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   24-JAN-2024, entry version 177.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   PDB; 7RNO; NMR; -; B=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   PDBsum; 7RNO; -.
DR   AlphaFoldDB; P01888; -.
DR   SMR; P01888; -.
DR   STRING; 9913.ENSBTAP00000016359; -.
DR   CarbonylDB; P01888; -.
DR   PaxDb; 9913-ENSBTAP00000016359; -.
DR   PeptideAtlas; P01888; -.
DR   Ensembl; ENSBTAT00000016359.3; ENSBTAP00000016359.2; ENSBTAG00000012330.6.
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; CRVAHST; -.
DR   OrthoDB; 4629494at2759; -.
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 cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031902; C:late endosome membrane; IBA:GO_Central.
DR   GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
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:0042605; F:peptide antigen 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:0050778; P:positive regulation of immune response; IBA:GO_Central.
DR   GO; GO:0050870; P:positive regulation of T cell activation; IBA:GO_Central.
DR   CDD; cd05770; IgC1_beta2m; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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; BETA-2-MICROGLOBULIN; 1.
DR   PANTHER; PTHR19944; MHC CLASS II-RELATED; 1.
DR   Pfam; PF07654; C1-set; 1.
DR   SMART; SM00407; IGc1; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 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          106..108
FT                   /evidence="ECO:0007829|PDB:7RNO"
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
//