MVD1_HUMAN
ID MVD1_HUMAN Reviewed; 400 AA.
AC P53602; Q53Y65;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Diphosphomevalonate decarboxylase;
DE EC=4.1.1.33 {ECO:0000269|PubMed:18823933, ECO:0000269|PubMed:8626466, ECO:0000269|PubMed:9392419};
DE AltName: Full=Mevalonate (diphospho)decarboxylase;
DE Short=MDDase;
DE AltName: Full=Mevalonate pyrophosphate decarboxylase;
GN Name=MVD; Synonyms=MPD {ECO:0000303|PubMed:14972328};
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, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=8626466; DOI=10.1074/jbc.271.14.7895;
RA Toth M.J., Huwyler L.;
RT "Molecular cloning and expression of the cDNAs encoding human and yeast
RT mevalonate pyrophosphate decarboxylase.";
RL J. Biol. Chem. 271:7895-7898(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND FUNCTION.
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=11108725;
RA Olivier L.M., Kovacs W., Masuda K., Keller G.A., Krisans S.K.;
RT "Identification of peroxisomal targeting signals in cholesterol
RT biosynthetic enzymes. AA-CoA thiolase, hmg-coa synthase, MPPD, and FPP
RT synthase.";
RL J. Lipid Res. 41:1921-1935(2000).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=14972328; DOI=10.1016/j.ymgme.2003.12.001;
RA Hogenboom S., Tuyp J.J., Espeel M., Koster J., Wanders R.J., Waterham H.R.;
RT "Human mevalonate pyrophosphate decarboxylase is localized in the
RT cytosol.";
RL Mol. Genet. Metab. 81:216-224(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
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 [10]
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 [11]
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=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION BY
RP 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 [14]
RP INVOLVEMENT IN POROK7, AND VARIANTS POROK7 ARG-101; VAL-128; GLN-161;
RP LEU-161; GLN-228; TRP-228; SER-249; SER-292; ILE-371 DEL AND ARG-376.
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 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), MUTAGENESIS OF ASN-17,
RP CHARACTERIZATION OF VARIANT POROK7 GLN-161, FUNCTION, CATALYTIC ACTIVITY,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18823933; DOI=10.1016/j.abb.2008.08.024;
RA Voynova N.E., Fu Z., Battaile K.P., Herdendorf T.J., Kim J.J.,
RA Miziorko H.M.;
RT "Human mevalonate diphosphate decarboxylase: characterization,
RT investigation of the mevalonate diphosphate binding site, and crystal
RT structure.";
RL Arch. Biochem. Biophys. 480:58-67(2008).
CC -!- FUNCTION: Catalyzes the ATP dependent decarboxylation of (R)-5-
CC diphosphomevalonate to form isopentenyl diphosphate (IPP). Functions in
CC the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP),
CC a key precursor for the biosynthesis of isoprenoids and sterol
CC synthesis. {ECO:0000269|PubMed:18823933, ECO:0000269|PubMed:8626466,
CC ECO:0000269|PubMed:9392419}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-5-diphosphomevalonate + ATP = ADP + CO2 + isopentenyl
CC diphosphate + phosphate; Xref=Rhea:RHEA:23732, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57557,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:456216; EC=4.1.1.33;
CC Evidence={ECO:0000269|PubMed:18823933, ECO:0000269|PubMed:8626466,
CC ECO:0000269|PubMed:9392419};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.4 uM for (R)-5-diphosphomevalonate {ECO:0000269|PubMed:9392419};
CC KM=28.9 uM for (S,R)-5-diphosphomevalonate
CC {ECO:0000269|PubMed:18823933};
CC KM=0.69 mM for ATP {ECO:0000269|PubMed:18823933};
CC KM=0.32 mM for ATP {ECO:0000269|PubMed:9392419};
CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8626466}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14972328}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, lung, liver,
CC brain, pancreas, kidney and placenta. {ECO:0000269|PubMed:8626466}.
CC -!- DISEASE: Porokeratosis 7, multiple types (POROK7) [MIM:614714]: 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:18823933,
CC ECO:0000269|PubMed:26202976}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the diphosphomevalonate decarboxylase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be located in the peroxisome
CC (PubMed:11108725). However, was later shown to be cytosolic
CC (PubMed:14972328). {ECO:0000269|PubMed:11108725,
CC ECO:0000269|PubMed:14972328}.
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DR EMBL; U49260; AAC50440.1; -; mRNA.
DR EMBL; BT006930; AAP35576.1; -; mRNA.
DR EMBL; CH471184; EAW66792.1; -; Genomic_DNA.
DR EMBL; BC000011; AAH00011.1; -; mRNA.
DR CCDS; CCDS10968.1; -.
DR RefSeq; NP_002452.1; NM_002461.2.
DR PDB; 3D4J; X-ray; 2.40 A; A/B=1-400.
DR PDBsum; 3D4J; -.
DR AlphaFoldDB; P53602; -.
DR SMR; P53602; -.
DR BioGRID; 110682; 45.
DR IntAct; P53602; 10.
DR STRING; 9606.ENSP00000301012; -.
DR BindingDB; P53602; -.
DR ChEMBL; CHEMBL4340; -.
DR GuidetoPHARMACOLOGY; 642; -.
DR SwissLipids; SLP:000001242; -.
DR GlyGen; P53602; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P53602; -.
DR PhosphoSitePlus; P53602; -.
DR BioMuta; MVD; -.
DR DMDM; 1706681; -.
DR EPD; P53602; -.
DR jPOST; P53602; -.
DR MassIVE; P53602; -.
DR MaxQB; P53602; -.
DR PaxDb; P53602; -.
DR PeptideAtlas; P53602; -.
DR PRIDE; P53602; -.
DR ProteomicsDB; 56588; -.
DR Antibodypedia; 30739; 207 antibodies from 28 providers.
DR DNASU; 4597; -.
DR Ensembl; ENST00000301012.8; ENSP00000301012.3; ENSG00000167508.12.
DR GeneID; 4597; -.
DR KEGG; hsa:4597; -.
DR MANE-Select; ENST00000301012.8; ENSP00000301012.3; NM_002461.3; NP_002452.1.
DR UCSC; uc002flg.2; human.
DR CTD; 4597; -.
DR DisGeNET; 4597; -.
DR GeneCards; MVD; -.
DR HGNC; HGNC:7529; MVD.
DR HPA; ENSG00000167508; Low tissue specificity.
DR MalaCards; MVD; -.
DR MIM; 603236; gene.
DR MIM; 614714; phenotype.
DR neXtProt; NX_P53602; -.
DR OpenTargets; ENSG00000167508; -.
DR Orphanet; 79152; Disseminated superficial actinic porokeratosis.
DR PharmGKB; PA31330; -.
DR VEuPathDB; HostDB:ENSG00000167508; -.
DR eggNOG; KOG2833; Eukaryota.
DR GeneTree; ENSGT00390000015359; -.
DR HOGENOM; CLU_040369_4_4_1; -.
DR InParanoid; P53602; -.
DR OMA; LTLHAMM; -.
DR OrthoDB; 1065019at2759; -.
DR PhylomeDB; P53602; -.
DR TreeFam; TF105952; -.
DR BioCyc; MetaCyc:ENSG00000167508-MON; -.
DR BRENDA; 4.1.1.33; 2681.
DR PathwayCommons; P53602; -.
DR Reactome; R-HSA-191273; Cholesterol biosynthesis.
DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR Reactome; R-HSA-446199; Synthesis of Dolichyl-phosphate.
DR SABIO-RK; P53602; -.
DR SignaLink; P53602; -.
DR SIGNOR; P53602; -.
DR UniPathway; UPA00063; -.
DR BioGRID-ORCS; 4597; 480 hits in 1079 CRISPR screens.
DR ChiTaRS; MVD; human.
DR EvolutionaryTrace; P53602; -.
DR GenomeRNAi; 4597; -.
DR Pharos; P53602; Tchem.
DR PRO; PR:P53602; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P53602; protein.
DR Bgee; ENSG00000167508; Expressed in right hemisphere of cerebellum and 111 other tissues.
DR ExpressionAtlas; P53602; baseline and differential.
DR Genevisible; P53602; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004163; F:diphosphomevalonate decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006695; P:cholesterol biosynthetic process; NAS:UniProtKB.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IBA:GO_Central.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; -; 1.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR005935; Mev_decarb.
DR InterPro; IPR029765; Mev_diP_decarb.
DR InterPro; IPR041431; Mvd1_C.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR Pfam; PF18376; MDD_C; 1.
DR PIRSF; PIRSF015950; Mev_P_decrbx; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
DR TIGRFAMs; TIGR01240; mevDPdecarb; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cholesterol biosynthesis;
KW Cholesterol metabolism; Cytoplasm; Disease variant; Lipid biosynthesis;
KW Lipid metabolism; Lyase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..400
FT /note="Diphosphomevalonate decarboxylase"
FT /id="PRO_0000087012"
FT BINDING 23..26
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 78
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 156..161
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 212
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VARIANT 101
FT /note="P -> R (in POROK7; unknown pathological
FT significance; dbSNP:rs200033380)"
FT /evidence="ECO:0000269|PubMed:26202976"
FT /id="VAR_075052"
FT VARIANT 128
FT /note="A -> V (in POROK7; unknown pathological
FT significance; dbSNP:rs776358937)"
FT /evidence="ECO:0000269|PubMed:26202976"
FT /id="VAR_075053"
FT VARIANT 161
FT /note="R -> L (in POROK7; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26202976"
FT /id="VAR_075054"
FT VARIANT 161
FT /note="R -> Q (in POROK7; 1000-fold diminution in
FT diphosphomevalonate decarboxylase activity;
FT dbSNP:rs144010349)"
FT /evidence="ECO:0000269|PubMed:18823933,
FT ECO:0000269|PubMed:26202976"
FT /id="VAR_075055"
FT VARIANT 228
FT /note="R -> Q (in POROK7; unknown pathological
FT significance; dbSNP:rs770939767)"
FT /evidence="ECO:0000269|PubMed:26202976"
FT /id="VAR_075056"
FT VARIANT 228
FT /note="R -> W (in POROK7; unknown pathological
FT significance; dbSNP:rs776684503)"
FT /evidence="ECO:0000269|PubMed:26202976"
FT /id="VAR_075057"
FT VARIANT 249
FT /note="F -> S (in POROK7; dbSNP:rs761991070)"
FT /evidence="ECO:0000269|PubMed:26202976"
FT /id="VAR_075058"
FT VARIANT 278
FT /note="N -> H (in dbSNP:rs34519538)"
FT /id="VAR_051605"
FT VARIANT 292
FT /note="N -> S (in POROK7; dbSNP:rs755948940)"
FT /evidence="ECO:0000269|PubMed:26202976"
FT /id="VAR_075059"
FT VARIANT 371
FT /note="Missing (in POROK7; unknown pathological
FT significance; dbSNP:rs764836183)"
FT /evidence="ECO:0000269|PubMed:26202976"
FT /id="VAR_075060"
FT VARIANT 376
FT /note="G -> R (in POROK7; unknown pathological
FT significance; dbSNP:rs546127665)"
FT /evidence="ECO:0000269|PubMed:26202976"
FT /id="VAR_075061"
FT MUTAGEN 17
FT /note="N->A: 15-fold inflation in KM for mevalonate
FT diphosphate."
FT /evidence="ECO:0000269|PubMed:18823933"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:3D4J"
FT STRAND 17..21
FT /evidence="ECO:0007829|PDB:3D4J"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:3D4J"
FT TURN 29..32
FT /evidence="ECO:0007829|PDB:3D4J"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:3D4J"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:3D4J"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:3D4J"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:3D4J"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:3D4J"
FT HELIX 77..88
FT /evidence="ECO:0007829|PDB:3D4J"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:3D4J"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:3D4J"
FT HELIX 126..139
FT /evidence="ECO:0007829|PDB:3D4J"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:3D4J"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:3D4J"
FT HELIX 157..163
FT /evidence="ECO:0007829|PDB:3D4J"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:3D4J"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:3D4J"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:3D4J"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:3D4J"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:3D4J"
FT HELIX 211..221
FT /evidence="ECO:0007829|PDB:3D4J"
FT HELIX 223..231
FT /evidence="ECO:0007829|PDB:3D4J"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:3D4J"
FT HELIX 249..268
FT /evidence="ECO:0007829|PDB:3D4J"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:3D4J"
FT HELIX 279..295
FT /evidence="ECO:0007829|PDB:3D4J"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:3D4J"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:3D4J"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:3D4J"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:3D4J"
FT HELIX 319..329
FT /evidence="ECO:0007829|PDB:3D4J"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:3D4J"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:3D4J"
FT HELIX 352..358
FT /evidence="ECO:0007829|PDB:3D4J"
FT STRAND 366..375
FT /evidence="ECO:0007829|PDB:3D4J"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:3D4J"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:3D4J"
SQ SEQUENCE 400 AA; 43405 MW; 3FD4741BCC4B68D8 CRC64;
MASEKPLAAV TCTAPVNIAV IKYWGKRDEE LVLPINSSLS VTLHQDQLKT TTTAVISKDF
TEDRIWLNGR EEDVGQPRLQ ACLREIRCLA RKRRNSRDGD PLPSSLSCKV HVASVNNFPT
AAGLASSAAG YACLAYTLAR VYGVESDLSE VARRGSGSAC RSLYGGFVEW QMGEQADGKD
SIARQVAPES HWPELRVLIL VVSAEKKLTG STVGMRASVE TSPLLRFRAE SVVPARMAEM
ARCIRERDFP SFAQLTMKDS NQFHATCLDT FPPISYLNAI SWRIIHLVHR FNAHHGDTKV
AYTFDAGPNA VIFTLDDTVA EFVAAVWHGF PPGSNGDTFL KGLQVRPAPL SAELQAALAM
EPTPGGVKYI IVTQVGPGPQ ILDDPCAHLL GPDGLPKPAA
