HA14_MOUSE
ID HA14_MOUSE Reviewed; 368 AA.
AC P14427;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=H-2 class I histocompatibility antigen, D-P alpha chain;
DE Short=H-2D(P);
DE Flags: Precursor;
GN Name=H2-D1;
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 [GENOMIC DNA].
RX PubMed=3082989;
RA Schepart B.S., Takahashi H., Cozad K.M., Murray R., Ozato K., Appella E.,
RA Frelinger J.A.;
RT "The nucleotide sequence and comparative analysis of the H-2Dp class I H-2
RT gene.";
RL J. Immunol. 136:3489-3495(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-111.
RX PubMed=2903482; DOI=10.1093/nar/16.20.9761;
RA Murray R., Pederson K., Prosser H., Muller D., Hutchison C.A. III,
RA Frelinger J.A.;
RT "Random oligonucleotide mutagenesis: application to a large protein coding
RT sequence of a major histocompatibility complex class I gene, H-2DP.";
RL Nucleic Acids Res. 16:9761-9773(1988).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
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; M12381; AAA39603.1; -; Genomic_DNA.
DR PIR; I55961; I55961.
DR AlphaFoldDB; P14427; -.
DR SMR; P14427; -.
DR GlyGen; P14427; 3 sites.
DR iPTMnet; P14427; -.
DR PhosphoSitePlus; P14427; -.
DR EPD; P14427; -.
DR jPOST; P14427; -.
DR MaxQB; P14427; -.
DR PeptideAtlas; P14427; -.
DR PRIDE; P14427; -.
DR ProteomicsDB; 269798; -.
DR MGI; MGI:95896; H2-D1.
DR InParanoid; P14427; -.
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 ChiTaRS; H2-D1; mouse.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P14427; protein.
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:0070971; C:endoplasmic reticulum exit site; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005797; C:Golgi medial cisterna; ISO:MGI.
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:0042824; C:MHC class I peptide loading complex; 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; IDA: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:0051087; F:chaperone 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:0046977; F:TAP binding; ISO:MGI.
DR GO; GO:0062061; F:TAP complex binding; ISO:MGI.
DR GO; GO:0046978; F:TAP1 binding; ISO:MGI.
DR GO; GO:0046979; F:TAP2 binding; ISO:MGI.
DR GO; GO:0002485; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent; IDA:MGI.
DR GO; GO:0002476; P:antigen processing and presentation of endogenous peptide antigen via MHC class Ib; IBA:GO_Central.
DR GO; GO:0010977; P:negative regulation of neuron projection 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 InterPro; IPR010579; MHC_I_a_C.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF00129; MHC_I; 1.
DR Pfam; PF06623; MHC_I_C; 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 Disulfide bond; Glycoprotein; Immunity; Membrane; MHC I; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..368
FT /note="H-2 class I histocompatibility antigen, D-P alpha
FT chain"
FT /id="PRO_0000018926"
FT TOPO_DOM 22..303
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..368
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 206..294
FT /note="Ig-like C1-type"
FT REGION 22..111
FT /note="Alpha-1"
FT REGION 112..203
FT /note="Alpha-2"
FT REGION 204..295
FT /note="Alpha-3"
FT REGION 296..303
FT /note="Connecting peptide"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01900"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01900"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 122..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 224..280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 368 AA; 41342 MW; EFD4FB8E14E6FAC0 CRC64;
MAPRTLLLLL AAALAPTQTR AGPHSLRYFV TAVSRPGLGK PRYMEVGYVD NTEFVRFDSD
AENPRMKPRV RWMEQEGPEY WEQETQNAKD HEQSFRVSLR NLLGYYNQSK GGSHTIQGMR
GCDVGSDWRL LRGYEQFAYD GPDYIALNED LKTWTAADMA AQITRRKWEQ AGAAETLRAY
LEGACVEWLR RYLELGNATL LCTDPPKAHV THHPRSEGKV TLRCWALGFY PADITLTWQL
NGEELTQDME LVETRPAGDG TFQKWAALVV PLGKEQNYTC HVEHEGLPEP LTLRWEPPPS
TDSYMVIVAV LVVLGAVFII GAVVAFVMMM RRNTGGKGGD YTLAPGSQSS EMSLRDCKVM
VHDSHSLA
