B2MG_CHICK
ID B2MG_CHICK Reviewed; 119 AA.
AC P21611; Q5W922;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Beta-2-microglobulin;
DE Flags: Precursor;
GN Name=B2M;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1538136;
RA Kaufman J., Andersen R., Avila D., Engberg J., Lambris J., Salomonsen J.,
RA Welinder K., Skjoedt K.;
RT "Different features of the MHC class I heterodimer have evolved at
RT different rates. Chicken B-F and beta 2-microglobulin sequences reveal
RT invariant surface residues.";
RL J. Immunol. 148:1532-1546(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=8577748; DOI=10.1073/pnas.93.3.1243;
RA Riegert P., Andersen R., Bumstead N., Doehring C., Dominguez-Steglich M.,
RA Engberg J., Salomonsen J., Schmid M., Schwager J., Skjoedt K., Kaufman J.;
RT "The chicken beta 2-microglobulin gene is located on a non-major
RT histocompatibility complex microchromosome: a small, G+C-rich gene with X
RT and Y boxes in the promoter.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:1243-1248(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yan R.Q., Xia C.;
RT "Molecular characteristics of MHC class I and beta-2-microglobulin
RT sequences in a chicken line.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu G., Tong T., Xiao Y., Wu D.;
RT "Assessment of AIV specific CTL by chicken MHC-peptide tetramer.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 22-119, AND DISULFIDE BOND.
RX PubMed=2011126; DOI=10.1016/0161-5890(91)90102-p;
RA Welinder K.G., Jespersen H.M., Walther-Rasmussen J., Skjoedt K.;
RT "Amino acid sequences and structures of chicken and turkey beta 2-
RT microglobulin.";
RL Mol. Immunol. 28:177-182(1991).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 22-119.
RX PubMed=18083574; DOI=10.1016/j.immuni.2007.11.007;
RA Koch M., Camp S., Collen T., Avila D., Salomonsen J., Wallny H.-J.,
RA van Hateren A., Hunt L., Jacob J.P., Johnston F., Marston D.A., Shaw I.,
RA Dunbar P.R., Cerundolo V., Jones E.Y., Kaufman J.;
RT "Structures of an MHC class I molecule from B21 chickens illustrate
RT promiscuous peptide binding.";
RL Immunity 27:885-899(2007).
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.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the beta-2-microglobulin family. {ECO:0000305}.
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DR EMBL; M84767; AAA64915.1; -; mRNA.
DR EMBL; Z48921; CAA88757.1; -; mRNA.
DR EMBL; Z48922; CAA88758.1; -; Genomic_DNA.
DR EMBL; Z48931; CAA88777.1; -; Genomic_DNA.
DR EMBL; AB178590; BAD69547.1; -; mRNA.
DR EMBL; AB178591; BAD69548.1; -; mRNA.
DR EMBL; AB178595; BAD69552.1; -; mRNA.
DR EMBL; AY989898; AAX94677.1; -; mRNA.
DR PIR; S52743; A46492.
DR RefSeq; NP_001001750.1; NM_001001750.1.
DR RefSeq; XP_015134563.1; XM_015279077.1.
DR PDB; 2YEZ; X-ray; 2.90 A; B=22-119.
DR PDB; 3BEV; X-ray; 2.10 A; B=22-119.
DR PDB; 3BEW; X-ray; 2.60 A; B/E=22-119.
DR PDB; 3JVG; X-ray; 2.20 A; C/D=22-119.
DR PDB; 3O81; X-ray; 2.00 A; A/B=1-119.
DR PDB; 3P73; X-ray; 1.32 A; B=21-119.
DR PDB; 3P77; X-ray; 1.60 A; B=21-119.
DR PDB; 4CVX; X-ray; 3.30 A; B/E=22-119.
DR PDB; 4CVZ; X-ray; 2.39 A; B=22-119.
DR PDB; 4CW1; X-ray; 2.58 A; B/E=22-119.
DR PDB; 4D0B; X-ray; 2.80 A; B=22-119.
DR PDB; 4D0C; X-ray; 2.81 A; B=22-119.
DR PDB; 4D0D; X-ray; 3.13 A; B/E/H/K=22-119.
DR PDB; 4E0R; X-ray; 2.26 A; B/E=22-119.
DR PDB; 4G42; X-ray; 2.29 A; B/E=22-119.
DR PDB; 4G43; X-ray; 1.80 A; B/E=22-119.
DR PDB; 5ACZ; X-ray; 2.69 A; B=22-119.
DR PDB; 5AD0; X-ray; 2.84 A; B=22-119.
DR PDB; 5YMV; X-ray; 2.20 A; B/E=22-119.
DR PDB; 5YMW; X-ray; 2.00 A; B/E/H/K=22-119.
DR PDB; 6IRL; X-ray; 2.10 A; B=22-119.
DR PDB; 6KX9; X-ray; 2.90 A; B=22-119.
DR PDB; 6LHF; X-ray; 2.70 A; B/E=23-118.
DR PDB; 6LHG; X-ray; 2.80 A; B/E=22-118.
DR PDB; 6LHH; X-ray; 2.71 A; B=22-119.
DR PDBsum; 2YEZ; -.
DR PDBsum; 3BEV; -.
DR PDBsum; 3BEW; -.
DR PDBsum; 3JVG; -.
DR PDBsum; 3O81; -.
DR PDBsum; 3P73; -.
DR PDBsum; 3P77; -.
DR PDBsum; 4CVX; -.
DR PDBsum; 4CVZ; -.
DR PDBsum; 4CW1; -.
DR PDBsum; 4D0B; -.
DR PDBsum; 4D0C; -.
DR PDBsum; 4D0D; -.
DR PDBsum; 4E0R; -.
DR PDBsum; 4G42; -.
DR PDBsum; 4G43; -.
DR PDBsum; 5ACZ; -.
DR PDBsum; 5AD0; -.
DR PDBsum; 5YMV; -.
DR PDBsum; 5YMW; -.
DR PDBsum; 6IRL; -.
DR PDBsum; 6KX9; -.
DR PDBsum; 6LHF; -.
DR PDBsum; 6LHG; -.
DR PDBsum; 6LHH; -.
DR AlphaFoldDB; P21611; -.
DR SMR; P21611; -.
DR STRING; 9031.ENSGALP00000039454; -.
DR PaxDb; P21611; -.
DR Ensembl; ENSGALT00000040255; ENSGALP00000039454; ENSGALG00000002160.
DR GeneID; 414830; -.
DR KEGG; gga:414830; -.
DR CTD; 567; -.
DR VEuPathDB; HostDB:geneid_414830; -.
DR eggNOG; ENOG502S8GM; Eukaryota.
DR GeneTree; ENSGT00690000102227; -.
DR HOGENOM; CLU_163066_0_0_1; -.
DR InParanoid; P21611; -.
DR OMA; FHPPKID; -.
DR OrthoDB; 1556447at2759; -.
DR PhylomeDB; P21611; -.
DR TreeFam; TF334167; -.
DR Reactome; R-GGA-1236974; ER-Phagosome pathway.
DR Reactome; R-GGA-1236977; Endosomal/Vacuolar pathway.
DR Reactome; R-GGA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-GGA-2424491; DAP12 signaling.
DR Reactome; R-GGA-6798695; Neutrophil degranulation.
DR Reactome; R-GGA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR EvolutionaryTrace; P21611; -.
DR PRO; PR:P21611; -.
DR Proteomes; UP000000539; Chromosome 10.
DR Bgee; ENSGALG00000002160; Expressed in lung and 13 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..21
FT /evidence="ECO:0000269|PubMed:2011126"
FT CHAIN 22..119
FT /note="Beta-2-microglobulin"
FT /evidence="ECO:0000269|PubMed:2011126"
FT /id="PRO_0000018804"
FT DOMAIN 25..113
FT /note="Ig-like C1-type"
FT DISULFID 45..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:2011126"
FT VARIANT 96
FT /note="S -> G"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:3P73"
FT STRAND 41..53
FT /evidence="ECO:0007829|PDB:3P73"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:3P73"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:4E0R"
FT STRAND 82..90
FT /evidence="ECO:0007829|PDB:3P73"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:3P73"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:4G43"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:3P73"
SQ SEQUENCE 119 AA; 13042 MW; DFC07B5011FD0ABD CRC64;
MGKAAAVVLV TLVALLGLAQ ADLTPKVQVY SRFPASAGTK NVLNCFAAGF HPPKISITLM
KDGVPMEGAQ YSDMSFNDDW TFQRLVHADF TPSSGSTYAC KVEHETLKEP QVYKWDPEF
