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 04-NOV-2026, entry version 230. 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, RC Spleen, 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. 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 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. 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}. 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; 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_001001892.3. 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=22-296. 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 PDB; 7WCY; X-ray; 2.36 A; A/D=22-296. DR PDB; 8JHW; X-ray; 3.12 A; A=22-296. DR AlphaFoldDB; P01901; -. DR MDposit; P01901; -. DR MDRepo; P01901; -. DR SMR; P01901; -. DR BioGRID; 200155; 5. DR DIP; DIP-6189N; -. DR FunCoup; P01901; 860. DR IntAct; P01901; 4. DR STRING; 10090.ENSMUSP00000025181; -. DR GlyCosmos; P01901; 3 sites, 2 glycans. DR GlyGen; P01901; 4 sites, 2 N-linked glycans (2 sites), 1 O-linked glycan (1 site). DR iPTMnet; P01901; -. DR PhosphoSitePlus; P01901; -. DR SwissPalm; P01901; -. DR jPOST; P01901; -. DR PaxDb; 10090-ENSMUSP00000025181; -. DR PeptideAtlas; P01901; -. DR ProteomicsDB; 269800; -. DR Pumba; P01901; -. DR ABCD; P01901; 1 sequenced antibody. DR DNASU; 14972; -. DR Ensembl; ENSMUST00000025181.18; ENSMUSP00000025181.11; ENSMUSG00000061232.17. DR GeneID; 14972; -. DR KEGG; mmu:14972; -. DR UCSC; uc008cap.1; mouse. DR AGR; MGI:95904; -. DR CTD; 14972; -. DR MGI; MGI:95904; H2-K1. DR VEuPathDB; HostDB:ENSMUSG00000061232; -. DR eggNOG; ENOG502RQEK; Eukaryota. DR GeneTree; ENSGT01120000271826; -. DR InParanoid; P01901; -. DR OMA; AGWTERK; -. DR OrthoDB; 8936120at2759; -. DR PhylomeDB; P01901; -. DR BioGRID-ORCS; 14972; 12 hits in 67 CRISPR screens. DR CD-CODE; 453FB656; Mast cell extracellular granules (MCEGs). DR EvolutionaryTrace; P01901; -. DR Proteomes; UP000000589; Chromosome 17. DR RNAct; P01901; protein. DR Bgee; ENSMUSG00000061232; Expressed in thoracic mammary gland and 235 other cell types or tissues. DR ExpressionAtlas; P01901; baseline and differential. DR GO; GO:0009986; C:cell surface; ISO:GO_Central. DR GO; GO:0033106; C:cis-Golgi network membrane; ISO:GO_Central. DR GO; GO:0005769; C:early endosome; ISO:GO_Central. DR GO; GO:0031901; C:early endosome membrane; ISO:GO_Central. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:GO_Central. DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISO:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:GO_Central. DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI. DR GO; GO:0005576; C:extracellular region; ISO:GO_Central. DR GO; GO:0005794; C:Golgi apparatus; ISO:GO_Central. DR GO; GO:0005797; C:Golgi medial cisterna; ISO:GO_Central. DR GO; GO:0000139; C:Golgi membrane; ISO:GO_Central. DR GO; GO:0098553; C:lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005765; C:lysosomal membrane; ISO:GO_Central. DR GO; GO:0042824; C:MHC class I peptide loading complex; ISO:GO_Central. DR GO; GO:0042612; C:MHC class I protein complex; ISO:GO_Central. DR GO; GO:0032398; C:MHC class Ib protein complex; ISO:GO_Central. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; ISO:GO_Central. DR GO; GO:0071889; F:14-3-3 protein binding; ISO:GO_Central. DR GO; GO:0030881; F:beta-2-microglobulin binding; ISO:GO_Central. DR GO; GO:0042610; F:CD8 receptor binding; ISO:GO_Central. DR GO; GO:0042802; F:identical protein binding; ISO:GO_Central. DR GO; GO:0042288; F:MHC class I protein binding; IPI:MGI. DR GO; GO:0046703; F:natural killer cell lectin-like receptor binding; ISO:GO_Central. DR GO; GO:0042605; F:peptide antigen binding; IDA:MGI. DR GO; GO:0042803; F:protein homodimerization activity; ISO:GO_Central. DR GO; GO:0051087; F:protein-folding chaperone binding; ISO:GO_Central. DR GO; GO:0048018; F:receptor ligand activity; ISO:GO_Central. DR GO; GO:0005102; F:signaling receptor binding; ISO:GO_Central. DR GO; GO:0042608; F:T cell receptor binding; ISO:GO_Central. DR GO; GO:0046977; F:TAP binding; ISO:GO_Central. DR GO; GO:0062061; F:TAP complex binding; ISO:GO_Central. DR GO; GO:0046978; F:TAP1 binding; ISO:GO_Central. DR GO; GO:0046979; F:TAP2 binding; ISO:GO_Central. 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:0002486; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent; IBA:GO_Central. 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:0006955; P:immune response; IBA:GO_Central. 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 CDD; cd21019; IgC1_MHC_Ia_H-2Kb; 1. DR FunFam; 2.60.40.10:FF:000014; H-2 class I histocompatibility antigen, alpha chain; 1. DR FunFam; 3.30.500.10:FF:000001; H-2 class I histocompatibility antigen, alpha chain; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 3.30.500.10; MHC class I-like antigen recognition-like; 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; IPR050208; MHC_class-I_related. 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 PANTHER; PTHR16675:SF251; HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, C ALPHA CHAIN; 1. DR PANTHER; PTHR16675; MHC CLASS I-RELATED; 1. 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; Immunoglobulin; 1. DR SUPFAM; SSF54452; MHC antigen-recognition domain; 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..179 FT /evidence="ECO:0007829|PDB:1LK2" FT HELIX 180..184 FT /evidence="ECO:0007829|PDB:1LK2" FT HELIX 185..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 //