ID KTHY_HUMAN Reviewed; 212 AA. AC P23919; B7ZW70; Q6FGX1; Q9BUX4; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 4. DT 24-JAN-2024, entry version 206. DE RecName: Full=Thymidylate kinase; DE EC=2.7.4.9 {ECO:0000269|PubMed:12614151, ECO:0000269|PubMed:2017365, ECO:0000269|PubMed:34918187, ECO:0000269|PubMed:8024690, ECO:0000305|PubMed:18469}; DE AltName: Full=dTMP kinase; GN Name=DTYMK; Synonyms=CDC8, TMPK, TYMK; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=2017365; DOI=10.1093/nar/19.4.823; RA Su J.Y., Sclafani R.A.; RT "Molecular cloning and expression of the human deoxythymidylate kinase gene RT in yeast."; RL Nucleic Acids Res. 19:823-827(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND RP DEVELOPMENTAL STAGE. RX PubMed=8024690; DOI=10.1089/dna.1994.13.461; RA Huang S.H., Tang A., Drisco B., Zhang S.Q., Seeger R., Li C., Jong A.; RT "Human dTMP kinase: gene expression and enzymatic activity coinciding with RT cell cycle progression and cell growth."; RL DNA Cell Biol. 13:461-471(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and Muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, AND PATHWAY. RX PubMed=18469; DOI=10.1016/s0021-9258(17)40077-9; RA Lee L.S., Cheng Y.; RT "Human thymidylate kinase. Purification, characterization, and kinetic RT behavior of the thymidylate kinase derived from chronic myelocytic RT leukemia."; RL J. Biol. Chem. 252:5686-5691(1977). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-169, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH ADP OR ATP ANALOG RP AND WITH THYMIDINE ANALOGS, CATALYTIC ACTIVITY, FUNCTION, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=12614151; DOI=10.1021/bi027302t; RA Ostermann N., Segura-Pena D., Meier C., Veit T., Monnerjahn C., Konrad M., RA Lavie A.; RT "Structures of human thymidylate kinase in complex with prodrugs: RT implications for the structure-based design of novel compounds."; RL Biochemistry 42:2568-2577(2003). RN [12] RP INVOLVEMENT IN CONPM, AND VARIANT CONPM THR-99. RX PubMed=31271740; DOI=10.1016/j.cca.2019.06.028; RA Lam C.W., Yeung W.L., Ling T.K., Wong K.C., Law C.Y.; RT "Deoxythymidylate kinase, DTYMK, is a novel gene for mitochondrial DNA RT depletion syndrome."; RL Clin. Chim. Acta 496:93-99(2019). RN [13] RP INVOLVEMENT IN CONPM, VARIANTS CONPM LEU-81 AND ASN-128, FUNCTION, RP CATALYTIC ACTIVITY, AND CHARACTERIZATION OF VARIANTS CONPM LEU-81 AND RP ASN-128. RX PubMed=34918187; DOI=10.1007/s00401-021-02394-0; RA Vanoevelen J.M., Bierau J., Grashorn J.C., Lambrichs E., Kamsteeg E.J., RA Bok L.A., Wevers R.A., van der Knaap M.S., Bugiani M., Frisk J.H., RA Colnaghi R., O'Driscoll M., Hellebrekers D.M.E.I., Rodenburg R., RA Ferreira C.R., Brunner H.G., van den Wijngaard A., Abdel-Salam G.M.H., RA Wang L., Stumpel C.T.R.M.; RT "DTYMK is essential for genome integrity and neuronal survival."; RL Acta Neuropathol. 143:245-262(2022). CC -!- FUNCTION: Catalyzes the phosphorylation of thymidine monophosphate CC (dTMP) to thymidine diphosphate (dTDP), the immediate precursor for the CC DNA building block dTTP, with ATP as the preferred phosphoryl donor in CC the presence of Mg(2+). {ECO:0000269|PubMed:12614151, CC ECO:0000269|PubMed:2017365, ECO:0000269|PubMed:34918187, CC ECO:0000269|PubMed:8024690, ECO:0000305|PubMed:18469}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + dTMP = ADP + dTDP; Xref=Rhea:RHEA:13517, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58369, ChEBI:CHEBI:63528, CC ChEBI:CHEBI:456216; EC=2.7.4.9; CC Evidence={ECO:0000269|PubMed:12614151, ECO:0000269|PubMed:2017365, CC ECO:0000269|PubMed:34918187, ECO:0000269|PubMed:8024690, CC ECO:0000305|PubMed:18469}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:18469}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=12 uM for AZTMP {ECO:0000269|PubMed:12614151}; CC KM=5 uM for dTMP {ECO:0000269|PubMed:12614151}; CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. CC {ECO:0000269|PubMed:18469}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18469}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P23919-1; Sequence=Displayed; CC Name=2; CC IsoId=P23919-2; Sequence=VSP_054164; CC -!- DEVELOPMENTAL STAGE: The levels of dTMP kinase mRNA and its enzymatic CC activity fluctuate during the cell cycle, peaking at the S phase. CC {ECO:0000269|PubMed:8024690}. CC -!- DISEASE: Neurodegeneration, childhood-onset, with progressive CC microcephaly (CONPM) [MIM:619847]: An autosomal recessive disorder CC characterized by global developmental delay apparent from infancy. Most CC severely affected individuals have severe and progressive microcephaly, CC early-onset seizures, lack of visual tracking, and almost no CC developmental milestones, resulting in early death. Less severely CC affected individuals have a small head circumference and severely CC impaired intellectual development with poor speech and motor delay. CC Additional features may include poor overall growth, axial hypotonia, CC limb hypertonia with spasticity, undescended testes, and cerebral CC atrophy with neuronal loss. {ECO:0000269|PubMed:31271740, CC ECO:0000269|PubMed:34918187}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the thymidylate kinase 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; X54729; CAA38528.1; -; mRNA. DR EMBL; L16991; AAA21719.1; -; mRNA. DR EMBL; CR541986; CAG46783.1; -; mRNA. DR EMBL; BC001827; AAH01827.1; -; mRNA. DR EMBL; BC171902; AAI71902.1; -; mRNA. DR CCDS; CCDS2552.1; -. [P23919-1] DR PIR; S26845; S26845. DR RefSeq; NP_001158503.1; NM_001165031.1. [P23919-2] DR RefSeq; NP_001307832.1; NM_001320903.1. DR RefSeq; NP_036277.2; NM_012145.3. [P23919-1] DR PDB; 1E2D; X-ray; 1.65 A; A=1-212. DR PDB; 1E2E; X-ray; 2.00 A; A=1-212. DR PDB; 1E2F; X-ray; 1.60 A; A=1-212. DR PDB; 1E2G; X-ray; 1.70 A; A=1-212. DR PDB; 1E2Q; X-ray; 1.70 A; A=1-212. DR PDB; 1E98; X-ray; 1.90 A; A=1-212. DR PDB; 1E99; X-ray; 1.80 A; A=1-212. DR PDB; 1E9A; X-ray; 1.60 A; A=1-212. DR PDB; 1E9B; X-ray; 1.70 A; A=1-212. DR PDB; 1E9C; X-ray; 1.60 A; A=1-212. DR PDB; 1E9D; X-ray; 1.70 A; A=1-212. DR PDB; 1E9E; X-ray; 1.60 A; A=1-212. DR PDB; 1E9F; X-ray; 1.90 A; A=1-144, A=149-212. DR PDB; 1NMX; X-ray; 1.70 A; A=1-212. DR PDB; 1NMY; X-ray; 1.60 A; A=4-212. DR PDB; 1NMZ; X-ray; 1.75 A; A=1-212. DR PDB; 1NN0; X-ray; 1.60 A; A=1-212. DR PDB; 1NN1; X-ray; 1.90 A; A=1-212. DR PDB; 1NN3; X-ray; 1.55 A; A=1-212. DR PDB; 1NN5; X-ray; 1.50 A; A=1-212. DR PDB; 2XX3; X-ray; 2.00 A; A=1-212. DR PDBsum; 1E2D; -. DR PDBsum; 1E2E; -. DR PDBsum; 1E2F; -. DR PDBsum; 1E2G; -. DR PDBsum; 1E2Q; -. DR PDBsum; 1E98; -. DR PDBsum; 1E99; -. DR PDBsum; 1E9A; -. DR PDBsum; 1E9B; -. DR PDBsum; 1E9C; -. DR PDBsum; 1E9D; -. DR PDBsum; 1E9E; -. DR PDBsum; 1E9F; -. DR PDBsum; 1NMX; -. DR PDBsum; 1NMY; -. DR PDBsum; 1NMZ; -. DR PDBsum; 1NN0; -. DR PDBsum; 1NN1; -. DR PDBsum; 1NN3; -. DR PDBsum; 1NN5; -. DR PDBsum; 2XX3; -. DR AlphaFoldDB; P23919; -. DR SMR; P23919; -. DR BioGRID; 108174; 66. DR IntAct; P23919; 9. DR MINT; P23919; -. DR STRING; 9606.ENSP00000304802; -. DR BindingDB; P23919; -. DR ChEMBL; CHEMBL4388; -. DR DrugBank; DB03150; 2',3'-Dideoxythymidine-5'-Monophosphate. DR DrugBank; DB03233; 3'-deoxy-3'-aminothymidine monophosphate. DR DrugBank; DB03195; 3'-Fluoro-3'-deoxythymidine 5'-monophosphate. DR DrugBank; DB03845; P1-(5'-Adenosyl)P5-(5'-(3'azido-3'-Deoxythymidyl))Pentaphosphate. DR DrugBank; DB03280; p1-(5'-adenosyl)p5-(5'-thymidyl)pentaphosphate. DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester. DR DrugBank; DB01643; Thymidine monophosphate. DR DrugBank; DB03666; Zidovudine monophosphate. DR DrugCentral; P23919; -. DR GlyGen; P23919; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P23919; -. DR PhosphoSitePlus; P23919; -. DR SwissPalm; P23919; -. DR BioMuta; DTYMK; -. DR DMDM; 56405325; -. DR EPD; P23919; -. DR jPOST; P23919; -. DR MassIVE; P23919; -. DR MaxQB; P23919; -. DR PaxDb; 9606-ENSP00000304802; -. DR PeptideAtlas; P23919; -. DR ProteomicsDB; 54165; -. [P23919-1] DR Pumba; P23919; -. DR Antibodypedia; 34572; 537 antibodies from 30 providers. DR DNASU; 1841; -. DR Ensembl; ENST00000305784.7; ENSP00000304802.2; ENSG00000168393.13. [P23919-1] DR GeneID; 1841; -. DR KEGG; hsa:1841; -. DR MANE-Select; ENST00000305784.7; ENSP00000304802.2; NM_012145.4; NP_036277.2. DR AGR; HGNC:3061; -. DR CTD; 1841; -. DR DisGeNET; 1841; -. DR GeneCards; DTYMK; -. DR HGNC; HGNC:3061; DTYMK. DR HPA; ENSG00000168393; Low tissue specificity. DR MalaCards; DTYMK; -. DR MIM; 188345; gene. DR MIM; 619847; phenotype. DR neXtProt; NX_P23919; -. DR OpenTargets; ENSG00000168393; -. DR PharmGKB; PA150; -. DR VEuPathDB; HostDB:ENSG00000168393; -. DR eggNOG; KOG3327; Eukaryota. DR GeneTree; ENSGT00940000154030; -. DR InParanoid; P23919; -. DR OMA; YWHQFDA; -. DR OrthoDB; 5473102at2759; -. DR PhylomeDB; P23919; -. DR TreeFam; TF324638; -. DR BioCyc; MetaCyc:HS11626-MONOMER; -. DR BRENDA; 2.7.4.9; 2681. DR PathwayCommons; P23919; -. DR Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates. DR SABIO-RK; P23919; -. DR SignaLink; P23919; -. DR SIGNOR; P23919; -. DR UniPathway; UPA00575; -. DR BioGRID-ORCS; 1841; 809 hits in 1168 CRISPR screens. DR EvolutionaryTrace; P23919; -. DR GeneWiki; DTYMK; -. DR GenomeRNAi; 1841; -. DR Pharos; P23919; Tbio. DR PRO; PR:P23919; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P23919; Protein. DR Bgee; ENSG00000168393; Expressed in ventricular zone and 143 other cell types or tissues. DR ExpressionAtlas; P23919; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IBA:GO_Central. DR GO; GO:0004798; F:thymidylate kinase activity; IDA:UniProtKB. DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl. DR GO; GO:0006233; P:dTDP biosynthetic process; IDA:UniProtKB. DR GO; GO:0006235; P:dTTP biosynthetic process; IBA:GO_Central. DR GO; GO:0006227; P:dUDP biosynthetic process; IBA:GO_Central. DR GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl. DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl. DR GO; GO:0046105; P:thymidine biosynthetic process; IDA:UniProtKB. DR CDD; cd01672; TMPK; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00165; Thymidylate_kinase; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR039430; Thymidylate_kin-like_dom. DR InterPro; IPR018095; Thymidylate_kin_CS. DR InterPro; IPR018094; Thymidylate_kinase. DR NCBIfam; TIGR00041; DTMP_kinase; 1. DR PANTHER; PTHR10344; THYMIDYLATE KINASE; 1. DR PANTHER; PTHR10344:SF1; THYMIDYLATE KINASE; 1. DR Pfam; PF02223; Thymidylate_kin; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS01331; THYMIDYLATE_KINASE; 1. DR Genevisible; P23919; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; KW Disease variant; Intellectual disability; Kinase; Neurodegeneration; KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome; KW Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..212 FT /note="Thymidylate kinase" FT /id="PRO_0000155210" FT REGION 133..157 FT /note="LID" FT /evidence="ECO:0000305|PubMed:12614151" FT BINDING 16..21 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:12614151, FT ECO:0007744|PDB:1NMX, ECO:0007744|PDB:1NMY, FT ECO:0007744|PDB:1NN0, ECO:0007744|PDB:1NN3" FT BINDING 97 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:12614151, FT ECO:0007744|PDB:1NMY, ECO:0007744|PDB:1NMZ, FT ECO:0007744|PDB:1NN1" FT BINDING 182 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0007744|PDB:1NMX, ECO:0007744|PDB:1NMY, FT ECO:0007744|PDB:1NN0, ECO:0007744|PDB:1NN3" FT BINDING 192 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0007744|PDB:1NMY, ECO:0007744|PDB:1NMZ, FT ECO:0007744|PDB:1NN1, ECO:0007744|PDB:1NN5" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 169 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT VAR_SEQ 111..134 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_054164" FT VARIANT 81 FT /note="P -> L (in CONPM; loss of catalytic activity in FT patient fibroblasts; dbSNP:rs1267106442)" FT /evidence="ECO:0000269|PubMed:34918187" FT /id="VAR_087114" FT VARIANT 99 FT /note="A -> T (in CONPM; uncertain significance; FT dbSNP:rs887888951)" FT /evidence="ECO:0000269|PubMed:31271740" FT /id="VAR_087115" FT VARIANT 128 FT /note="D -> N (in CONPM; loss of catalytic activity in FT patient fibroblasts; dbSNP:rs373875797)" FT /evidence="ECO:0000269|PubMed:34918187" FT /id="VAR_087116" FT CONFLICT 3 FT /note="A -> P (in Ref. 3; CAG46783)" FT /evidence="ECO:0000305" FT CONFLICT 31..37 FT /note="CAAGHRA -> SRGPPP (in Ref. 1; CAA38528)" FT /evidence="ECO:0000305" FT CONFLICT 58 FT /note="Q -> K (in Ref. 2; AAA21719)" FT /evidence="ECO:0000305" FT CONFLICT 68 FT /note="V -> A (in Ref. 3; CAG46783)" FT /evidence="ECO:0000305" FT CONFLICT 183..184 FT /note="SI -> RL (in Ref. 1; CAA38528)" FT /evidence="ECO:0000305" FT CONFLICT 190..191 FT /note="DI -> EL (in Ref. 1; CAA38528 and 2; AAA21719)" FT /evidence="ECO:0000305" FT STRAND 8..14 FT /evidence="ECO:0007829|PDB:1NN5" FT HELIX 19..32 FT /evidence="ECO:0007829|PDB:1NN5" FT STRAND 37..43 FT /evidence="ECO:0007829|PDB:1NN5" FT HELIX 48..57 FT /evidence="ECO:0007829|PDB:1NN5" FT HELIX 65..77 FT /evidence="ECO:0007829|PDB:1NN5" FT HELIX 80..88 FT /evidence="ECO:0007829|PDB:1NN5" FT STRAND 92..97 FT /evidence="ECO:0007829|PDB:1NN5" FT HELIX 99..107 FT /evidence="ECO:0007829|PDB:1NN5" FT HELIX 114..118 FT /evidence="ECO:0007829|PDB:1NN5" FT HELIX 119..121 FT /evidence="ECO:0007829|PDB:1NN5" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:1NN3" FT STRAND 128..134 FT /evidence="ECO:0007829|PDB:1NN5" FT HELIX 137..142 FT /evidence="ECO:0007829|PDB:1NN5" FT HELIX 149..151 FT /evidence="ECO:0007829|PDB:2XX3" FT HELIX 154..167 FT /evidence="ECO:0007829|PDB:1NN5" FT STRAND 171..173 FT /evidence="ECO:0007829|PDB:1E2E" FT STRAND 175..179 FT /evidence="ECO:0007829|PDB:1NN5" FT HELIX 184..201 FT /evidence="ECO:0007829|PDB:1NN5" FT HELIX 202..204 FT /evidence="ECO:0007829|PDB:1NN5" SQ SEQUENCE 212 AA; 23819 MW; A52876625B3621B1 CRC64; MAARRGALIV LEGVDRAGKS TQSRKLVEAL CAAGHRAELL RFPERSTEIG KLLSSYLQKK SDVEDHSVHL LFSANRWEQV PLIKEKLSQG VTLVVDRYAF SGVAFTGAKE NFSLDWCKQP DVGLPKPDLV LFLQLQLADA AKRGAFGHER YENGAFQERA LRCFHQLMKD TTLNWKMVDA SKSIEAVHED IRVLSEDAIR TATEKPLGEL WK //