; AY911322; AAW82090.1; -; mRNA.
DR EMBL; BC118352; AAI18353.1; -; mRNA.
DR PIR; I46000; MGBOB2.
DR RefSeq; NP_776318.1; NM_173893.3.
DR RefSeq; XP_001251108.1; XM_001251107.5.
DR RefSeq; XP_002691165.1; XM_002691119.3.
DR PDB; 1BMG; X-ray; 2.50 A; A=21-118.
DR PDB; 2XFX; X-ray; 1.90 A; B=20-118.
DR PDB; 3L9R; X-ray; 2.30 A; B/D/F/H=21-118.
DR PDB; 3PWV; X-ray; 2.70 A; B/E=21-118.
DR PDB; 4F7C; X-ray; 2.86 A; B/D=21-118.
DR PDB; 4F7E; X-ray; 2.40 A; B=21-118.
DR PDB; 4IIQ; X-ray; 2.86 A; C=21-118.
DR PDB; 4L8S; X-ray; 2.90 A; C=21-118.
DR PDB; 4L9L; X-ray; 3.40 A; C=21-118.
DR PDB; 4LCC; X-ray; 3.26 A; C=21-118.
DR PDBsum; 1BMG; -.
DR PDBsum; 2XFX; -.
DR PDBsum; 3L9R; -.
DR PDBsum; 3PWV; -.
DR PDBsum; 4F7C; -.
DR PDBsum; 4F7E; -.
DR PDBsum; 4IIQ; -.
DR PDBsum; 4L8S; -.
DR PDBsum; 4L9L; -.
DR PDBsum; 4LCC; -.
DR AlphaFoldDB; P01888; -.
DR SMR; P01888; -.
DR STRING; 9913.ENSBTAP00000016359; -.
DR CarbonylDB; P01888; -.
DR PaxDb; P01888; -.
DR PeptideAtlas; P01888; -.
DR PRIDE; P01888; -.
DR Ensembl; ENSBTAT00000016359; ENSBTAP00000016359; ENSBTAG00000012330.
DR GeneID; 280729; -.
DR GeneID; 783680; -.
DR KEGG; bta:280729; -.
DR KEGG; bta:783680; -.
DR CTD; 567; -.
DR VEuPathDB; HostDB:ENSBTAG00000012330; -.
DR eggNOG; ENOG502S8GM; Eukaryota.
DR GeneTree; ENSGT00690000102227; -.
DR HOGENOM; CLU_163066_0_0_1; -.
DR InParanoid; P01888; -.
DR OMA; FHPPKID; -.
DR OrthoDB; 1556447at2759; -.
DR TreeFam; TF334167; -.
DR Reactome; R-BTA-1236974; ER-Phagosome pathway.
DR Reactome; R-BTA-1236977; Endosomal/Vacuolar pathway.
DR Reactome; R-BTA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-BTA-2424491; DAP12 signaling.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Reactome; R-BTA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR EvolutionaryTrace; P01888; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000012330; Expressed in monocyte and 106 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0023026; F:MHC class II protein complex binding; IBA:GO_Central.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IBA:GO_Central.
DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
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 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:6174509"
FT CHAIN 21..118
FT /note="Beta-2-microglobulin"
FT /id="PRO_0000018756"
FT DOMAIN 25..112
FT /note="Ig-like C1-type"
FT DISULFID 45..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:23613577"
FT CONFLICT 37
FT /note="D -> N (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="N -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="Q -> E (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:2XFX"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:4IIQ"
FT STRAND 41..53
FT /evidence="ECO:0007829|PDB:2XFX"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:2XFX"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:4IIQ"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:4F7C"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1BMG"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:1BMG"
FT STRAND 81..89
FT /evidence="ECO:0007829|PDB:2XFX"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:2XFX"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:2XFX"
SQ SEQUENCE 118 AA; 13677 MW; 140854676D3332E6 CRC64;
MARFVALVLL GLLSLSGLDA IQRPPKIQVY SRHPPEDGKP NYLNCYVYGF HPPQIEIDLL
KNGEKIKSEQ SDLSFSKDWS FYLLSHAEFT PNSKDQYSCR VKHVTLEQPR IVKWDRDL
