HA15_MOUSE
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 03-AUG-2022, entry version 181.
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; 1.
DR IntAct; P06339; 1.
DR STRING; 10090.ENSMUSP00000099739; -.
DR GlyGen; P06339; 2 sites.
DR iPTMnet; P06339; -.
DR PhosphoSitePlus; P06339; -.
DR EPD; P06339; -.
DR jPOST; P06339; -.
DR PaxDb; P06339; -.
DR PRIDE; P06339; -.
DR ProteomicsDB; 269673; -.
DR DNASU; 15040; -.
DR Ensembl; ENSMUST00000102678; ENSMUSP00000099739; ENSMUSG00000067212.
DR GeneID; 15040; -.
DR KEGG; mmu:15040; -.
DR UCSC; uc008cjr.1; mouse.
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; KNERWIA; -.
DR OrthoDB; 1390181at2759; -.
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-2424491; DAP12 signaling.
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; 6 hits in 74 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 60 other tissues.
DR ExpressionAtlas; P06339; baseline and differential.
DR Genevisible; P06339; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0033106; C:cis-Golgi network membrane; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; 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:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
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:0071889; F:14-3-3 protein binding; ISO:MGI.
DR GO; GO:0030881; F:beta-2-microglobulin binding; ISO:MGI.
DR GO; GO:0042610; F:CD8 receptor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein 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:0042803; F:protein homodimerization activity; 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:0046978; F:TAP1 binding; ISO:MGI.
DR GO; GO:0046979; F:TAP2 binding; ISO:MGI.
DR GO; GO:0002476; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib; IBA:GO_Central.
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:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; IEA:UniProtKB-KW.
DR GO; GO:0048839; P:inner ear development; IDA:MGI.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IDA:MGI.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; IDA:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.500.10; -; 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 Pfam; PF07654; C1-set; 1.
DR Pfam; PF00129; MHC_I; 1.
DR PRINTS; PR01638; MHCCLASSI.
DR SMART; SM00407; IGc1; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF54452; SSF54452; 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
