HA1K_MOUSE
ID HA1K_MOUSE Reviewed; 369 AA.
AC P04223; O19459; Q31165; Q31192; Q95458;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=H-2 class I histocompatibility antigen, K-K alpha chain;
DE Short=H-2K(K);
DE Flags: Precursor;
GN Name=H2-K1; Synonyms=H2-K;
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] (ISOFORM 1).
RX PubMed=6096831; DOI=10.1093/nar/12.24.9473;
RA Arnold B., Burgert H.-G., Archibald A.L., Kvist S.;
RT "Complete nucleotide sequence of the murine H-2Kk gene. Comparison of three
RT H-2K locus alleles.";
RL Nucleic Acids Res. 12:9473-9487(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C3H/HeJ; TISSUE=Splenocyte;
RX PubMed=9869916;
RA Wang M., Stepkowski S.M., Hebert J.S., Tian L., Yu J., Kahan B.D.;
RT "Nucleotide sequences of three H-2K and three H-2D complementary DNA clones
RT coding mouse class I MHC heavy chain proteins.";
RL Ann. Transplant. 1:26-31(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE OF 1-359.
RC STRAIN=C3H/HeN;
RX PubMed=3335396; DOI=10.1007/bf00351091;
RA Minamide L.S., Callahan G.N., Grosveld F.G., Hui K.M.;
RT "The nucleotide sequence of the H-2K gene of C3Hf/HeN mice.";
RL Immunogenetics 27:148-152(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-369 (ISOFORM 2).
RX PubMed=3840763; DOI=10.1016/0378-1119(85)90223-9;
RA Reddy E.S., Pan J.Y.;
RT "Molecular cloning and sequencing of H-2Kk cDNA: comparison with other H-2
RT genes and evidence for alternative splicing.";
RL Gene 38:239-244(1985).
RN [6]
RP NUCLEOTIDE SEQUENCE OF 22-313.
RX PubMed=3374494; DOI=10.1016/0161-5890(88)90018-1;
RA Martinko J.M., Solheim J.C., Geliebter J.;
RT "The H-2Kkml mutation: a single nucleotide substitution is responsible for
RT multiple functional differences in a class I MHC molecule.";
RL Mol. Immunol. 25:267-274(1988).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-107.
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).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-351 AND SER-354 (ISOFORM 2), AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen, and
RC Testis;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P04223-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P04223-2; Sequence=VSP_011855;
CC -!- SIMILARITY: Belongs to the MHC class I family. {ECO:0000305}.
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DR EMBL; X01652; CAA25816.1; -; Genomic_DNA.
DR EMBL; M18525; AAA53202.1; -; Genomic_DNA.
DR EMBL; U47330; AAB17608.1; -; mRNA.
DR EMBL; M18964; AAA39568.1; -; Genomic_DNA.
DR EMBL; M11975; AAA39654.1; -; mRNA.
DR EMBL; M34932; AAA39596.1; -; mRNA.
DR PIR; A02203; HLMSKK.
DR PDB; 1ZT1; X-ray; 2.50 A; A=22-297.
DR PDB; 1ZT7; X-ray; 3.00 A; A/C=22-296.
DR PDBsum; 1ZT1; -.
DR PDBsum; 1ZT7; -.
DR AlphaFoldDB; P04223; -.
DR SMR; P04223; -.
DR iPTMnet; P04223; -.
DR PhosphoSitePlus; P04223; -.
DR EPD; P04223; -.
DR jPOST; P04223; -.
DR MaxQB; P04223; -.
DR PeptideAtlas; P04223; -.
DR PRIDE; P04223; -.
DR ProteomicsDB; 270923; -. [P04223-1]
DR ProteomicsDB; 270924; -. [P04223-2]
DR MGI; MGI:95904; H2-K1.
DR ChiTaRS; H2-K1; mouse.
DR EvolutionaryTrace; P04223; -.
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; 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: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; IDA: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:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; IDA:MGI.
DR GO; GO:0042742; P:defense response to bacterium; IDA:MGI.
DR GO; GO:0048839; P:inner ear development; IDA:MGI.
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 3D-structure; Alternative splicing; Disulfide bond; Glycoprotein; Immunity;
KW Membrane; MHC I; Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT CHAIN 22..369
FT /note="H-2 class I histocompatibility antigen, K-K alpha
FT chain"
FT /id="PRO_0000018930"
FT TOPO_DOM 22..305
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..369
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..305
FT /note="Connecting peptide"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01900"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 197
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"
FT VAR_SEQ 360..369
FT /note="VMVHDPHSLA -> A (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:3840763,
FT ECO:0000303|PubMed:9869916"
FT /id="VSP_011855"
FT VARIANT 173
FT /note="D -> A"
FT CONFLICT 50
FT /note="D -> E (in Ref. 5; AAA39654)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="N -> S (in Ref. 2; AAA53202)"
FT /evidence="ECO:0000305"
FT STRAND 23..33
FT /evidence="ECO:0007829|PDB:1ZT1"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:1ZT1"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:1ZT1"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:1ZT1"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1ZT1"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1ZT7"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:1ZT1"
FT HELIX 78..105
FT /evidence="ECO:0007829|PDB:1ZT1"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1ZT1"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:1ZT1"
FT STRAND 128..139
FT /evidence="ECO:0007829|PDB:1ZT1"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:1ZT1"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:1ZT1"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:1ZT1"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:1ZT1"
FT HELIX 184..193
FT /evidence="ECO:0007829|PDB:1ZT1"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:1ZT7"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:1ZT1"
FT STRAND 216..232
FT /evidence="ECO:0007829|PDB:1ZT1"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:1ZT1"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:1ZT7"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1ZT1"
FT STRAND 262..271
FT /evidence="ECO:0007829|PDB:1ZT1"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:1ZT1"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:1ZT1"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:1ZT1"
FT MOD_RES P04223-2:351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES P04223-2:354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 369 AA; 41646 MW; 9533CF96600A595C CRC64;
MAPCMLLLLL AAALAPTQTR AGPHSLRYFH TAVSRPGLGK PRFISVGYVD DTQFVRFDSD
AENPRYEPRV RWMEQVEPEY WERNTQIAKG NEQIFRVNLR TALRYYNQSA GGSHTFQRMY
GCEVGSDWRL LRGYEQYAYD GCDYIALNED LKTWTAADMA ALITKHKWEQ AGDAERDRAY
LEGTCVEWLR RYLQLGNATL PRTDSPKAHV TRHSRPEDKV TLRCWALGFY PADITLTWQL
NGEELTQDME LVETRPAGDG TFQKWASVVV PLGKEQYYTC HVYHQGLPEP LTLRWEPPPS
TVSNTVIIAV LVVLGAAIVT GAVVAFVMKM RRRNTGGKGG DYALAPGSQT SDLSLPDCKV
MVHDPHSLA
