HA13_MOUSE
ID HA13_MOUSE Reviewed; 362 AA.
AC P14426;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=H-2 class I histocompatibility antigen, D-K alpha chain;
DE Short=H-2D(K);
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].
RC STRAIN=C3H/HeJ;
RX PubMed=3680952;
RA Watts S., Vogel J.M., Harriman W.D., Itoh T., Stauss H.J., Goodenow R.S.;
RT "DNA sequence analysis of the C3H H-2Kk and H-2Dk loci. Evolutionary
RT relationships to H-2 genes from four other mouse strains.";
RL J. Immunol. 139:3878-3885(1987).
RN [2]
RP UBIQUITINATION.
RX PubMed=11672544; DOI=10.1016/s1074-7613(01)00213-8;
RA Boname J.M., Stevenson P.G.;
RT "MHC class I ubiquitination by a viral PHD/LAP finger protein.";
RL Immunity 15:627-636(2001).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110 AND ASN-200.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(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 -!- PTM: Polyubiquitinated in case of infection by murid herpesvirus 4, by
CC the viral E3 ligase K3 (mK3), leading to target the protein for rapid
CC degradation by the endoplasmic reticulum-associated degradation (ERAD)
CC system. Ubiquitination takes place on lysine, as well as serine and
CC threonine residues present in the cytoplasmic tail. Hydroxylated serine
CC and threonine residues in the cytoplasmic tail are subject to
CC ubiquitination via ester bonds instead of the classical isopeptide
CC linkage (Probable). {ECO:0000305|PubMed:11672544}.
CC -!- PTM: Hydroxylation of residues in the cytoplasmic tail. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
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DR EMBL; M18524; AAA53201.1; -; Genomic_DNA.
DR PIR; I71998; I71998.
DR AlphaFoldDB; P14426; -.
DR SMR; P14426; -.
DR GlyConnect; 2365; 1 N-Linked glycan (1 site).
DR iPTMnet; P14426; -.
DR PhosphoSitePlus; P14426; -.
DR SwissPalm; P14426; -.
DR EPD; P14426; -.
DR jPOST; P14426; -.
DR MaxQB; P14426; -.
DR PeptideAtlas; P14426; -.
DR PRIDE; P14426; -.
DR ProteomicsDB; 269672; -.
DR MGI; MGI:95896; H2-D1.
DR ChiTaRS; H2-D1; mouse.
DR Proteomes; UP000000589; Unplaced.
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; Hydroxylation; Immunity; Membrane; MHC I;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..362
FT /note="H-2 class I histocompatibility antigen, D-K alpha
FT chain"
FT /id="PRO_0000018925"
FT TOPO_DOM 25..306
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 209..297
FT /note="Ig-like C1-type"
FT REGION 25..114
FT /note="Alpha-1"
FT REGION 115..206
FT /note="Alpha-2"
FT REGION 207..298
FT /note="Alpha-3"
FT REGION 299..306
FT /note="Connecting peptide"
FT REGION 340..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01900"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01900"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 125..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 227..283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 362 AA; 40620 MW; FF071720457D084D CRC64;
MGAMVPRTLL LLLAAALAPA QTRAGPHSLR YFETVVSRPG LGEPRFISVG YVDNTEFVRF
DSDAENPRDE PRVRWMEQEG PEYWERETQI AKGNEQSFRV DLRTLLRYYN QSEGGSHTIQ
RLSGCDVGSD WRLLRGYEQF AYDGCDYIAL NEDLKTWTAA DMAALITKHK WEQAGAAERD
RAYLEGTCVE WLRRYLELGN ATLLHTDSPK AHVTHHPRSK VEVTLRCWAL GFYPADITLT
WQLNGEELTQ DMELVETRPA GDGTFQKWAS VVVPLGKEQN YTCHVYHEGL PEPLTLRWEP
PPSTDSYMVI VAVLGVLGAV AIIGAVVAFV MMMRRNTGGK GGDYTLTPGS QSSEMSLPDC
KA
