LCMT1_HUMAN
ID LCMT1_HUMAN Reviewed; 334 AA.
AC Q9UIC8; A6NL89; A8K770; Q53FC5; Q96CI5; Q9H6I9; Q9NTG4; Q9Y378;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Leucine carboxyl methyltransferase 1;
DE EC=2.1.1.233 {ECO:0000269|PubMed:10600115, ECO:0000269|PubMed:21206058};
DE AltName: Full=Protein-leucine O-methyltransferase;
DE AltName: Full=[Phosphatase 2A protein]-leucine-carboxy methyltransferase 1;
GN Name=LCMT1; Synonyms=LCMT; ORFNames=CGI-68;
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, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10600115; DOI=10.1021/bi991646a;
RA De Baere I., Derua R., Janssens V., Van Hoof C., Waelkens E., Merlevede W.,
RA Goris J.;
RT "Purification of porcine brain protein phosphatase 2A leucine carboxyl
RT methyltransferase and cloning of the human homologue.";
RL Biochemistry 38:16539-16547(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Skeletal muscle, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, and 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-334 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
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 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-334 IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE, AND CATALYTIC ACTIVITY.
RX PubMed=21206058; DOI=10.1107/s0907444910042204;
RA Tsai M.L., Cronin N., Djordjevic S.;
RT "The structure of human leucine carboxyl methyltransferase 1 that regulates
RT protein phosphatase PP2A.";
RL Acta Crystallogr. D 67:14-24(2011).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) ALONE AND IN COMPLEX WITH PPP2CA.
RX PubMed=21292165; DOI=10.1016/j.molcel.2010.12.030;
RA Stanevich V., Jiang L., Satyshur K.A., Li Y., Jeffrey P.D., Li Z.,
RA Menden P., Semmelhack M.F., Xing Y.;
RT "The structural basis for tight control of PP2A methylation and function by
RT LCMT-1.";
RL Mol. Cell 41:331-342(2011).
CC -!- FUNCTION: Methylates the carboxyl group of the C-terminal leucine
CC residue of protein phosphatase 2A catalytic subunits to form alpha-
CC leucine ester residues. {ECO:0000269|PubMed:10600115}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-
CC methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl
CC ester + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48544, Rhea:RHEA-
CC COMP:12134, Rhea:RHEA-COMP:12135, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:90516, ChEBI:CHEBI:90517;
CC EC=2.1.1.233; Evidence={ECO:0000269|PubMed:10600115,
CC ECO:0000269|PubMed:21206058};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 uM for PP2AD {ECO:0000269|PubMed:10600115};
CC KM=1.3 uM for AdoMet {ECO:0000269|PubMed:10600115};
CC -!- INTERACTION:
CC Q9UIC8; P51116: FXR2; NbExp=2; IntAct=EBI-747632, EBI-740459;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UIC8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UIC8-2; Sequence=VSP_017428;
CC Name=3;
CC IsoId=Q9UIC8-3; Sequence=VSP_041416;
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. LCMT family.
CC {ECO:0000305}.
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DR EMBL; AF037601; AAF18267.1; -; mRNA.
DR EMBL; AF151826; AAD34063.1; -; mRNA.
DR EMBL; AK025884; BAB15270.1; -; mRNA.
DR EMBL; AK223364; BAD97084.1; -; mRNA.
DR EMBL; AK291885; BAF84574.1; -; mRNA.
DR EMBL; AK314409; BAG37031.1; -; mRNA.
DR EMBL; AC008741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC133552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001214; AAH01214.1; -; mRNA.
DR EMBL; BC014217; AAH14217.1; -; mRNA.
DR EMBL; AL137283; CAB70677.1; -; mRNA.
DR CCDS; CCDS45445.1; -. [Q9UIC8-1]
DR CCDS; CCDS45446.1; -. [Q9UIC8-3]
DR PIR; T46352; T46352.
DR RefSeq; NP_001027563.1; NM_001032391.1. [Q9UIC8-3]
DR RefSeq; NP_057393.2; NM_016309.2. [Q9UIC8-1]
DR RefSeq; XP_011544166.1; XM_011545864.1. [Q9UIC8-2]
DR PDB; 3IEI; X-ray; 1.90 A; A/B/C/D/E/F/G/H=1-334.
DR PDB; 3O7W; X-ray; 2.00 A; A=23-232, A=259-334.
DR PDB; 3P71; X-ray; 2.70 A; T=1-334.
DR PDBsum; 3IEI; -.
DR PDBsum; 3O7W; -.
DR PDBsum; 3P71; -.
DR AlphaFoldDB; Q9UIC8; -.
DR SMR; Q9UIC8; -.
DR BioGRID; 119549; 21.
DR IntAct; Q9UIC8; 6.
DR MINT; Q9UIC8; -.
DR STRING; 9606.ENSP00000382021; -.
DR DrugBank; DB00149; Leucine.
DR iPTMnet; Q9UIC8; -.
DR MetOSite; Q9UIC8; -.
DR PhosphoSitePlus; Q9UIC8; -.
DR BioMuta; LCMT1; -.
DR DMDM; 12643251; -.
DR EPD; Q9UIC8; -.
DR jPOST; Q9UIC8; -.
DR MassIVE; Q9UIC8; -.
DR MaxQB; Q9UIC8; -.
DR PaxDb; Q9UIC8; -.
DR PeptideAtlas; Q9UIC8; -.
DR PRIDE; Q9UIC8; -.
DR ProteomicsDB; 84491; -. [Q9UIC8-1]
DR ProteomicsDB; 84492; -. [Q9UIC8-2]
DR ProteomicsDB; 84493; -. [Q9UIC8-3]
DR Antibodypedia; 26192; 263 antibodies from 21 providers.
DR DNASU; 51451; -.
DR Ensembl; ENST00000380966.8; ENSP00000370353.4; ENSG00000205629.12. [Q9UIC8-3]
DR Ensembl; ENST00000399069.8; ENSP00000382021.3; ENSG00000205629.12. [Q9UIC8-1]
DR GeneID; 51451; -.
DR KEGG; hsa:51451; -.
DR MANE-Select; ENST00000399069.8; ENSP00000382021.3; NM_016309.3; NP_057393.2.
DR UCSC; uc002dnx.2; human. [Q9UIC8-1]
DR CTD; 51451; -.
DR DisGeNET; 51451; -.
DR GeneCards; LCMT1; -.
DR HGNC; HGNC:17557; LCMT1.
DR HPA; ENSG00000205629; Low tissue specificity.
DR MIM; 610286; gene.
DR neXtProt; NX_Q9UIC8; -.
DR OpenTargets; ENSG00000205629; -.
DR PharmGKB; PA134928443; -.
DR VEuPathDB; HostDB:ENSG00000205629; -.
DR eggNOG; KOG2918; Eukaryota.
DR GeneTree; ENSGT00940000156372; -.
DR HOGENOM; CLU_031312_0_0_1; -.
DR InParanoid; Q9UIC8; -.
DR OMA; IIYEPIR; -.
DR OrthoDB; 1094856at2759; -.
DR PhylomeDB; Q9UIC8; -.
DR TreeFam; TF315087; -.
DR BioCyc; MetaCyc:MON-16510; -.
DR BRENDA; 2.1.1.233; 2681.
DR PathwayCommons; Q9UIC8; -.
DR Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR SABIO-RK; Q9UIC8; -.
DR SignaLink; Q9UIC8; -.
DR SIGNOR; Q9UIC8; -.
DR BioGRID-ORCS; 51451; 250 hits in 1090 CRISPR screens.
DR ChiTaRS; LCMT1; human.
DR EvolutionaryTrace; Q9UIC8; -.
DR GeneWiki; Leucine_carboxyl_methyltransferase_1; -.
DR GenomeRNAi; 51451; -.
DR Pharos; Q9UIC8; Tbio.
DR PRO; PR:Q9UIC8; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9UIC8; protein.
DR Bgee; ENSG00000205629; Expressed in middle temporal gyrus and 202 other tissues.
DR ExpressionAtlas; Q9UIC8; baseline and differential.
DR Genevisible; Q9UIC8; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003880; F:protein C-terminal carboxyl O-methyltransferase activity; IDA:MGI.
DR GO; GO:0018423; F:protein C-terminal leucine carboxyl O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; TAS:ProtInc.
DR GO; GO:0006481; P:C-terminal protein methylation; IDA:MGI.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IMP:MGI.
DR GO; GO:0006479; P:protein methylation; IMP:MGI.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:MGI.
DR GO; GO:0010906; P:regulation of glucose metabolic process; IEA:Ensembl.
DR GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; IMP:MGI.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016651; PPM1.
DR InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13600; PTHR13600; 1.
DR Pfam; PF04072; LCM; 1.
DR PIRSF; PIRSF016305; LCM_mtfrase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..334
FT /note="Leucine carboxyl methyltransferase 1"
FT /id="PRO_0000204422"
FT BINDING 37
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21206058,
FT ECO:0007744|PDB:3O7W"
FT BINDING 73
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21206058,
FT ECO:0007744|PDB:3O7W"
FT BINDING 98
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21206058,
FT ECO:0007744|PDB:3O7W"
FT BINDING 122
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21206058,
FT ECO:0007744|PDB:3O7W"
FT BINDING 171..172
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21206058,
FT ECO:0007744|PDB:3O7W"
FT BINDING 198
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:21206058,
FT ECO:0007744|PDB:3O7W"
FT VAR_SEQ 1..37
FT /note="MATRQRESSITSCCSTSSCDADDEGVRGTCEDASLCK -> MLPCARELPSA
FT APDSTLLLTAQHWVANLFILATLIGWTVRSFFLGRMETCCSHLGLRSGR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_017428"
FT VAR_SEQ 136..190
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_041416"
FT CONFLICT 49
FT /note="P -> S (in Ref. 4; BAD97084)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="L -> P (in Ref. 3; BAB15270)"
FT /evidence="ECO:0000305"
FT CONFLICT 248..249
FT /note="RQ -> PS (in Ref. 2; AAD34063)"
FT /evidence="ECO:0000305"
FT CONFLICT 251
FT /note="D -> E (in Ref. 1; AAF18267)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="F -> L (in Ref. 3; BAB15270)"
FT /evidence="ECO:0000305"
FT CONFLICT 306..307
FT /note="EL -> DV (in Ref. 1; AAF18267)"
FT /evidence="ECO:0000305"
FT CONFLICT 312..313
FT /note="MR -> NA (in Ref. 1; AAF18267)"
FT /evidence="ECO:0000305"
FT HELIX 28..43
FT /evidence="ECO:0007829|PDB:3IEI"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:3IEI"
FT HELIX 64..87
FT /evidence="ECO:0007829|PDB:3IEI"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:3IEI"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:3IEI"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:3IEI"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:3IEI"
FT HELIX 124..136
FT /evidence="ECO:0007829|PDB:3IEI"
FT HELIX 138..147
FT /evidence="ECO:0007829|PDB:3IEI"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:3IEI"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:3IEI"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:3IEI"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:3IEI"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:3IEI"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:3IEI"
FT HELIX 206..219
FT /evidence="ECO:0007829|PDB:3IEI"
FT STRAND 221..230
FT /evidence="ECO:0007829|PDB:3IEI"
FT HELIX 236..246
FT /evidence="ECO:0007829|PDB:3IEI"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:3IEI"
FT HELIX 255..259
FT /evidence="ECO:0007829|PDB:3IEI"
FT HELIX 261..269
FT /evidence="ECO:0007829|PDB:3IEI"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:3IEI"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:3IEI"
FT HELIX 281..286
FT /evidence="ECO:0007829|PDB:3IEI"
FT HELIX 290..299
FT /evidence="ECO:0007829|PDB:3IEI"
FT HELIX 305..312
FT /evidence="ECO:0007829|PDB:3IEI"
FT STRAND 315..323
FT /evidence="ECO:0007829|PDB:3IEI"
FT TURN 325..328
FT /evidence="ECO:0007829|PDB:3IEI"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:3IEI"
SQ SEQUENCE 334 AA; 38379 MW; C8D200118E6F353D CRC64;
MATRQRESSI TSCCSTSSCD ADDEGVRGTC EDASLCKRFA VSIGYWHDPY IQHFVRLSKE
RKAPEINRGY FARVHGVSQL IKAFLRKTEC HCQIVNLGAG MDTTFWRLKD EDLLPSKYFE
VDFPMIVTRK LHSIKCKPPL SSPILELHSE DTLQMDGHIL DSKRYAVIGA DLRDLSELEE
KLKKCNMNTQ LPTLLIAECV LVYMTPEQSA NLLKWAANSF ERAMFINYEQ VNMGDRFGQI
MIENLRRRQC DLAGVETCKS LESQKERLLS NGWETASAVD MMELYNRLPR AEVSRIESLE
FLDEMELLEQ LMRHYCLCWA TKGGNELGLK EITY
