PPM1H_HUMAN
ID PPM1H_HUMAN Reviewed; 514 AA.
AC Q9ULR3; B1Q2A9; B2RXG4; Q6PI86;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Protein phosphatase 1H;
DE EC=3.1.3.16;
GN Name=PPM1H; Synonyms=ARHCL1, KIAA1157, URCC2;
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].
RA Shimokawa T., Furukawa Y., Nakamura Y.;
RT "Cloning and characterization of Urcc2, a novel gene up-regulated in colon
RT cancer.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 87-514.
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [6]
RP IDENTIFICATION.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-211; SER-221;
RP THR-224 AND SER-422, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF HIS-153.
RX PubMed=22586611; DOI=10.1158/2159-8290.cd-11-0062;
RA Lee-Hoeflich S.T., Pham T.Q., Dowbenko D., Munroe X., Lee J., Li L.,
RA Zhou W., Haverty P.M., Pujara K., Stinson J., Chan S.M.,
RA Eastham-Anderson J., Pandita A., Seshagiri S., Hoeflich K.P.,
RA Turashvili G., Gelmon K.A., Aparicio S.A., Davis D.P., Sliwkowski M.X.,
RA Stern H.M.;
RT "PPM1H is a p27 phosphatase implicated in trastuzumab resistance.";
RL Cancer Discov. 1:326-337(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-211 AND SER-221, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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).
CC -!- FUNCTION: Dephosphorylates CDKN1B at 'Thr-187', thus removing a signal
CC for proteasomal degradation. {ECO:0000269|PubMed:22586611}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- INTERACTION:
CC Q9ULR3; Q9ULR3: PPM1H; NbExp=3; IntAct=EBI-8796752, EBI-8796752;
CC Q9ULR3; P61026: RAB10; NbExp=4; IntAct=EBI-8796752, EBI-726075;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22586611}. Cytoplasm
CC {ECO:0000269|PubMed:22586611}.
CC -!- MISCELLANEOUS: May act as a suppressor of trastuzumab resistance.
CC {ECO:0000303|PubMed:22586611}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC -!- CAUTION: A report observed N-glycosylation at Asn-354
CC (PubMed:19139490). However, as the protein is not predicted to localize
CC in an extracellular compartment of the cell, additional evidence is
CC required to confirm this result. {ECO:0000305|PubMed:19139490}.
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DR EMBL; AB084258; BAG16181.1; -; mRNA.
DR EMBL; AC023359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025264; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC048341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC078814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97112.1; -; Genomic_DNA.
DR EMBL; BC157843; AAI57844.1; -; mRNA.
DR EMBL; AB032983; BAA86471.1; -; mRNA.
DR CCDS; CCDS44934.1; -.
DR RefSeq; NP_065751.1; NM_020700.1.
DR PDB; 7KPR; X-ray; 3.09 A; A/B=33-514.
DR PDB; 7L4I; X-ray; 2.58 A; A/B=33-187, A/B=227-514.
DR PDB; 7L4J; X-ray; 2.45 A; A/B=33-187, A/B=227-514.
DR PDB; 7N0Z; X-ray; 2.19 A; A/B=33-187, A/B=227-514.
DR PDBsum; 7KPR; -.
DR PDBsum; 7L4I; -.
DR PDBsum; 7L4J; -.
DR PDBsum; 7N0Z; -.
DR AlphaFoldDB; Q9ULR3; -.
DR SMR; Q9ULR3; -.
DR BioGRID; 121530; 102.
DR IntAct; Q9ULR3; 48.
DR MINT; Q9ULR3; -.
DR STRING; 9606.ENSP00000228705; -.
DR DEPOD; PPM1H; -.
DR iPTMnet; Q9ULR3; -.
DR MetOSite; Q9ULR3; -.
DR PhosphoSitePlus; Q9ULR3; -.
DR BioMuta; PPM1H; -.
DR DMDM; 147721250; -.
DR EPD; Q9ULR3; -.
DR jPOST; Q9ULR3; -.
DR MassIVE; Q9ULR3; -.
DR MaxQB; Q9ULR3; -.
DR PaxDb; Q9ULR3; -.
DR PeptideAtlas; Q9ULR3; -.
DR PRIDE; Q9ULR3; -.
DR ProteomicsDB; 85100; -.
DR Antibodypedia; 53103; 157 antibodies from 22 providers.
DR DNASU; 57460; -.
DR Ensembl; ENST00000228705.7; ENSP00000228705.5; ENSG00000111110.12.
DR GeneID; 57460; -.
DR KEGG; hsa:57460; -.
DR MANE-Select; ENST00000228705.7; ENSP00000228705.5; NM_020700.2; NP_065751.1.
DR UCSC; uc001srk.5; human.
DR CTD; 57460; -.
DR DisGeNET; 57460; -.
DR GeneCards; PPM1H; -.
DR HGNC; HGNC:18583; PPM1H.
DR HPA; ENSG00000111110; Tissue enhanced (brain, parathyroid gland).
DR MIM; 616016; gene.
DR neXtProt; NX_Q9ULR3; -.
DR OpenTargets; ENSG00000111110; -.
DR PharmGKB; PA38354; -.
DR VEuPathDB; HostDB:ENSG00000111110; -.
DR eggNOG; KOG1323; Eukaryota.
DR GeneTree; ENSGT00940000160095; -.
DR HOGENOM; CLU_029072_2_0_1; -.
DR InParanoid; Q9ULR3; -.
DR OMA; KEHVEWT; -.
DR OrthoDB; 601888at2759; -.
DR PhylomeDB; Q9ULR3; -.
DR TreeFam; TF314700; -.
DR PathwayCommons; Q9ULR3; -.
DR SignaLink; Q9ULR3; -.
DR BioGRID-ORCS; 57460; 8 hits in 1075 CRISPR screens.
DR ChiTaRS; PPM1H; human.
DR GenomeRNAi; 57460; -.
DR Pharos; Q9ULR3; Tbio.
DR PRO; PR:Q9ULR3; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9ULR3; protein.
DR Bgee; ENSG00000111110; Expressed in paraflocculus and 177 other tissues.
DR Genevisible; Q9ULR3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IMP:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 2.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Methylation; Nucleus; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..514
FT /note="Protein phosphatase 1H"
FT /id="PRO_0000286603"
FT DOMAIN 77..507
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 109..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UYC0"
FT MOD_RES 113
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5M821"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 213
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q3UYC0"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 224
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MUTAGEN 153
FT /note="H->L: Decreased enzymatic activity."
FT /evidence="ECO:0000269|PubMed:22586611"
FT CONFLICT 77
FT /note="A -> V (in Ref. 4; AAI57844)"
FT /evidence="ECO:0000305"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:7N0Z"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:7N0Z"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:7N0Z"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:7N0Z"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:7L4J"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:7N0Z"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:7N0Z"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:7N0Z"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:7N0Z"
FT STRAND 143..156
FT /evidence="ECO:0007829|PDB:7N0Z"
FT HELIX 157..175
FT /evidence="ECO:0007829|PDB:7N0Z"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:7N0Z"
FT HELIX 237..259
FT /evidence="ECO:0007829|PDB:7N0Z"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:7N0Z"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:7N0Z"
FT STRAND 271..277
FT /evidence="ECO:0007829|PDB:7N0Z"
FT STRAND 280..288
FT /evidence="ECO:0007829|PDB:7N0Z"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:7N0Z"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:7N0Z"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:7N0Z"
FT HELIX 312..321
FT /evidence="ECO:0007829|PDB:7N0Z"
FT HELIX 323..326
FT /evidence="ECO:0007829|PDB:7N0Z"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:7N0Z"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:7N0Z"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:7N0Z"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:7N0Z"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:7N0Z"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:7N0Z"
FT STRAND 369..376
FT /evidence="ECO:0007829|PDB:7N0Z"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:7N0Z"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:7N0Z"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:7N0Z"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:7L4J"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:7N0Z"
FT STRAND 415..420
FT /evidence="ECO:0007829|PDB:7N0Z"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:7N0Z"
FT STRAND 431..435
FT /evidence="ECO:0007829|PDB:7N0Z"
FT HELIX 437..440
FT /evidence="ECO:0007829|PDB:7N0Z"
FT HELIX 445..455
FT /evidence="ECO:0007829|PDB:7N0Z"
FT HELIX 456..458
FT /evidence="ECO:0007829|PDB:7N0Z"
FT HELIX 466..479
FT /evidence="ECO:0007829|PDB:7N0Z"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:7N0Z"
FT STRAND 486..488
FT /evidence="ECO:0007829|PDB:7N0Z"
FT HELIX 490..492
FT /evidence="ECO:0007829|PDB:7N0Z"
FT STRAND 500..506
FT /evidence="ECO:0007829|PDB:7N0Z"
FT HELIX 507..510
FT /evidence="ECO:0007829|PDB:7N0Z"
SQ SEQUENCE 514 AA; 56448 MW; 9348C6AC3D74D1B7 CRC64;
MLTRVKSAVA NFMGGIMAGS SGSEHGGGSC GGSDLPLRFP YGRPEFLGLS QDEVECSADH
IARPILILKE TRRLPWATGY AEVINAGKST HNEDQASCEV LTVKKKAGAV TSTPNRNSSK
RRSSLPNGEG LQLKENSESE GVSCHYWSLF DGHAGSGAAV VASRLLQHHI TEQLQDIVDI
LKNSAVLPPT CLGEEPENTP ANSRTLTRAA SLRGGVGAPG SPSTPPTRFF TEKKIPHECL
VIGALESAFK EMDLQIERER SSYNISGGCT ALIVICLLGK LYVANAGDSR AIIIRNGEII
PMSSEFTPET ERQRLQYLAF MQPHLLGNEF THLEFPRRVQ RKELGKKMLY RDFNMTGWAY
KTIEDEDLKF PLIYGEGKKA RVMATIGVTR GLGDHDLKVH DSNIYIKPFL SSAPEVRIYD
LSKYDHGSDD VLILATDGLW DVLSNEEVAE AITQFLPNCD PDDPHRYTLA AQDLVMRARG
VLKDRGWRIS NDRLGSGDDI SVYVIPLIHG NKLS
