PMVK_HUMAN
ID PMVK_HUMAN Reviewed; 192 AA.
AC Q15126; Q5TZW9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Phosphomevalonate kinase;
DE Short=PMKase;
DE Short=hPMK;
DE EC=2.7.4.2 {ECO:0000269|PubMed:16519518, ECO:0000269|PubMed:17902708, ECO:0000269|PubMed:8663599, ECO:0000269|PubMed:9392419};
GN Name=PMVK; Synonyms=PMKI;
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], CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND
RP FUNCTION.
RC TISSUE=Liver;
RX PubMed=8663599; DOI=10.1074/jbc.271.29.17330;
RA Chambliss K.L., Slaughter C.A., Schreiner R., Hoffmann G.F., Gibson K.M.;
RT "Molecular cloning of human phosphomevalonate kinase and identification of
RT a consensus peroxisomal targeting sequence.";
RL J. Biol. Chem. 271:17330-17334(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-125.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin, and Uterus;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-192, AND INDUCTION.
RX PubMed=10191291;
RA Olivier L.M., Chambliss K.L., Gibson K.M., Krisans S.K.;
RT "Characterization of phosphomevalonate kinase: chromosomal localization,
RT regulation, and subcellular targeting.";
RL J. Lipid Res. 40:672-679(1999).
RN [5]
RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9392419;
RA Hinson D.D., Chambliss K.L., Toth M.J., Tanaka R.D., Gibson K.M.;
RT "Post-translational regulation of mevalonate kinase by intermediates of the
RT cholesterol and nonsterol isoprene biosynthetic pathways.";
RL J. Lipid Res. 38:2216-2223(1997).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=14729858; DOI=10.1194/jlr.m300373-jlr200;
RA Hogenboom S., Tuyp J.J., Espeel M., Koster J., Wanders R.J., Waterham H.R.;
RT "Phosphomevalonate kinase is a cytosolic protein in humans.";
RL J. Lipid Res. 45:697-705(2004).
RN [7]
RP FUNCTION, MUTAGENESIS OF LYS-17; ARG-18; LYS-19; LYS-22 AND ASP-23,
RP BIOPHYSICOCHEMICAL PROPERTIES, ATP-BINDING, CATALYTIC ACTIVITY, AND
RP SUBUNIT.
RX PubMed=16519518; DOI=10.1021/bi052231u;
RA Herdendorf T.J., Miziorko H.M.;
RT "Phosphomevalonate kinase: functional investigation of the recombinant
RT human enzyme.";
RL Biochemistry 45:3235-3242(2006).
RN [8]
RP FUNCTION, MUTAGENESIS OF LYS-48; LYS-69; ARG-73; ARG-84; ARG-110; ARG-111
RP AND ARG-141, ATP-BINDING, AND CATALYTIC ACTIVITY.
RX PubMed=17902708; DOI=10.1021/bi701408t;
RA Herdendorf T.J., Miziorko H.M.;
RT "Functional evaluation of conserved basic residues in human
RT phosphomevalonate kinase.";
RL Biochemistry 46:11780-11788(2007).
RN [9]
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
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 [12]
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 [13]
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS), ATP-BINDING, AND SUBSTRATE BINDING.
RX PubMed=18618710; DOI=10.1002/prot.22151;
RA Chang Q., Yan X.-X., Gu S.-Y., Liu J.-F., Liang D.-C.;
RT "Crystal structure of human phosphomevalonate kinase at 1.8 A resolution.";
RL Proteins 73:254-258(2008).
RN [14]
RP INVOLVEMENT IN POROK1, AND VARIANT POROK1 GLU-69.
RX PubMed=26202976; DOI=10.7554/elife.06322;
RA Zhang Z., Li C., Wu F., Ma R., Luan J., Yang F., Liu W., Wang L., Zhang S.,
RA Liu Y., Gu J., Hua W., Fan M., Peng H., Meng X., Song N., Bi X., Gu C.,
RA Zhang Z., Huang Q., Chen L., Xiang L., Xu J., Zheng Z., Jiang Z.;
RT "Genomic variations of the mevalonate pathway in porokeratosis.";
RL Elife 4:E06322-E06322(2015).
RN [15]
RP VARIANT POROK1 138-ARG--LEU-192 DEL, AND SUBCELLULAR LOCATION.
RX PubMed=27052676; DOI=10.1038/srep24226;
RA Wang J., Liu Y., Liu F., Huang C., Han S., Lv Y., Liu C.J., Zhang S.,
RA Qin Y., Ling L., Gao M., Yu S., Li C., Huang M., Liao S., Hu X., Lu Z.,
RA Liu X., Jiang T., Tang Z., Zhang H., Guo A.Y., Liu M.;
RT "Loss-of-function mutation in PMVK causes autosomal dominant disseminated
RT superficial porokeratosis.";
RL Sci. Rep. 6:24226-24226(2016).
CC -!- FUNCTION: Catalyzes the reversible ATP-dependent phosphorylation of
CC mevalonate 5-phosphate to produce mevalonate diphosphate and ADP, a key
CC step in the mevalonic acid mediated biosynthesis of isopentenyl
CC diphosphate and other polyisoprenoid metabolites.
CC {ECO:0000269|PubMed:16519518, ECO:0000269|PubMed:17902708,
CC ECO:0000269|PubMed:8663599, ECO:0000269|PubMed:9392419}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-5-phosphomevalonate + ATP = (R)-5-diphosphomevalonate +
CC ADP; Xref=Rhea:RHEA:16341, ChEBI:CHEBI:30616, ChEBI:CHEBI:57557,
CC ChEBI:CHEBI:58146, ChEBI:CHEBI:456216; EC=2.7.4.2;
CC Evidence={ECO:0000269|PubMed:16519518, ECO:0000269|PubMed:17902708,
CC ECO:0000269|PubMed:8663599, ECO:0000269|PubMed:9392419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16342;
CC Evidence={ECO:0000305|PubMed:16519518, ECO:0000305|PubMed:9392419};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16343;
CC Evidence={ECO:0000305|PubMed:16519518};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25 uM for (R)-5-phosphomevalonate {ECO:0000269|PubMed:16519518,
CC ECO:0000269|PubMed:9392419};
CC KM=0.26 mM for ATP {ECO:0000269|PubMed:16519518,
CC ECO:0000269|PubMed:9392419};
CC Vmax=46.4 umol/min/mg enzyme with (R)-5-phosphomevalonate as
CC substrate {ECO:0000269|PubMed:16519518, ECO:0000269|PubMed:9392419};
CC Vmax=52 umol/min/mg enzyme with ATP as substrate
CC {ECO:0000269|PubMed:16519518, ECO:0000269|PubMed:9392419};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC step 2/3. {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16519518}.
CC -!- INTERACTION:
CC Q15126; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-1055562, EBI-742054;
CC Q15126; Q13360-2: ZNF177; NbExp=3; IntAct=EBI-1055562, EBI-12272076;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10191291,
CC ECO:0000269|PubMed:27052676}.
CC -!- TISSUE SPECIFICITY: Heart, liver, skeletal muscle, kidney, and
CC pancreas. Lower level in brain, placenta and lung.
CC {ECO:0000269|PubMed:8663599}.
CC -!- INDUCTION: By sterol. {ECO:0000269|PubMed:10191291}.
CC -!- DISEASE: Porokeratosis 1, multiple types (POROK1) [MIM:175800]: A form
CC of porokeratosis, a disorder of faulty keratinization characterized by
CC one or more atrophic patches surrounded by a distinctive hyperkeratotic
CC ridgelike border called the cornoid lamella. The keratotic lesions can
CC progress to overt cutaneous neoplasms, typically squamous cell
CC carcinomas. Multiple clinical variants of porokeratosis are recognized,
CC including porokeratosis of Mibelli, linear porokeratosis, disseminated
CC superficial actinic porokeratosis, palmoplantar porokeratosis, and
CC punctate porokeratosis. Different clinical presentations can be
CC observed among members of the same family. Individuals expressing more
CC than one variant have also been reported. {ECO:0000269|PubMed:26202976,
CC ECO:0000269|PubMed:27052676}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- CAUTION: Was originally thought to be located in the peroxisome
CC (PubMed:10191291). However, was later shown to be cytosolic
CC (PubMed:14729858, PubMed:27052676). {ECO:0000269|PubMed:14729858,
CC ECO:0000269|PubMed:27052676, ECO:0000305|PubMed:10191291}.
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DR EMBL; L77213; AAC37593.1; -; mRNA.
DR EMBL; BT019976; AAV38779.1; -; mRNA.
DR EMBL; BC006089; AAH06089.1; -; mRNA.
DR EMBL; BC007694; AAH07694.1; -; mRNA.
DR EMBL; AF026069; AAC60791.1; -; Genomic_DNA.
DR CCDS; CCDS1073.1; -.
DR RefSeq; NP_006547.1; NM_006556.3.
DR PDB; 3CH4; X-ray; 1.76 A; B=1-192.
DR PDBsum; 3CH4; -.
DR AlphaFoldDB; Q15126; -.
DR SMR; Q15126; -.
DR BioGRID; 115897; 61.
DR IntAct; Q15126; 25.
DR MINT; Q15126; -.
DR STRING; 9606.ENSP00000357452; -.
DR GuidetoPHARMACOLOGY; 641; -.
DR SwissLipids; SLP:000001241; -.
DR iPTMnet; Q15126; -.
DR PhosphoSitePlus; Q15126; -.
DR BioMuta; PMVK; -.
DR DMDM; 3024422; -.
DR REPRODUCTION-2DPAGE; IPI00220648; -.
DR EPD; Q15126; -.
DR jPOST; Q15126; -.
DR MassIVE; Q15126; -.
DR PaxDb; Q15126; -.
DR PeptideAtlas; Q15126; -.
DR PRIDE; Q15126; -.
DR ProteomicsDB; 60453; -.
DR Antibodypedia; 34158; 246 antibodies from 28 providers.
DR DNASU; 10654; -.
DR Ensembl; ENST00000368467.4; ENSP00000357452.3; ENSG00000163344.6.
DR GeneID; 10654; -.
DR KEGG; hsa:10654; -.
DR MANE-Select; ENST00000368467.4; ENSP00000357452.3; NM_006556.4; NP_006547.1.
DR CTD; 10654; -.
DR DisGeNET; 10654; -.
DR GeneCards; PMVK; -.
DR HGNC; HGNC:9141; PMVK.
DR HPA; ENSG00000163344; Low tissue specificity.
DR MalaCards; PMVK; -.
DR MIM; 175800; phenotype.
DR MIM; 607622; gene.
DR neXtProt; NX_Q15126; -.
DR OpenTargets; ENSG00000163344; -.
DR Orphanet; 735; Porokeratosis of Mibelli.
DR PharmGKB; PA33465; -.
DR VEuPathDB; HostDB:ENSG00000163344; -.
DR eggNOG; ENOG502QYPQ; Eukaryota.
DR GeneTree; ENSGT00390000014801; -.
DR HOGENOM; CLU_092097_0_0_1; -.
DR InParanoid; Q15126; -.
DR OMA; YGFFCRA; -.
DR OrthoDB; 1307762at2759; -.
DR PhylomeDB; Q15126; -.
DR TreeFam; TF312935; -.
DR BioCyc; MetaCyc:HS08830-MON; -.
DR BRENDA; 2.7.4.2; 2681.
DR PathwayCommons; Q15126; -.
DR Reactome; R-HSA-191273; Cholesterol biosynthesis.
DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR SABIO-RK; Q15126; -.
DR SignaLink; Q15126; -.
DR UniPathway; UPA00057; UER00099.
DR BioGRID-ORCS; 10654; 297 hits in 1085 CRISPR screens.
DR ChiTaRS; PMVK; human.
DR EvolutionaryTrace; Q15126; -.
DR GenomeRNAi; 10654; -.
DR Pharos; Q15126; Tchem.
DR PRO; PR:Q15126; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q15126; protein.
DR Bgee; ENSG00000163344; Expressed in apex of heart and 199 other tissues.
DR ExpressionAtlas; Q15126; baseline and differential.
DR Genevisible; Q15126; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0004631; F:phosphomevalonate kinase activity; IDA:UniProtKB.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0070723; P:response to cholesterol; IEP:UniProtKB.
DR GO; GO:0016126; P:sterol biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005919; Pmev_kin_anim.
DR PANTHER; PTHR13101; PTHR13101; 1.
DR Pfam; PF04275; P-mevalo_kinase; 1.
DR PIRSF; PIRSF036639; PMK_anim; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01223; Pmev_kin_anim; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cholesterol biosynthesis;
KW Cholesterol metabolism; Cytoplasm; Disease variant; Kinase;
KW Lipid biosynthesis; Lipid metabolism; Nucleotide-binding;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transferase.
FT CHAIN 1..192
FT /note="Phosphomevalonate kinase"
FT /id="PRO_0000058472"
FT BINDING 17..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:16519518,
FT ECO:0000305|PubMed:18618710"
FT BINDING 141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:17902708,
FT ECO:0000305|PubMed:18618710"
FT BINDING 170
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18618710"
FT BINDING 171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:18618710"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:18618710"
FT BINDING 180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:18618710"
FT VARIANT 69
FT /note="K -> E (in POROK1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26202976"
FT /id="VAR_075051"
FT VARIANT 125
FT /note="V -> M (in dbSNP:rs16836525)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_051283"
FT VARIANT 138..192
FT /note="Missing (in POROK1; results in reduced expression
FT and solubility; disturbs subcellular localization with
FT punctate rather than diffuse cytoplasmic distribution)"
FT /evidence="ECO:0000269|PubMed:27052676"
FT /id="VAR_080138"
FT MUTAGEN 17
FT /note="K->M: Approximately 8-fold decrease in Vmax for
FT MgATP and R-MVP. Approximately 5-fold increase in KM for
FT MgATP and R-MVP."
FT /evidence="ECO:0000269|PubMed:16519518"
FT MUTAGEN 18
FT /note="R->Q: Approximately 85-fold decrease in Vmax for
FT MgATP and R-MVP. Approximately 5-fold increase in KM for
FT MgATP and R-MVP."
FT /evidence="ECO:0000269|PubMed:16519518"
FT MUTAGEN 19
FT /note="K->M: Approximately 9-fold decrease in Vmax for
FT MgATP and R-MVP. Approximately 10-fold increase in KM for
FT MgATP and R-MVP."
FT /evidence="ECO:0000269|PubMed:16519518"
FT MUTAGEN 22
FT /note="K->M: Approximately 100000-fold decrease in Vmax for
FT MgATP."
FT /evidence="ECO:0000269|PubMed:16519518"
FT MUTAGEN 23
FT /note="D->N: Approximately 7-fold decrease in Vmax for
FT MgATP and R-MVP. Approximately 10-fold increase in KM for
FT MgATP and 5-fold increase in KM for R-MVP."
FT /evidence="ECO:0000269|PubMed:16519518"
FT MUTAGEN 48
FT /note="K->M: Approximately 1400-fold decrease in Vmax for
FT MgATP and R-MVP. Approximately 3-fold increase in KM for
FT MgATP and R-MVP."
FT /evidence="ECO:0000269|PubMed:17902708"
FT MUTAGEN 69
FT /note="K->M: Approximately 500-fold decrease in Vmax for
FT MgATP and R-MVP. Approximately 3-fold increase in KM for
FT MgATP and R-MVP."
FT /evidence="ECO:0000269|PubMed:17902708"
FT MUTAGEN 73
FT /note="R->M: Approximately 3000-fold decrease in Vmax for
FT MgATP and R-MVP. No change in KM for MgATP and
FT approximately 3-fold increase in KM for R-MVP."
FT /evidence="ECO:0000269|PubMed:17902708"
FT MUTAGEN 84
FT /note="R->M: Approximately 10-fold decrease in Vmax for
FT MgATP and R-MVP. Approximately 3-fold increase in KM for
FT MgATP and 50-fold increase in KM for R-MVP."
FT /evidence="ECO:0000269|PubMed:17902708"
FT MUTAGEN 93
FT /note="R->M: Almost no change in KM and Vmax for MgATP and
FT R-MVP."
FT MUTAGEN 110
FT /note="R->M: Approximately 20000-fold decrease in Vmax for
FT MgATP."
FT /evidence="ECO:0000269|PubMed:17902708"
FT MUTAGEN 111
FT /note="R->M: Approximately 65-fold decrease in Vmax for
FT MgATP and R-MVP. Approximately 8-fold increase in KM for
FT MgATP and 60-fold increase in KM for R-MVP."
FT /evidence="ECO:0000269|PubMed:17902708"
FT MUTAGEN 130
FT /note="R->M: Approximately 4-fold decrease in Vmax for
FT MgATP and R-MVP. Approximately 3-fold increase in KM for
FT MgATP and R-MVP."
FT MUTAGEN 138
FT /note="R->M: Approximately 3-fold decrease in Vmax for
FT MgATP and R-MVP. Approximately 5-fold increase in KM for
FT MgATP and no change in KM for R-MVP."
FT MUTAGEN 141
FT /note="R->M: Approximately 15-fold decrease in Vmax for
FT MgATP and R-MVP. Approximately 50-fold increase in KM for
FT MgATP and approximately 7-fold in KM for R-MVP."
FT /evidence="ECO:0000269|PubMed:17902708"
FT STRAND 9..16
FT /evidence="ECO:0007829|PDB:3CH4"
FT HELIX 22..33
FT /evidence="ECO:0007829|PDB:3CH4"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:3CH4"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:3CH4"
FT HELIX 44..53
FT /evidence="ECO:0007829|PDB:3CH4"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:3CH4"
FT HELIX 72..86
FT /evidence="ECO:0007829|PDB:3CH4"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:3CH4"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:3CH4"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:3CH4"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:3CH4"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:3CH4"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:3CH4"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:3CH4"
FT TURN 147..151
FT /evidence="ECO:0007829|PDB:3CH4"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:3CH4"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:3CH4"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:3CH4"
FT HELIX 174..189
FT /evidence="ECO:0007829|PDB:3CH4"
SQ SEQUENCE 192 AA; 21995 MW; D7E720D0DDCCA249 CRC64;
MAPLGGAPRL VLLFSGKRKS GKDFVTEALQ SRLGADVCAV LRLSGPLKEQ YAQEHGLNFQ
RLLDTSTYKE AFRKDMIRWG EEKRQADPGF FCRKIVEGIS QPIWLVSDTR RVSDIQWFRE
AYGAVTQTVR VVALEQSRQQ RGWVFTPGVD DAESECGLDN FGDFDWVIEN HGVEQRLEEQ
LENLIEFIRS RL
