CISY_HUMAN
ID CISY_HUMAN Reviewed; 466 AA.
AC O75390; Q71UT9; Q7KZH0; Q96FZ8; Q9BWN8;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Citrate synthase, mitochondrial;
DE EC=2.3.3.1;
DE AltName: Full=Citrate (Si)-synthase;
DE Flags: Precursor;
GN Name=CS;
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].
RC TISSUE=Heart;
RX PubMed=9809442; DOI=10.1139/g98-074;
RA Goldenthal M.J., Marin-Garcia J., Ananthakrishnan R.;
RT "Cloning and molecular analysis of the human citrate synthase gene.";
RL Genome 41:733-738(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12549038;
RA Liu Q., Yu L., Han X.F., Fu Q., Zhang J.X., Tang H., Zhao S.Y.;
RT "Cloning and tissue expression pattern analysis of the human citrate
RT synthase cDNA.";
RL Shi Yan Sheng Wu Xue Bao 33:207-214(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
RC TISSUE=Rectum tumor;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lymph, and Prostate;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 203-466.
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 [7]
RP PROTEIN SEQUENCE OF 77-92 AND 383-393.
RC TISSUE=Adipocyte;
RX PubMed=15242332; DOI=10.1042/bj20040647;
RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
RT "Vectorial proteomics reveal targeting, phosphorylation and specific
RT fragmentation of polymerase I and transcript release factor (PTRF) at the
RT surface of caveolae in human adipocytes.";
RL Biochem. J. 383:237-248(2004).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-327; LYS-375; LYS-382 AND
RP LYS-393, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
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].
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 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 [12]
RP METHYLATION AT LYS-395 BY CSKMT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28391595; DOI=10.1002/1873-3468.12649;
RA Rhein V.F., Carroll J., Ding S., Fearnley I.M., Walker J.E.;
RT "Human METTL12 is a mitochondrial methyltransferase that modifies citrate
RT synthase.";
RL FEBS Lett. 591:1641-1652(2017).
RN [13]
RP METHYLATION AT LYS-395 BY CSKMT, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP MUTAGENESIS OF LYS-393 AND LYS-395.
RX PubMed=28887308; DOI=10.1074/jbc.m117.808451;
RA Malecki J., Jakobsson M.E., Ho A.Y.Y., Moen A., Rustan A.C., Falnes P.O.;
RT "Uncovering human METTL12 as a mitochondrial methyltransferase that
RT modulates citrate synthase activity through metabolite-sensitive lysine
RT methylation.";
RL J. Biol. Chem. 292:17950-17962(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+);
CC Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.3.1; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10117};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 1/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- PTM: Methylated (PubMed:28391595, PubMed:28887308). Trimethylation at
CC Lys-395 by CSKMT decreases citrate synthase activity (PubMed:28887308).
CC {ECO:0000269|PubMed:28391595, ECO:0000269|PubMed:28887308}.
CC -!- MISCELLANEOUS: Citrate synthase is found in nearly all cells capable of
CC oxidative metabolism.
CC -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE45911.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Citrate synthase entry;
CC URL="https://en.wikipedia.org/wiki/Citrate_synthase";
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DR EMBL; AF047042; AAC25560.1; -; mRNA.
DR EMBL; AF053631; AAQ13428.1; -; mRNA.
DR EMBL; AK074956; BAC11314.1; -; mRNA.
DR EMBL; BX640838; CAE45911.1; ALT_SEQ; mRNA.
DR EMBL; BC000105; AAH00105.3; -; mRNA.
DR EMBL; BC010106; AAH10106.1; -; mRNA.
DR EMBL; BC072016; AAH72016.1; -; mRNA.
DR EMBL; BT007414; AAP36082.1; -; mRNA.
DR CCDS; CCDS8913.1; -.
DR RefSeq; NP_004068.2; NM_004077.2.
DR PDB; 5UZP; X-ray; 2.29 A; A/B=28-466.
DR PDB; 5UZQ; X-ray; 2.16 A; A=28-466.
DR PDB; 5UZR; X-ray; 2.30 A; A/D=28-466.
DR PDBsum; 5UZP; -.
DR PDBsum; 5UZQ; -.
DR PDBsum; 5UZR; -.
DR AlphaFoldDB; O75390; -.
DR SASBDB; O75390; -.
DR SMR; O75390; -.
DR BioGRID; 107818; 428.
DR CORUM; O75390; -.
DR IntAct; O75390; 28.
DR MINT; O75390; -.
DR STRING; 9606.ENSP00000342056; -.
DR ChEMBL; CHEMBL4295678; -.
DR DrugBank; DB03182; alpha-Fluoro-carboxymethyldethia coenzyme A complex.
DR DrugBank; DB04272; Citric acid.
DR DrugBank; DB01992; Coenzyme A.
DR DrugBank; DB03499; D-Malic acid.
DR DrugBank; DB04230; Nitromethyldethia coenzyme A.
DR DrugBank; DB02637; Oxaloacetate Ion.
DR DrugBank; DB01969; Trifluoroacetonyl coenzyme A.
DR CarbonylDB; O75390; -.
DR GlyGen; O75390; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75390; -.
DR PhosphoSitePlus; O75390; -.
DR SwissPalm; O75390; -.
DR BioMuta; CS; -.
DR EPD; O75390; -.
DR jPOST; O75390; -.
DR MassIVE; O75390; -.
DR MaxQB; O75390; -.
DR PaxDb; O75390; -.
DR PeptideAtlas; O75390; -.
DR PRIDE; O75390; -.
DR ProteomicsDB; 49963; -.
DR TopDownProteomics; O75390; -.
DR Antibodypedia; 28123; 417 antibodies from 35 providers.
DR DNASU; 1431; -.
DR Ensembl; ENST00000351328.8; ENSP00000342056.3; ENSG00000062485.19.
DR GeneID; 1431; -.
DR KEGG; hsa:1431; -.
DR MANE-Select; ENST00000351328.8; ENSP00000342056.3; NM_004077.3; NP_004068.2.
DR UCSC; uc001skr.2; human.
DR CTD; 1431; -.
DR DisGeNET; 1431; -.
DR GeneCards; CS; -.
DR HGNC; HGNC:2422; CS.
DR HPA; ENSG00000062485; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 118950; gene.
DR neXtProt; NX_O75390; -.
DR OpenTargets; ENSG00000062485; -.
DR PharmGKB; PA26928; -.
DR VEuPathDB; HostDB:ENSG00000062485; -.
DR eggNOG; KOG2617; Eukaryota.
DR GeneTree; ENSGT00390000006813; -.
DR InParanoid; O75390; -.
DR OMA; TVGWCAQ; -.
DR OrthoDB; 1131452at2759; -.
DR PhylomeDB; O75390; -.
DR TreeFam; TF300398; -.
DR BioCyc; MetaCyc:ENSG00000062485-MON; -.
DR BRENDA; 2.3.3.1; 2681.
DR BRENDA; 2.3.3.16; 2681.
DR PathwayCommons; O75390; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR Reactome; R-HSA-71403; Citric acid cycle (TCA cycle).
DR SignaLink; O75390; -.
DR SIGNOR; O75390; -.
DR UniPathway; UPA00223; UER00717.
DR BioGRID-ORCS; 1431; 176 hits in 1092 CRISPR screens.
DR ChiTaRS; CS; human.
DR GenomeRNAi; 1431; -.
DR Pharos; O75390; Tbio.
DR PRO; PR:O75390; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O75390; protein.
DR Bgee; ENSG00000062485; Expressed in left ventricle myocardium and 211 other tissues.
DR ExpressionAtlas; O75390; baseline and differential.
DR Genevisible; O75390; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0004108; F:citrate (Si)-synthase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR GO; GO:0006101; P:citrate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 1.10.230.10; -; 1.
DR Gene3D; 1.10.580.10; -; 1.
DR InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
DR InterPro; IPR002020; Citrate_synthase.
DR InterPro; IPR019810; Citrate_synthase_AS.
DR InterPro; IPR010109; Citrate_synthase_euk.
DR InterPro; IPR036969; Citrate_synthase_sf.
DR PANTHER; PTHR11739; PTHR11739; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR PRINTS; PR00143; CITRTSNTHASE.
DR SUPFAM; SSF48256; SSF48256; 1.
DR TIGRFAMs; TIGR01793; cit_synth_euk; 1.
DR PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Methylation;
KW Mitochondrion; Reference proteome; Transferase; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT CHAIN 28..466
FT /note="Citrate synthase, mitochondrial"
FT /id="PRO_0000005471"
FT ACT_SITE 301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 347
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT MOD_RES 57
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 76
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q29RK1"
FT MOD_RES 76
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q29RK1"
FT MOD_RES 103
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 193
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 321
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 321
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 327
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 327
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 375
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 375
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 382
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 393
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 393
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 395
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:28391595,
FT ECO:0000269|PubMed:28887308"
FT MOD_RES 450
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 459
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 459
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MUTAGEN 393
FT /note="K->R: Does not inhibit methylation."
FT /evidence="ECO:0000269|PubMed:28887308"
FT MUTAGEN 395
FT /note="K->R: Inhibits methylation."
FT /evidence="ECO:0000269|PubMed:28887308"
FT CONFLICT 55
FT /note="H -> R (in Ref. 4; CAE45911)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="H -> C (in Ref. 1; AAC25560)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="R -> Q (in Ref. 1; AAC25560)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="Q -> R (in Ref. 1; AAC25560)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="M -> V (in Ref. 1; AAC25560)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="R -> W (in Ref. 1; AAC25560)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="T -> M (in Ref. 1; AAC25560)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="L -> F (in Ref. 2; AAQ13428)"
FT /evidence="ECO:0000305"
FT HELIX 33..55
FT /evidence="ECO:0007829|PDB:5UZQ"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:5UZP"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:5UZQ"
FT TURN 70..74
FT /evidence="ECO:0007829|PDB:5UZQ"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:5UZP"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:5UZQ"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:5UZQ"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:5UZQ"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:5UZQ"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:5UZQ"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:5UZQ"
FT HELIX 149..157
FT /evidence="ECO:0007829|PDB:5UZQ"
FT HELIX 164..174
FT /evidence="ECO:0007829|PDB:5UZQ"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:5UZQ"
FT HELIX 180..187
FT /evidence="ECO:0007829|PDB:5UZQ"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:5UZQ"
FT HELIX 194..221
FT /evidence="ECO:0007829|PDB:5UZQ"
FT HELIX 236..244
FT /evidence="ECO:0007829|PDB:5UZQ"
FT HELIX 249..261
FT /evidence="ECO:0007829|PDB:5UZQ"
FT HELIX 270..279
FT /evidence="ECO:0007829|PDB:5UZQ"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:5UZQ"
FT HELIX 285..296
FT /evidence="ECO:0007829|PDB:5UZQ"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:5UZQ"
FT HELIX 304..319
FT /evidence="ECO:0007829|PDB:5UZQ"
FT HELIX 325..337
FT /evidence="ECO:0007829|PDB:5UZQ"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:5UZQ"
FT HELIX 355..367
FT /evidence="ECO:0007829|PDB:5UZQ"
FT HELIX 372..391
FT /evidence="ECO:0007829|PDB:5UZQ"
FT STRAND 394..399
FT /evidence="ECO:0007829|PDB:5UZQ"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:5UZQ"
FT HELIX 405..411
FT /evidence="ECO:0007829|PDB:5UZQ"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:5UZQ"
FT HELIX 420..441
FT /evidence="ECO:0007829|PDB:5UZQ"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:5UZP"
FT HELIX 454..462
FT /evidence="ECO:0007829|PDB:5UZQ"
SQ SEQUENCE 466 AA; 51712 MW; 459CB29C0BA06997 CRC64;
MALLTAAARL LGTKNASCLV LAARHASASS TNLKDILADL IPKEQARIKT FRQQHGKTVV
GQITVDMMYG GMRGMKGLVY ETSVLDPDEG IRFRGFSIPE CQKLLPKAKG GEEPLPEGLF
WLLVTGHIPT EEQVSWLSKE WAKRAALPSH VVTMLDNFPT NLHPMSQLSA AVTALNSESN
FARAYAQGIS RTKYWELIYE DSMDLIAKLP CVAAKIYRNL YREGSGIGAI DSNLDWSHNF
TNMLGYTDHQ FTELTRLYLT IHSDHEGGNV SAHTSHLVGS ALSDPYLSFA AAMNGLAGPL
HGLANQEVLV WLTQLQKEVG KDVSDEKLRD YIWNTLNSGR VVPGYGHAVL RKTDPRYTCQ
REFALKHLPN DPMFKLVAQL YKIVPNVLLE QGKAKNPWPN VDAHSGVLLQ YYGMTEMNYY
TVLFGVSRAL GVLAQLIWSR ALGFPLERPK SMSTEGLMKF VDSKSG
