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H-2 class I histocompatibility antigen, D-37 alpha chain

 HA15_MOUSE              Reviewed;         357 AA.
P06339;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
23-MAY-2018, entry version 159.
RecName: Full=H-2 class I histocompatibility antigen, D-37 alpha chain;
Flags: Precursor;
Name=H2-T23;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=DBA/2J;
PubMed=3838699; DOI=10.1016/S0092-8674(85)80020-9;
Lalanne J.-L., Transy C., Guerin S., Darche S., Meulien P.,
Kourilsky P.;
"Expression of class I genes in the major histocompatibility complex:
identification of eight distinct mRNAs in DBA/2 mouse liver.";
Cell 41:469-478(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BALB/cJ; TISSUE=Sperm;
PubMed=3036997; DOI=10.1084/jem.166.2.341;
Transy C., Nash S.R., David-Watine B., Cochet M., Hunt S.W. III,
Hood L.E., Kourilsky P.;
"A low polymorphic mouse H-2 class I gene from the Tla complex is
expressed in a broad variety of cell types.";
J. Exp. Med. 166:341-361(1987).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
-!- FUNCTION: Involved in the presentation of foreign antigens to the
immune system.
-!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-
microglobulin).
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M11284; AAA39693.1; -; mRNA.
EMBL; Y00629; CAA68665.1; -; Genomic_DNA.
CCDS; CCDS28715.1; -.
PIR; A02205; HLMS37.
RefSeq; NP_034528.1; NM_010398.3.
UniGene; Mm.439648; -.
UniGene; Mm.441651; -.
PDB; 3VJ6; X-ray; 1.90 A; A=21-297.
PDBsum; 3VJ6; -.
ProteinModelPortal; P06339; -.
SMR; P06339; -.
STRING; 10090.ENSMUSP00000099739; -.
iPTMnet; P06339; -.
PhosphoSitePlus; P06339; -.
EPD; P06339; -.
PaxDb; P06339; -.
PRIDE; P06339; -.
Ensembl; ENSMUST00000102678; ENSMUSP00000099739; ENSMUSG00000067212.
GeneID; 15040; -.
KEGG; mmu:15040; -.
UCSC; uc008cjr.1; mouse.
CTD; 15040; -.
MGI; MGI:95957; H2-T23.
eggNOG; ENOG410II5V; Eukaryota.
eggNOG; ENOG4111K8F; LUCA.
GeneTree; ENSGT00760000118960; -.
HOGENOM; HOG000296917; -.
HOVERGEN; HBG016709; -.
InParanoid; P06339; -.
KO; K06751; -.
OMA; GYCQEAY; -.
OrthoDB; EOG091G09OH; -.
PhylomeDB; P06339; -.
TreeFam; TF336617; -.
Reactome; R-MMU-1236974; ER-Phagosome pathway.
Reactome; R-MMU-1236977; Endosomal/Vacuolar pathway.
Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
PRO; PR:P06339; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000067212; -.
CleanEx; MM_H2-T23; -.
ExpressionAtlas; P06339; baseline and differential.
Genevisible; P06339; MM.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0042612; C:MHC class I protein complex; ISO:MGI.
GO; GO:0032398; C:MHC class Ib protein complex; ISO:MGI.
GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0030881; F:beta-2-microglobulin binding; ISO:MGI.
GO; GO:0042288; F:MHC class I protein binding; ISO:MGI.
GO; GO:0046703; F:natural killer cell lectin-like receptor binding; ISO:MGI.
GO; GO:0042605; F:peptide antigen binding; ISO:MGI.
GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
GO; GO:0042608; F:T cell receptor binding; ISO:MGI.
GO; GO:0002250; P:adaptive immune response; ISO:MGI.
GO; GO:0019731; P:antibacterial humoral response; ISO:MGI.
GO; GO:0002476; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib; ISO:MGI.
GO; GO:0002489; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib via ER pathway, TAP-dependent; IDA:MGI.
GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; IBA:GO_Central.
GO; GO:0036037; P:CD8-positive, alpha-beta T cell activation; ISO:MGI.
GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:MGI.
GO; GO:0048839; P:inner ear development; IDA:MGI.
GO; GO:2000566; P:positive regulation of CD8-positive, alpha-beta T cell proliferation; ISO:MGI.
GO; GO:0051024; P:positive regulation of immunoglobulin secretion; ISO:MGI.
GO; GO:0032736; P:positive regulation of interleukin-13 production; ISO:MGI.
GO; GO:0032753; P:positive regulation of interleukin-4 production; ISO:MGI.
GO; GO:0002717; P:positive regulation of natural killer cell mediated immunity; ISO:MGI.
GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IDA:MGI.
GO; GO:0032759; P:positive regulation of TRAIL production; ISO:MGI.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
GO; GO:0042270; P:protection from natural killer cell mediated cytotoxicity; ISO:MGI.
GO; GO:0002715; P:regulation of natural killer cell mediated immunity; ISO:MGI.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.30.500.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003006; Ig/MHC_CS.
InterPro; IPR003597; Ig_C1-set.
InterPro; IPR011161; MHC_I-like_Ag-recog.
InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
InterPro; IPR011162; MHC_I/II-like_Ag-recog.
InterPro; IPR001039; MHC_I_a_a1/a2.
Pfam; PF07654; C1-set; 1.
Pfam; PF00129; MHC_I; 1.
PRINTS; PR01638; MHCCLASSI.
SMART; SM00407; IGc1; 1.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF54452; SSF54452; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00290; IG_MHC; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond; Glycoprotein;
Immunity; Membrane; MHC I; Phosphoprotein; Reference proteome; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 357 H-2 class I histocompatibility antigen,
D-37 alpha chain.
/FTId=PRO_0000018927.
TOPO_DOM 21 304 Extracellular. {ECO:0000255}.
TRANSMEM 305 327 Helical. {ECO:0000255}.
TOPO_DOM 328 357 Cytoplasmic. {ECO:0000255}.
DOMAIN 205 293 Ig-like C1-type.
REGION 21 110 Alpha-1.
REGION 111 202 Alpha-2.
REGION 203 294 Alpha-3.
REGION 295 304 Connecting peptide.
MOD_RES 347 347 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
CARBOHYD 106 106 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 196 196 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 121 184 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 223 279 {ECO:0000255|PROSITE-ProRule:PRU00114}.
STRAND 23 32 {ECO:0000244|PDB:3VJ6}.
STRAND 41 48 {ECO:0000244|PDB:3VJ6}.
STRAND 51 57 {ECO:0000244|PDB:3VJ6}.
STRAND 60 62 {ECO:0000244|PDB:3VJ6}.
STRAND 66 69 {ECO:0000244|PDB:3VJ6}.
HELIX 70 74 {ECO:0000244|PDB:3VJ6}.
HELIX 77 105 {ECO:0000244|PDB:3VJ6}.
STRAND 114 123 {ECO:0000244|PDB:3VJ6}.
STRAND 129 138 {ECO:0000244|PDB:3VJ6}.
STRAND 141 146 {ECO:0000244|PDB:3VJ6}.
STRAND 153 155 {ECO:0000244|PDB:3VJ6}.
HELIX 158 169 {ECO:0000244|PDB:3VJ6}.
HELIX 172 181 {ECO:0000244|PDB:3VJ6}.
HELIX 183 194 {ECO:0000244|PDB:3VJ6}.
HELIX 196 199 {ECO:0000244|PDB:3VJ6}.
STRAND 206 215 {ECO:0000244|PDB:3VJ6}.
STRAND 218 231 {ECO:0000244|PDB:3VJ6}.
STRAND 234 239 {ECO:0000244|PDB:3VJ6}.
STRAND 257 259 {ECO:0000244|PDB:3VJ6}.
STRAND 261 270 {ECO:0000244|PDB:3VJ6}.
HELIX 274 276 {ECO:0000244|PDB:3VJ6}.
STRAND 277 282 {ECO:0000244|PDB:3VJ6}.
STRAND 290 292 {ECO:0000244|PDB:3VJ6}.
SEQUENCE 357 AA; 40875 MW; 62139862B099D411 CRC64;
MLLFAHLLQL LVSATVPTQS SPHSLRYFTT AVSRPGLGEP RFIIVGYVDD TQFVRFDSDA
ENPRMEPRAR WIEQEGPEYW ERETWKARDM GRNFRVNLRT LLGYYNQSND ESHTLQWMYG
CDVGPDGRLL RGYCQEAYDG QDYISLNEDL RSWTANDIAS QISKHKSEAV DEAHQQRAYL
QGPCVEWLHR YLRLGNETLQ RSDPPKAHVT HHPRSEDEVT LRCWALGFYP ADITLTWQLN
GEELTQDMEL VETRPAGDGT FQKWAAVVVP LGKEQYYTCH VYHEGLPEPL TLRWEPPPST
VSNMVIIAVL VVLGAVIILG AVVAFVMKRR RHIGVKGCYA HVLGSKSFQT SDWPQKA


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