ID HA15_MOUSE Reviewed; 357 AA.
AC P06339;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 27-MAR-2024, entry version 190.
DE RecName: Full=H-2 class I histocompatibility antigen, D-37 alpha chain;
DE Flags: Precursor;
GN Name=H2-T23;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=DBA/2J;
RX PubMed=3838699; DOI=10.1016/s0092-8674(85)80020-9;
RA Lalanne J.-L., Transy C., Guerin S., Darche S., Meulien P., Kourilsky P.;
RT "Expression of class I genes in the major histocompatibility complex:
RT identification of eight distinct mRNAs in DBA/2 mouse liver.";
RL Cell 41:469-478(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Sperm;
RX PubMed=3036997; DOI=10.1084/jem.166.2.341;
RA Transy C., Nash S.R., David-Watine B., Cochet M., Hunt S.W. III, Hood L.E.,
RA Kourilsky P.;
RT "A low polymorphic mouse H-2 class I gene from the Tla complex is expressed
RT in a broad variety of cell types.";
RL J. Exp. Med. 166:341-361(1987).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
CC -!- FUNCTION: Involved in the presentation of foreign antigens to the
CC immune system.
CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2-
CC microglobulin).
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
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DR EMBL; M11284; AAA39693.1; -; mRNA.
DR EMBL; Y00629; CAA68665.1; -; Genomic_DNA.
DR CCDS; CCDS28715.1; -.
DR PIR; A02205; HLMS37.
DR RefSeq; NP_034528.1; NM_010398.3.
DR PDB; 3VJ6; X-ray; 1.90 A; A=21-297.
DR PDBsum; 3VJ6; -.
DR AlphaFoldDB; P06339; -.
DR SMR; P06339; -.
DR BioGRID; 200189; 2.
DR IntAct; P06339; 1.
DR STRING; 10090.ENSMUSP00000099739; -.
DR GlyCosmos; P06339; 2 sites, No reported glycans.
DR GlyGen; P06339; 2 sites.
DR iPTMnet; P06339; -.
DR PhosphoSitePlus; P06339; -.
DR EPD; P06339; -.
DR jPOST; P06339; -.
DR PaxDb; 10090-ENSMUSP00000099739; -.
DR ProteomicsDB; 269673; -.
DR DNASU; 15040; -.
DR Ensembl; ENSMUST00000102678.5; ENSMUSP00000099739.5; ENSMUSG00000067212.9.
DR GeneID; 15040; -.
DR KEGG; mmu:15040; -.
DR UCSC; uc008cjr.1; mouse.
DR AGR; MGI:95957; -.
DR CTD; 15040; -.
DR MGI; MGI:95957; H2-T23.
DR VEuPathDB; HostDB:ENSMUSG00000067212; -.
DR eggNOG; ENOG502RQEK; Eukaryota.
DR GeneTree; ENSGT00980000198488; -.
DR HOGENOM; CLU_047501_1_1_1; -.
DR InParanoid; P06339; -.
DR OMA; WEEETRV; -.
DR OrthoDB; 3840485at2759; -.
DR PhylomeDB; P06339; -.
DR TreeFam; TF336617; -.
DR Reactome; R-MMU-1236974; ER-Phagosome pathway.
DR Reactome; R-MMU-1236977; Endosomal/Vacuolar pathway.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-2172127; DAP12 interactions.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR BioGRID-ORCS; 15040; 8 hits in 80 CRISPR screens.
DR ChiTaRS; H2-T23; mouse.
DR PRO; PR:P06339; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P06339; Protein.
DR Bgee; ENSMUSG00000067212; Expressed in granulocyte and 63 other cell types or tissues.
DR ExpressionAtlas; P06339; baseline and differential.
DR Genevisible; P06339; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0098553; C:lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0042612; C:MHC class I protein complex; ISO:MGI.
DR GO; GO:0032398; C:MHC class Ib protein complex; ISO:MGI.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030881; F:beta-2-microglobulin binding; ISO:MGI.
DR GO; GO:0042288; F:MHC class I protein binding; ISO:MGI.
DR GO; GO:0046703; F:natural killer cell lectin-like receptor binding; ISO:MGI.
DR GO; GO:0042605; F:peptide antigen binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0042608; F:T cell receptor binding; ISO:MGI.
DR GO; GO:0002250; P:adaptive immune response; ISO:MGI.
DR GO; GO:0019731; P:antibacterial humoral response; ISO:MGI.
DR GO; GO:0002486; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent; IBA:GO_Central.
DR GO; GO:0002476; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib; ISO:MGI.
DR GO; GO:0002489; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib via ER pathway, TAP-dependent; IDA:MGI.
DR GO; GO:0002477; P:antigen processing and presentation of exogenous peptide antigen via MHC class Ib; ISO:MGI.
DR GO; GO:0036037; P:CD8-positive, alpha-beta T cell activation; ISO:MGI.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISO:MGI.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0048839; P:inner ear development; IDA:MGI.
DR GO; GO:0002519; P:natural killer cell tolerance induction; ISO:MGI.
DR GO; GO:0032815; P:negative regulation of natural killer cell activation; ISO:MGI.
DR GO; GO:0045953; P:negative regulation of natural killer cell mediated cytotoxicity; ISO:MGI.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:MGI.
DR GO; GO:0001815; P:positive regulation of antibody-dependent cellular cytotoxicity; ISO:MGI.
DR GO; GO:2001187; P:positive regulation of CD8-positive, alpha-beta T cell activation; ISO:MGI.
DR GO; GO:2000566; P:positive regulation of CD8-positive, alpha-beta T cell proliferation; ISO:MGI.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; ISO:MGI.
DR GO; GO:0032736; P:positive regulation of interleukin-13 production; ISO:MGI.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; ISO:MGI.
DR GO; GO:0032816; P:positive regulation of natural killer cell activation; ISO:MGI.
DR GO; GO:0002729; P:positive regulation of natural killer cell cytokine production; ISO:MGI.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISO:MGI.
DR GO; GO:0002717; P:positive regulation of natural killer cell mediated immunity; ISO:MGI.
DR GO; GO:0032819; P:positive regulation of natural killer cell proliferation; ISO:MGI.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IDA:MGI.
DR GO; GO:0032759; P:positive regulation of TRAIL production; ISO:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:0042270; P:protection from natural killer cell mediated cytotoxicity; ISO:MGI.
DR GO; GO:0002715; P:regulation of natural killer cell mediated immunity; ISO:MGI.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; IDA:MGI.
DR CDD; cd21820; IgC1_MHC_1b_Qa-1b; 1.
DR CDD; cd12087; TM_EGFR-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.30.500.10; MHC class I-like antigen recognition-like; 1.
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 InterPro; IPR011161; MHC_I-like_Ag-recog.
DR InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
DR InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR InterPro; IPR001039; MHC_I_a_a1/a2.
DR PANTHER; PTHR16675:SF244; H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, D-37 ALPHA CHAIN; 1.
DR PANTHER; PTHR16675; MHC CLASS I-RELATED; 1.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF00129; MHC_I; 1.
DR PRINTS; PR01638; MHCCLASSI.
DR SMART; SM00407; IGc1; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF54452; MHC antigen-recognition domain; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Immunity; Membrane; MHC I;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..357
FT /note="H-2 class I histocompatibility antigen, D-37 alpha
FT chain"
FT /id="PRO_0000018927"
FT TOPO_DOM 21..304
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 205..293
FT /note="Ig-like C1-type"
FT REGION 21..110
FT /note="Alpha-1"
FT REGION 111..202
FT /note="Alpha-2"
FT REGION 203..294
FT /note="Alpha-3"
FT REGION 295..304
FT /note="Connecting peptide"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 121..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 223..279
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT STRAND 23..32
FT /evidence="ECO:0007829|PDB:3VJ6"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:3VJ6"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:3VJ6"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:3VJ6"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:3VJ6"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:3VJ6"
FT HELIX 77..105
FT /evidence="ECO:0007829|PDB:3VJ6"
FT STRAND 114..123
FT /evidence="ECO:0007829|PDB:3VJ6"
FT STRAND 129..138
FT /evidence="ECO:0007829|PDB:3VJ6"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:3VJ6"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3VJ6"
FT HELIX 158..169
FT /evidence="ECO:0007829|PDB:3VJ6"
FT HELIX 172..181
FT /evidence="ECO:0007829|PDB:3VJ6"
FT HELIX 183..194
FT /evidence="ECO:0007829|PDB:3VJ6"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:3VJ6"
FT STRAND 206..215
FT /evidence="ECO:0007829|PDB:3VJ6"
FT STRAND 218..231
FT /evidence="ECO:0007829|PDB:3VJ6"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:3VJ6"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:3VJ6"
FT STRAND 261..270
FT /evidence="ECO:0007829|PDB:3VJ6"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:3VJ6"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:3VJ6"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:3VJ6"
SQ 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
//
