NMT2_HUMAN
ID NMT2_HUMAN Reviewed; 498 AA.
AC O60551; B0YJ49; Q53Y38; Q5VUC8; Q9BRB4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Glycylpeptide N-tetradecanoyltransferase 2;
DE EC=2.3.1.97 {ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:9506952};
DE AltName: Full=Myristoyl-CoA:protein N-myristoyltransferase 2;
DE Short=NMT 2;
DE AltName: Full=Peptide N-myristoyltransferase 2;
DE AltName: Full=Protein-lysine myristoyltransferase NMT2 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:32103017};
DE AltName: Full=Type II N-myristoyltransferase;
GN Name=NMT2 {ECO:0000303|PubMed:9506952, ECO:0000312|HGNC:HGNC:7858};
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, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Liver;
RX PubMed=9506952; DOI=10.1074/jbc.273.12.6595;
RA Giang D.K., Cravatt B.F.;
RT "A second mammalian N-myristoyltransferase.";
RL J. Biol. Chem. 273:6595-6598(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Rundle D.R., Anderson R.E.;
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, 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 [11]
RP X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) OF 112-498 IN COMPLEX WITH SUBSTRATE
RP ANALOG, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [12] {ECO:0007744|PDB:6PAU}
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 116-498, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=32103017; DOI=10.1038/s41467-020-14893-x;
RA Kosciuk T., Price I.R., Zhang X., Zhu C., Johnson K.N., Zhang S.,
RA Halaby S.L., Komaniecki G.P., Yang M., DeHart C.J., Thomas P.M.,
RA Kelleher N.L., Fromme J.C., Lin H.;
RT "NMT1 and NMT2 are lysine myristoyltransferases regulating the ARF6 GTPase
RT cycle.";
RL Nat. Commun. 11:1067-1067(2020).
CC -!- FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of
CC certain cellular and viral proteins (PubMed:25255805, PubMed:9506952).
CC Also able to mediate N-terminal lysine myristoylation of proteins:
CC catalyzes myristoylation of ARF6 on both 'Gly-2' and 'Lys-3'
CC (PubMed:32103017). Lysine myristoylation is required to maintain ARF6
CC on membranes during the GTPase cycle (PubMed:32103017).
CC {ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:32103017,
CC ECO:0000269|PubMed:9506952}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-terminal glycyl-[protein] + tetradecanoyl-CoA = CoA + H(+) +
CC N-tetradecanoylglycyl-[protein]; Xref=Rhea:RHEA:15521, Rhea:RHEA-
CC COMP:12666, Rhea:RHEA-COMP:12667, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:64723,
CC ChEBI:CHEBI:133050; EC=2.3.1.97;
CC Evidence={ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:32103017,
CC ECO:0000269|PubMed:9506952};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-terminal glycyl-L-lysyl-[protein] + tetradecanoyl-CoA = CoA
CC + H(+) + N-terminal glycyl-(N(6)-tetradecanoyl)-L-lysyl-[protein];
CC Xref=Rhea:RHEA:70671, Rhea:RHEA-COMP:17947, Rhea:RHEA-COMP:17948,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:189855, ChEBI:CHEBI:189856;
CC Evidence={ECO:0000269|PubMed:32103017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70672;
CC Evidence={ECO:0000269|PubMed:32103017};
CC -!- INTERACTION:
CC O60551; Q9BR61: ACBD6; NbExp=16; IntAct=EBI-3920273, EBI-2848793;
CC O60551; P20290-2: BTF3; NbExp=3; IntAct=EBI-3920273, EBI-1054703;
CC O60551; P42574: CASP3; NbExp=2; IntAct=EBI-3920273, EBI-524064;
CC O60551; Q8N2W9: PIAS4; NbExp=3; IntAct=EBI-3920273, EBI-473160;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9506952}. Membrane
CC {ECO:0000269|PubMed:9506952}; Peripheral membrane protein
CC {ECO:0000269|PubMed:9506952}.
CC -!- SIMILARITY: Belongs to the NMT family. {ECO:0000305}.
CC -!- CAUTION: Sequence AAF36406.2 was incorrectly indicated as originating
CC from bovine. {ECO:0000305}.
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DR EMBL; AF043325; AAC09295.1; -; mRNA.
DR EMBL; AF232826; AAF36406.2; -; mRNA.
DR EMBL; BT007024; AAP35670.1; -; mRNA.
DR EMBL; EF445001; ACA06028.1; -; Genomic_DNA.
DR EMBL; EF445001; ACA06029.1; -; Genomic_DNA.
DR EMBL; AL590365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86238.1; -; Genomic_DNA.
DR EMBL; BC006376; AAH06376.1; -; mRNA.
DR CCDS; CCDS7109.1; -.
DR RefSeq; NP_001295224.1; NM_001308295.1.
DR RefSeq; NP_004799.1; NM_004808.2.
DR PDB; 4C2X; X-ray; 2.33 A; A=112-498.
DR PDB; 6PAU; X-ray; 1.93 A; A=116-498.
DR PDBsum; 4C2X; -.
DR PDBsum; 6PAU; -.
DR AlphaFoldDB; O60551; -.
DR SMR; O60551; -.
DR BioGRID; 114794; 73.
DR IntAct; O60551; 35.
DR MINT; O60551; -.
DR STRING; 9606.ENSP00000367407; -.
DR BindingDB; O60551; -.
DR ChEMBL; CHEMBL2849; -.
DR DrugBank; DB07838; (Z)-3-BENZYL-5-(2-HYDROXY-3-NITROBENZYLIDENE)-2-THIOXOTHIAZOLIDIN-4-ONE.
DR DrugBank; DB07061; 1-(CYCLOHEXYLAMINO)-3-(6-METHYL-3,4-DIHYDRO-1H-CARBAZOL-9(2H)-YL)PROPAN-2-OL.
DR DrugBank; DB02180; Myristoyl-Coa.
DR DrugBank; DB02271; S-(2-oxo)pentadecylcoa.
DR iPTMnet; O60551; -.
DR MetOSite; O60551; -.
DR PhosphoSitePlus; O60551; -.
DR SwissPalm; O60551; -.
DR BioMuta; NMT2; -.
DR EPD; O60551; -.
DR jPOST; O60551; -.
DR MassIVE; O60551; -.
DR MaxQB; O60551; -.
DR PaxDb; O60551; -.
DR PeptideAtlas; O60551; -.
DR PRIDE; O60551; -.
DR ProteomicsDB; 49467; -.
DR Antibodypedia; 673; 424 antibodies from 28 providers.
DR DNASU; 9397; -.
DR Ensembl; ENST00000378165.9; ENSP00000367407.3; ENSG00000152465.18.
DR GeneID; 9397; -.
DR KEGG; hsa:9397; -.
DR MANE-Select; ENST00000378165.9; ENSP00000367407.3; NM_004808.3; NP_004799.1.
DR UCSC; uc001inz.2; human.
DR CTD; 9397; -.
DR DisGeNET; 9397; -.
DR GeneCards; NMT2; -.
DR HGNC; HGNC:7858; NMT2.
DR HPA; ENSG00000152465; Low tissue specificity.
DR MIM; 603801; gene.
DR neXtProt; NX_O60551; -.
DR OpenTargets; ENSG00000152465; -.
DR PharmGKB; PA31662; -.
DR VEuPathDB; HostDB:ENSG00000152465; -.
DR eggNOG; KOG2779; Eukaryota.
DR GeneTree; ENSGT00390000017837; -.
DR HOGENOM; CLU_022882_1_0_1; -.
DR InParanoid; O60551; -.
DR OMA; ILNVKSC; -.
DR OrthoDB; 1025421at2759; -.
DR PhylomeDB; O60551; -.
DR TreeFam; TF300701; -.
DR BRENDA; 2.3.1.97; 2681.
DR PathwayCommons; O60551; -.
DR Reactome; R-HSA-174490; Membrane binding and targetting of GAG proteins.
DR Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR SignaLink; O60551; -.
DR BioGRID-ORCS; 9397; 10 hits in 1075 CRISPR screens.
DR ChiTaRS; NMT2; human.
DR GeneWiki; NMT2; -.
DR GenomeRNAi; 9397; -.
DR Pharos; O60551; Tchem.
DR PRO; PR:O60551; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O60551; protein.
DR Bgee; ENSG00000152465; Expressed in endothelial cell and 191 other tissues.
DR ExpressionAtlas; O60551; baseline and differential.
DR Genevisible; O60551; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043657; C:host cell; IEA:GOC.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0004379; F:glycylpeptide N-tetradecanoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0018030; F:peptidyl-lysine N6-myristoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome.
DR GO; GO:0018008; P:N-terminal peptidyl-glycine N-myristoylation; IDA:UniProtKB.
DR GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; TAS:Reactome.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000903; NMT.
DR InterPro; IPR022677; NMT_C.
DR InterPro; IPR022678; NMT_CS.
DR InterPro; IPR022676; NMT_N.
DR PANTHER; PTHR11377; PTHR11377; 1.
DR Pfam; PF01233; NMT; 1.
DR Pfam; PF02799; NMT_C; 1.
DR PIRSF; PIRSF015892; N-myristl_transf; 1.
DR SUPFAM; SSF55729; SSF55729; 2.
DR PROSITE; PS00975; NMT_1; 1.
DR PROSITE; PS00976; NMT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Membrane; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..498
FT /note="Glycylpeptide N-tetradecanoyltransferase 2"
FT /id="PRO_0000064226"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..58
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000269|PubMed:25255805"
FT BINDING 122
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000269|PubMed:25255805"
FT BINDING 250
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000269|PubMed:25255805"
FT BINDING 252
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000269|PubMed:25255805"
FT BINDING 258
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000269|PubMed:25255805"
FT BINDING 260
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000269|PubMed:25255805"
FT BINDING 261
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000269|PubMed:25255805"
FT BINDING 262
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000269|PubMed:25255805"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CONFLICT 306
FT /note="R -> K (in Ref. 3; AAP35670 and 7; AAH06376)"
FT /evidence="ECO:0000305"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:4C2X"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:4C2X"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:6PAU"
FT HELIX 168..181
FT /evidence="ECO:0007829|PDB:6PAU"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:6PAU"
FT HELIX 196..203
FT /evidence="ECO:0007829|PDB:6PAU"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:6PAU"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:6PAU"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:6PAU"
FT STRAND 224..237
FT /evidence="ECO:0007829|PDB:6PAU"
FT STRAND 240..252
FT /evidence="ECO:0007829|PDB:6PAU"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:6PAU"
FT HELIX 261..274
FT /evidence="ECO:0007829|PDB:6PAU"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:6PAU"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:6PAU"
FT STRAND 293..304
FT /evidence="ECO:0007829|PDB:6PAU"
FT HELIX 305..310
FT /evidence="ECO:0007829|PDB:6PAU"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:6PAU"
FT HELIX 322..328
FT /evidence="ECO:0007829|PDB:6PAU"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:6PAU"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:6PAU"
FT HELIX 348..358
FT /evidence="ECO:0007829|PDB:6PAU"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:6PAU"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:6PAU"
FT HELIX 370..377
FT /evidence="ECO:0007829|PDB:6PAU"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:6PAU"
FT STRAND 384..390
FT /evidence="ECO:0007829|PDB:6PAU"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:4C2X"
FT STRAND 396..404
FT /evidence="ECO:0007829|PDB:6PAU"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:6PAU"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:4C2X"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:6PAU"
FT STRAND 427..431
FT /evidence="ECO:0007829|PDB:6PAU"
FT HELIX 433..446
FT /evidence="ECO:0007829|PDB:6PAU"
FT STRAND 450..456
FT /evidence="ECO:0007829|PDB:6PAU"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:6PAU"
FT TURN 463..468
FT /evidence="ECO:0007829|PDB:6PAU"
FT STRAND 470..482
FT /evidence="ECO:0007829|PDB:6PAU"
FT HELIX 490..492
FT /evidence="ECO:0007829|PDB:6PAU"
SQ SEQUENCE 498 AA; 56980 MW; 1B1486CC6559B6A9 CRC64;
MAEDSESAAS QQSLELDDQD TCGIDGDNEE ETEHAKGSPG GYLGAKKKKK KQKRKKEKPN
SGGTKSDSAS DSQEIKIQQP SKNPSVPMQK LQDIQRAMEL LSACQGPARN IDEAAKHRYQ
FWDTQPVPKL DEVITSHGAI EPDKDNVRQE PYSLPQGFMW DTLDLSDAEV LKELYTLLNE
NYVEDDDNMF RFDYSPEFLL WALRPPGWLL QWHCGVRVSS NKKLVGFISA IPANIRIYDS
VKKMVEINFL CVHKKLRSKR VAPVLIREIT RRVNLEGIFQ AVYTAGVVLP KPIATCRYWH
RSLNPRKLVE VKFSHLSRNM TLQRTMKLYR LPDVTKTSGL RPMEPKDIKS VRELINTYLK
QFHLAPVMDE EEVAHWFLPR EHIIDTFVVE SPNGKLTDFL SFYTLPSTVM HHPAHKSLKA
AYSFYNIHTE TPLLDLMSDA LILAKSKGFD VFNALDLMEN KTFLEKLKFG IGDGNLQYYL
YNWRCPGTDS EKVGLVLQ
