HA1B_MOUSE
ID HA1B_MOUSE Reviewed; 369 AA.
AC P01901;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=H-2 class I histocompatibility antigen, K-B alpha chain;
DE Short=H-2K(B);
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.
RX PubMed=11894963; DOI=10.1002/j.1460-2075.1983.tb01444.x;
RA Weiss E., Golden L., Zakut R., Mellor A., Fahrner K., Kvist S.,
RA Flavell R.A.;
RT "The DNA sequence of the H-2K(b) gene: evidence for gene conversion as a
RT mechanism for the generation of polymorphism in histocompatibility
RT antigens.";
RL EMBO J. 2:453-462(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/10;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 87-369.
RX PubMed=6954478; DOI=10.1073/pnas.79.10.3270;
RA Reyes A.A., Schold M., Itakura K., Wallace R.B.;
RT "Isolation of a cDNA clone for the murine transplantation antigen H-2Kb.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:3270-3274(1982).
RN [4]
RP PROTEIN SEQUENCE OF 22-367, AND GLYCOSYLATION AT ASN-107 AND ASN-197.
RX PubMed=7306483; DOI=10.1021/bi00524a003;
RA Uehara H., Coligan J.E., Nathenson S.G.;
RT "Amino acid sequence of the carboxyl-terminal hydrophilic region of the H-
RT 2Kb MHC alloantigen. Completion of the entire primary structure of the H-
RT 2Kb molecule.";
RL Biochemistry 20:5940-5945(1981).
RN [5]
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 [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-107.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and 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).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-295.
RX PubMed=1323877; DOI=10.1126/science.1323877;
RA Fremont D.H., Matsumura M., Stura E.A., Peterson P.A., Wilson I.A.;
RT "Crystal structures of two viral peptides in complex with murine MHC class
RT I H-2Kb.";
RL Science 257:919-927(1992).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-295 IN COMPLEX WITH CD8A.
RX PubMed=9806638; DOI=10.1016/s1074-7613(00)80635-4;
RA Kern P.S., Teng M.K., Smolyar A., Liu J.H., Liu J., Hussey R.E., Spoerl R.,
RA Chang H.-C., Reinherz E.L., Wang J.-H.;
RT "Structural basis of CD8 coreceptor function revealed by crystallographic
RT analysis of a murine CD8alphaalpha ectodomain fragment in complex with H-
RT 2Kb.";
RL Immunity 9:519-530(1998).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 22-295.
RX PubMed=10023770; DOI=10.1016/s1074-7613(00)80006-0;
RA Speir J.A., Abdel-Motal U.M., Jondal M., Wilson I.A.;
RT "Crystal structure of an MHC class I presented glycopeptide that generates
RT carbohydrate-specific CTL.";
RL Immunity 10:51-61(1999).
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). {ECO:0000269|PubMed:9806638}.
CC -!- INTERACTION:
CC P01901; P16879: Fes; NbExp=3; IntAct=EBI-1265227, EBI-771815;
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; J00400; AAA39648.1; -; mRNA.
DR EMBL; U47328; AAB17606.1; -; mRNA.
DR EMBL; V00746; CAA24119.2; -; Genomic_DNA.
DR EMBL; V00747; CAA24119.2; JOINED; Genomic_DNA.
DR CCDS; CCDS50069.1; -.
DR PIR; A90980; HLMSKB.
DR RefSeq; NP_001001892.2; NM_001001892.2.
DR PDB; 1BQH; X-ray; 2.80 A; A/D=22-295.
DR PDB; 1FO0; X-ray; 2.50 A; H=22-296.
DR PDB; 1FZJ; X-ray; 1.90 A; A=22-295.
DR PDB; 1FZK; X-ray; 1.70 A; A=22-295.
DR PDB; 1FZM; X-ray; 1.80 A; A=22-295.
DR PDB; 1FZO; X-ray; 1.80 A; A=22-295.
DR PDB; 1G6R; X-ray; 2.80 A; H/I=22-295.
DR PDB; 1G7P; X-ray; 1.50 A; A=22-295.
DR PDB; 1G7Q; X-ray; 1.60 A; A=22-295.
DR PDB; 1KBG; X-ray; 2.20 A; H=22-295.
DR PDB; 1KJ2; X-ray; 2.71 A; H/I=22-298.
DR PDB; 1KJ3; X-ray; 2.30 A; H/I=22-299.
DR PDB; 1KPU; X-ray; 1.50 A; A=22-295.
DR PDB; 1KPV; X-ray; 1.71 A; A=22-295.
DR PDB; 1LEG; X-ray; 1.75 A; A=22-295.
DR PDB; 1LEK; X-ray; 2.15 A; A=22-295.
DR PDB; 1LK2; X-ray; 1.35 A; A=22-295.
DR PDB; 1MWA; X-ray; 2.40 A; H/I=22-295.
DR PDB; 1N59; X-ray; 2.95 A; A/C=22-297.
DR PDB; 1NAM; X-ray; 2.70 A; H=22-296.
DR PDB; 1NAN; X-ray; 2.30 A; H/L=22-299.
DR PDB; 1OSZ; X-ray; 2.10 A; A=22-295.
DR PDB; 1P1Z; X-ray; 3.26 A; A=22-295.
DR PDB; 1P4L; X-ray; 2.90 A; A=22-295.
DR PDB; 1RJY; X-ray; 1.90 A; A/D=22-301.
DR PDB; 1RJZ; X-ray; 2.60 A; A/D=22-301.
DR PDB; 1RK0; X-ray; 2.61 A; A=22-295.
DR PDB; 1RK1; X-ray; 2.10 A; A=22-295.
DR PDB; 1S7Q; X-ray; 1.99 A; A=22-369.
DR PDB; 1S7R; X-ray; 2.95 A; A/D=22-369.
DR PDB; 1S7S; X-ray; 1.99 A; A=22-369.
DR PDB; 1S7T; X-ray; 2.30 A; A/D=22-369.
DR PDB; 1T0M; X-ray; 2.00 A; A/D=22-299.
DR PDB; 1T0N; X-ray; 1.80 A; A/D=22-299.
DR PDB; 1VAC; X-ray; 2.50 A; A=22-295.
DR PDB; 1VAD; X-ray; 2.50 A; A=22-295.
DR PDB; 1WBZ; X-ray; 2.00 A; A/C=22-296.
DR PDB; 2CKB; X-ray; 3.00 A; H/I=22-295.
DR PDB; 2CLV; X-ray; 1.90 A; A/H=22-300.
DR PDB; 2CLZ; X-ray; 1.90 A; A/H=22-300.
DR PDB; 2FO4; X-ray; 2.70 A; A=22-295.
DR PDB; 2MHA; X-ray; 2.50 A; A/C=22-291.
DR PDB; 2OL3; X-ray; 2.90 A; H=22-300.
DR PDB; 2QRI; X-ray; 2.00 A; A/B=22-301.
DR PDB; 2QRS; X-ray; 2.00 A; A/B=22-301.
DR PDB; 2QRT; X-ray; 1.80 A; A/B=22-301.
DR PDB; 2VAA; X-ray; 2.30 A; A=22-295.
DR PDB; 2VAB; X-ray; 2.50 A; A=22-295.
DR PDB; 2ZSV; X-ray; 1.80 A; A/C=22-299.
DR PDB; 2ZSW; X-ray; 2.80 A; A/C/E/G=22-299.
DR PDB; 3C8K; X-ray; 2.90 A; A=22-295.
DR PDB; 3CVH; X-ray; 2.90 A; A/M=22-295.
DR PDB; 3P4M; X-ray; 2.50 A; A/D=22-298.
DR PDB; 3P4N; X-ray; 2.50 A; A/D=22-298.
DR PDB; 3P4O; X-ray; 2.30 A; A/D=22-298.
DR PDB; 3P9L; X-ray; 2.00 A; A/D=22-299.
DR PDB; 3P9M; X-ray; 2.00 A; A/D=22-298.
DR PDB; 3PAB; X-ray; 2.20 A; A/D=22-299.
DR PDB; 3RGV; X-ray; 2.90 A; C=22-296.
DR PDB; 3ROL; X-ray; 2.60 A; A/C=22-296.
DR PDB; 3ROO; X-ray; 2.00 A; A/C=22-296.
DR PDB; 3TID; X-ray; 1.65 A; A=22-297.
DR PDB; 3TIE; X-ray; 2.25 A; A/D=22-297.
DR PDB; 4HKJ; X-ray; 3.00 A; A/E/I/M=22-301.
DR PDB; 4HS3; X-ray; 2.10 A; A=22-297.
DR PDB; 4PG9; X-ray; 2.40 A; A=22-299.
DR PDB; 4PGB; X-ray; 2.80 A; A/D=22-299.
DR PDB; 4PGC; X-ray; 2.30 A; A/D=22-299.
DR PDB; 4PGD; X-ray; 2.70 A; A=22-299.
DR PDB; 4PGE; X-ray; 2.00 A; A=22-299.
DR PDB; 4PV8; X-ray; 2.31 A; A/C=22-299.
DR PDB; 4PV9; X-ray; 2.00 A; A/C=22-299.
DR PDB; 5OQF; X-ray; 2.27 A; A/B=23-304.
DR PDB; 5OQG; X-ray; 1.90 A; A/B=22-304.
DR PDB; 5OQH; X-ray; 2.05 A; A/B=22-304.
DR PDB; 5OQI; X-ray; 2.40 A; A/B=22-304.
DR PDB; 6GB6; X-ray; 1.78 A; A/D=22-297.
DR PDB; 6JQ2; X-ray; 2.40 A; A=22-295.
DR PDB; 6JQ3; X-ray; 2.50 A; A=22-295.
DR PDB; 6WL2; X-ray; 3.30 A; A/D/G=22-206.
DR PDB; 6WL3; X-ray; 3.45 A; A/D/G=22-206.
DR PDB; 6WL4; X-ray; 3.60 A; A/D/G=22-206.
DR PDB; 7JI2; X-ray; 1.95 A; A/D=22-301.
DR PDBsum; 1BQH; -.
DR PDBsum; 1FO0; -.
DR PDBsum; 1FZJ; -.
DR PDBsum; 1FZK; -.
DR PDBsum; 1FZM; -.
DR PDBsum; 1FZO; -.
DR PDBsum; 1G6R; -.
DR PDBsum; 1G7P; -.
DR PDBsum; 1G7Q; -.
DR PDBsum; 1KBG; -.
DR PDBsum; 1KJ2; -.
DR PDBsum; 1KJ3; -.
DR PDBsum; 1KPU; -.
DR PDBsum; 1KPV; -.
DR PDBsum; 1LEG; -.
DR PDBsum; 1LEK; -.
DR PDBsum; 1LK2; -.
DR PDBsum; 1MWA; -.
DR PDBsum; 1N59; -.
DR PDBsum; 1NAM; -.
DR PDBsum; 1NAN; -.
DR PDBsum; 1OSZ; -.
DR PDBsum; 1P1Z; -.
DR PDBsum; 1P4L; -.
DR PDBsum; 1RJY; -.
DR PDBsum; 1RJZ; -.
DR PDBsum; 1RK0; -.
DR PDBsum; 1RK1; -.
DR PDBsum; 1S7Q; -.
DR PDBsum; 1S7R; -.
DR PDBsum; 1S7S; -.
DR PDBsum; 1S7T; -.
DR PDBsum; 1T0M; -.
DR PDBsum; 1T0N; -.
DR PDBsum; 1VAC; -.
DR PDBsum; 1VAD; -.
DR PDBsum; 1WBZ; -.
DR PDBsum; 2CKB; -.
DR PDBsum; 2CLV; -.
DR PDBsum; 2CLZ; -.
DR PDBsum; 2FO4; -.
DR PDBsum; 2MHA; -.
DR PDBsum; 2OL3; -.
DR PDBsum; 2QRI; -.
DR PDBsum; 2QRS; -.
DR PDBsum; 2QRT; -.
DR PDBsum; 2VAA; -.
DR PDBsum; 2VAB; -.
DR PDBsum; 2ZSV; -.
DR PDBsum; 2ZSW; -.
DR PDBsum; 3C8K; -.
DR PDBsum; 3CVH; -.
DR PDBsum; 3P4M; -.
DR PDBsum; 3P4N; -.
DR PDBsum; 3P4O; -.
DR PDBsum; 3P9L; -.
DR PDBsum; 3P9M; -.
DR PDBsum; 3PAB; -.
DR PDBsum; 3RGV; -.
DR PDBsum; 3ROL; -.
DR PDBsum; 3ROO; -.
DR PDBsum; 3TID; -.
DR PDBsum; 3TIE; -.
DR PDBsum; 4HKJ; -.
DR PDBsum; 4HS3; -.
DR PDBsum; 4PG9; -.
DR PDBsum; 4PGB; -.
DR PDBsum; 4PGC; -.
DR PDBsum; 4PGD; -.
DR PDBsum; 4PGE; -.
DR PDBsum; 4PV8; -.
DR PDBsum; 4PV9; -.
DR PDBsum; 5OQF; -.
DR PDBsum; 5OQG; -.
DR PDBsum; 5OQH; -.
DR PDBsum; 5OQI; -.
DR PDBsum; 6GB6; -.
DR PDBsum; 6JQ2; -.
DR PDBsum; 6JQ3; -.
DR PDBsum; 6WL2; -.
DR PDBsum; 6WL3; -.
DR PDBsum; 6WL4; -.
DR PDBsum; 7JI2; -.
DR AlphaFoldDB; P01901; -.
DR SMR; P01901; -.
DR BioGRID; 200155; 3.
DR DIP; DIP-6189N; -.
DR IntAct; P01901; 4.
DR MINT; P01901; -.
DR STRING; 10090.ENSMUSP00000025181; -.
DR GlyGen; P01901; 3 sites.
DR iPTMnet; P01901; -.
DR PhosphoSitePlus; P01901; -.
DR SwissPalm; P01901; -.
DR EPD; P01901; -.
DR jPOST; P01901; -.
DR PaxDb; P01901; -.
DR PeptideAtlas; P01901; -.
DR PRIDE; P01901; -.
DR ProteomicsDB; 269800; -.
DR ABCD; P01901; 1 sequenced antibody.
DR DNASU; 14972; -.
DR Ensembl; ENSMUST00000025181; ENSMUSP00000025181; ENSMUSG00000061232.
DR GeneID; 14972; -.
DR KEGG; mmu:14972; -.
DR UCSC; uc008cap.1; mouse.
DR CTD; 14972; -.
DR MGI; MGI:95904; H2-K1.
DR VEuPathDB; HostDB:ENSMUSG00000061232; -.
DR eggNOG; ENOG502RQEK; Eukaryota.
DR GeneTree; ENSGT00980000198488; -.
DR InParanoid; P01901; -.
DR OMA; NTENPEY; -.
DR OrthoDB; 1390181at2759; -.
DR PhylomeDB; P01901; -.
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; 14972; 12 hits in 64 CRISPR screens.
DR ChiTaRS; H2-K1; mouse.
DR EvolutionaryTrace; P01901; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P01901; protein.
DR Bgee; ENSMUSG00000061232; Expressed in thoracic mammary gland and 232 other tissues.
DR ExpressionAtlas; P01901; baseline and differential.
DR Genevisible; P01901; 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: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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunity; Membrane; MHC I; Phosphoprotein; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:7306483"
FT CHAIN 22..369
FT /note="H-2 class I histocompatibility antigen, K-B alpha
FT chain"
FT /id="PRO_0000018928"
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:19349973,
FT ECO:0000269|PubMed:7306483"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:7306483"
FT DISULFID 122..185
FT DISULFID 224..280
FT CONFLICT 217
FT /note="E -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="E -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="N -> A (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="D -> P (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:1LK2"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1LK2"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:1LK2"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:1LK2"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1LK2"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:3TID"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:1LK2"
FT HELIX 78..105
FT /evidence="ECO:0007829|PDB:1LK2"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1G7P"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:1LK2"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1G6R"
FT STRAND 130..139
FT /evidence="ECO:0007829|PDB:1LK2"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:1LK2"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:2MHA"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:1LK2"
FT HELIX 159..171
FT /evidence="ECO:0007829|PDB:1LK2"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:1LK2"
FT HELIX 184..195
FT /evidence="ECO:0007829|PDB:1LK2"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:1LK2"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:1LK2"
FT STRAND 216..232
FT /evidence="ECO:0007829|PDB:1LK2"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:1LK2"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:2MHA"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:1LK2"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:1T0N"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1LK2"
FT STRAND 262..271
FT /evidence="ECO:0007829|PDB:1LK2"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:1LK2"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:1LK2"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:6GB6"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:1LK2"
SQ SEQUENCE 369 AA; 41302 MW; 3D2F125318193443 CRC64;
MVPCTLLLLL AAALAPTQTR AGPHSLRYFV TAVSRPGLGE PRYMEVGYVD DTEFVRFDSD
AENPRYEPRA RWMEQEGPEY WERETQKAKG NEQSFRVDLR TLLGYYNQSK GGSHTIQVIS
GCEVGSDGRL LRGYQQYAYD GCDYIALNED LKTWTAADMA ALITKHKWEQ AGEAERLRAY
LEGTCVEWLR RYLKNGNATL LRTDSPKAHV THHSRPEDKV TLRCWALGFY PADITLTWQL
NGEELIQDME LVETRPAGDG TFQKWASVVV PLGKEQYYTC HVYHQGLPEP LTLRWEPPPS
TVSNMATVAV LVVLGAAIVT GAVVAFVMKM RRRNTGGKGG DYALAPGSQT SDLSLPDCKV
MVHDPHSLA
