ID   ACOT4_HUMAN             Reviewed;         421 AA.
AC   Q8N9L9; Q17RF4; Q5BKT6; Q86TX0; Q86TX1; Q96N88;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   24-JAN-2024, entry version 164.
DE   RecName: Full=Peroxisomal succinyl-coenzyme A thioesterase {ECO:0000305|PubMed:16940157};
DE            EC=3.1.2.3 {ECO:0000269|PubMed:16940157};
DE   AltName: Full=Acyl-coenzyme A thioesterase 4;
DE            Short=Acyl-CoA thioesterase 4;
DE            EC=3.1.2.2 {ECO:0000269|PubMed:16940157};
DE   AltName: Full=PTE-2b;
DE   AltName: Full=Peroxisomal acyl coenzyme A thioester hydrolase Ib;
DE   AltName: Full=Peroxisomal long-chain acyl-CoA thioesterase Ib;
DE            Short=PTE-Ib;
GN   Name=ACOT4; Synonyms=PTE2B, PTEIB;
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 [LARGE SCALE MRNA].
RC   TISSUE=Cerebellum, and Kidney;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neuroblastoma, and Placenta;
RA   Li W.B., Gruber C., Jessee J., Polayes D.;
RT   "Full-length cDNA libraries and normalization.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT CYS-57.
RC   TISSUE=Colon, and Urinary bladder;
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   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MISCELLANEOUS.
RX   PubMed=16940157; DOI=10.1096/fj.06-6042com;
RA   Hunt M.C., Rautanen A., Westin M.A.K., Svensson L.T., Alexson S.E.H.;
RT   "Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters
RT   shows that convergent, functional evolution results in a reduced number of
RT   human peroxisomal ACOTs.";
RL   FASEB J. 20:1855-1864(2006).
RN   [5]
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   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
RA   Siponen M.I., Moche M., Arrowsmith C.H., Berglund H., Bountra C.,
RA   Collins R., Edwards A.M., Flodin S., Flores A., Graslund S.,
RA   Hammarstrom M., Johansson A., Johansson I., Kallas A., Karlberg T.,
RA   Kraulis P., Kotenyova T., Kotzsch A., Markova N., Nielsen T.K.,
RA   Nordlund P., Nyman T., Persson C., Roos A.K., Schutz P., Svensson L.,
RA   Thorsell A.G., Tresaugues L., Van Den Berg S., Wahlberg E., Weigelt J.,
RA   Welin M., Wisniewska M., Schuler H.;
RT   "Human Acyl-coenzyme A thioesterase 4.";
RL   Submitted (SEP-2009) to the PDB data bank.
CC   -!- FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids
CC       and coenzyme A (CoASH), regulating their respective intracellular
CC       levels (PubMed:16940157). Functions as a peroxisomal succinyl-coenzyme
CC       A thioesterase that can also hydrolyze glutaryl-CoA and long chain
CC       saturated acyl-CoAs (PubMed:16940157). {ECO:0000269|PubMed:16940157}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + succinyl-CoA = CoA + H(+) + succinate;
CC         Xref=Rhea:RHEA:11516, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292; EC=3.1.2.3;
CC         Evidence={ECO:0000269|PubMed:16940157};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11517;
CC         Evidence={ECO:0000305|PubMed:16940157};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutaryl-CoA + H2O = CoA + glutarate + H(+);
CC         Xref=Rhea:RHEA:40575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30921, ChEBI:CHEBI:57287, ChEBI:CHEBI:57378;
CC         Evidence={ECO:0000269|PubMed:16940157};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40576;
CC         Evidence={ECO:0000305|PubMed:16940157};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
CC         Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2;
CC         Evidence={ECO:0000269|PubMed:16940157};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC         Evidence={ECO:0000305|PubMed:16940157};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+);
CC         Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387;
CC         Evidence={ECO:0000269|PubMed:16940157};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140;
CC         Evidence={ECO:0000305|PubMed:16940157};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoyl-CoA + H2O = (9Z,12Z)-octadecadienoate
CC         + CoA + H(+); Xref=Rhea:RHEA:40143, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57383; Evidence={ECO:0000269|PubMed:16940157};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40144;
CC         Evidence={ECO:0000305|PubMed:16940157};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = (5Z,8Z,11Z,14Z)-
CC         eicosatetraenoate + CoA + H(+); Xref=Rhea:RHEA:40151,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57368;
CC         Evidence={ECO:0000269|PubMed:16940157};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40152;
CC         Evidence={ECO:0000305|PubMed:16940157};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+);
CC         Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430;
CC         Evidence={ECO:0000269|PubMed:16940157};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060;
CC         Evidence={ECO:0000305|PubMed:16940157};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+);
CC         Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375;
CC         Evidence={ECO:0000269|PubMed:16940157};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC         Evidence={ECO:0000305|PubMed:16940157};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate;
CC         Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385;
CC         Evidence={ECO:0000269|PubMed:16940157};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC         Evidence={ECO:0000305|PubMed:16940157};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate;
CC         Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394;
CC         Evidence={ECO:0000269|PubMed:16940157};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
CC         Evidence={ECO:0000305|PubMed:16940157};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=eicosanoyl-CoA + H2O = CoA + eicosanoate + H(+);
CC         Xref=Rhea:RHEA:40147, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:32360, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380;
CC         Evidence={ECO:0000269|PubMed:16940157};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148;
CC         Evidence={ECO:0000305|PubMed:16940157};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=14 uM for succinyl-CoA {ECO:0000269|PubMed:16940157};
CC         KM=147 uM for glutaryl-CoA {ECO:0000269|PubMed:16940157};
CC         KM=3.4 uM for C14-acyl-CoA {ECO:0000269|PubMed:16940157};
CC         Vmax=581 nmol/min/mg enzyme with succinyl-CoA as substrate
CC         {ECO:0000269|PubMed:16940157};
CC         Vmax=132 nmol/min/mg enzyme with glutaryl-CoA as substrate
CC         {ECO:0000269|PubMed:16940157};
CC         Vmax=137 nmol/min/mg enzyme with C14-acyl-CoA as substrate
CC         {ECO:0000269|PubMed:16940157};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000305|PubMed:16940157}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:16940157}.
CC   -!- TISSUE SPECIFICITY: Strongest expression in liver and kidney and weaker
CC       expression in placenta, heart, and muscle.
CC       {ECO:0000269|PubMed:16940157}.
CC   -!- MISCELLANEOUS: Compared to mouse peroxisomal succinyl-coenzyme A
CC       thioesterase/ACOT4, the human enzyme has a broad substrate specificity
CC       overlapping the activity of three mouse acyl-coenzyme A thioesterases,
CC       providing an explanation for the unexpectedly low number of acyl-
CC       coenzyme A thioesterase genes in the human genome.
CC       {ECO:0000303|PubMed:16940157}.
CC   -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC       {ECO:0000305}.
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DR   EMBL; AK094223; BAC04313.1; -; mRNA.
DR   EMBL; AK055797; BAB71017.1; -; mRNA.
DR   EMBL; BX248023; CAD62346.1; -; mRNA.
DR   EMBL; BX248047; CAD62354.1; -; mRNA.
DR   EMBL; BC031799; AAH31799.2; -; mRNA.
DR   EMBL; BC090945; AAH90945.1; -; mRNA.
DR   EMBL; BC117341; AAI17342.1; -; mRNA.
DR   EMBL; BC117343; AAI17344.1; -; mRNA.
DR   CCDS; CCDS9817.1; -.
DR   RefSeq; NP_689544.3; NM_152331.3.
DR   PDB; 3K2I; X-ray; 2.40 A; A/B=1-421.
DR   PDBsum; 3K2I; -.
DR   AlphaFoldDB; Q8N9L9; -.
DR   SMR; Q8N9L9; -.
DR   BioGRID; 125809; 3.
DR   STRING; 9606.ENSP00000323071; -.
DR   SwissLipids; SLP:000000592; -.
DR   ESTHER; human-ACOT4; Acyl-CoA_Thioesterase.
DR   MEROPS; S09.943; -.
DR   iPTMnet; Q8N9L9; -.
DR   PhosphoSitePlus; Q8N9L9; -.
DR   BioMuta; ACOT4; -.
DR   DMDM; 50401071; -.
DR   EPD; Q8N9L9; -.
DR   jPOST; Q8N9L9; -.
DR   MassIVE; Q8N9L9; -.
DR   MaxQB; Q8N9L9; -.
DR   PaxDb; 9606-ENSP00000323071; -.
DR   PeptideAtlas; Q8N9L9; -.
DR   ProteomicsDB; 72555; -.
DR   Antibodypedia; 33; 101 antibodies from 22 providers.
DR   DNASU; 122970; -.
DR   Ensembl; ENST00000326303.5; ENSP00000323071.4; ENSG00000177465.5.
DR   GeneID; 122970; -.
DR   KEGG; hsa:122970; -.
DR   MANE-Select; ENST00000326303.5; ENSP00000323071.4; NM_152331.4; NP_689544.3.
DR   UCSC; uc001xoo.4; human.
DR   AGR; HGNC:19748; -.
DR   CTD; 122970; -.
DR   DisGeNET; 122970; -.
DR   GeneCards; ACOT4; -.
DR   HGNC; HGNC:19748; ACOT4.
DR   HPA; ENSG00000177465; Tissue enhanced (kidney, liver).
DR   MIM; 614314; gene.
DR   neXtProt; NX_Q8N9L9; -.
DR   OpenTargets; ENSG00000177465; -.
DR   PharmGKB; PA142672654; -.
DR   VEuPathDB; HostDB:ENSG00000177465; -.
DR   eggNOG; ENOG502QQ8Z; Eukaryota.
DR   GeneTree; ENSGT01010000222336; -.
DR   HOGENOM; CLU_029849_4_0_1; -.
DR   InParanoid; Q8N9L9; -.
DR   OMA; KHVIWGG; -.
DR   OrthoDB; 5356064at2759; -.
DR   PhylomeDB; Q8N9L9; -.
DR   TreeFam; TF314911; -.
DR   BioCyc; MetaCyc:HS16863-MONOMER; -.
DR   PathwayCommons; Q8N9L9; -.
DR   Reactome; R-HSA-390247; Beta-oxidation of very long chain fatty acids.
DR   Reactome; R-HSA-9033241; Peroxisomal protein import.
DR   SABIO-RK; Q8N9L9; -.
DR   SignaLink; Q8N9L9; -.
DR   SIGNOR; Q8N9L9; -.
DR   UniPathway; UPA00094; -.
DR   BioGRID-ORCS; 122970; 8 hits in 1145 CRISPR screens.
DR   ChiTaRS; ACOT4; human.
DR   EvolutionaryTrace; Q8N9L9; -.
DR   GeneWiki; ACOT4; -.
DR   GenomeRNAi; 122970; -.
DR   Pharos; Q8N9L9; Tbio.
DR   PRO; PR:Q8N9L9; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q8N9L9; Protein.
DR   Bgee; ENSG00000177465; Expressed in ileal mucosa and 117 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR   GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR   GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044466; F:glutaryl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004778; F:succinyl-CoA hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0006637; P:acyl-CoA metabolic process; IDA:HGNC-UCL.
DR   GO; GO:0043649; P:dicarboxylic acid catabolic process; IDA:UniProtKB.
DR   GO; GO:0043648; P:dicarboxylic acid metabolic process; IDA:HGNC-UCL.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR   GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:HGNC-UCL.
DR   GO; GO:0032788; P:saturated monocarboxylic acid metabolic process; IDA:HGNC-UCL.
DR   GO; GO:0046459; P:short-chain fatty acid metabolic process; IDA:HGNC-UCL.
DR   GO; GO:0006104; P:succinyl-CoA metabolic process; IDA:HGNC-UCL.
DR   GO; GO:0032789; P:unsaturated monocarboxylic acid metabolic process; IDA:HGNC-UCL.
DR   GO; GO:0000038; P:very long-chain fatty acid metabolic process; IDA:HGNC-UCL.
DR   Gene3D; 2.60.40.2240; Acyl-CoA thioester hydrolase/BAAT N-terminal domain; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR016662; Acyl-CoA_thioEstase_long-chain.
DR   InterPro; IPR014940; BAAT_C.
DR   InterPro; IPR006862; Thio_Ohase/aa_AcTrfase.
DR   InterPro; IPR042490; Thio_Ohase/BAAT_N.
DR   PANTHER; PTHR10824; ACYL-COENZYME A THIOESTERASE-RELATED; 1.
DR   PANTHER; PTHR10824:SF6; PEROXISOMAL SUCCINYL-COENZYME A THIOESTERASE; 1.
DR   Pfam; PF08840; BAAT_C; 1.
DR   Pfam; PF04775; Bile_Hydr_Trans; 1.
DR   PIRSF; PIRSF016521; Acyl-CoA_hydro; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   Genevisible; Q8N9L9; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Fatty acid metabolism; Hydrolase; Lipid metabolism;
KW   Peroxisome; Reference proteome; Serine esterase.
FT   CHAIN           1..421
FT                   /note="Peroxisomal succinyl-coenzyme A thioesterase"
FT                   /id="PRO_0000202149"
FT   MOTIF           419..421
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        232
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P49753"
FT   ACT_SITE        326
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P49753"
FT   ACT_SITE        360
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:P49753"
FT   MOD_RES         313
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWN8"
FT   VARIANT         57
FT                   /note="R -> C (in dbSNP:rs3742819)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_052300"
FT   VARIANT         187
FT                   /note="A -> D (in dbSNP:rs35724886)"
FT                   /id="VAR_052301"
FT   CONFLICT        130
FT                   /note="L -> P (in Ref. 1; BAC04313)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        187..190
FT                   /note="ALAY -> DLQS (in Ref. 1; BAC04313)"
FT                   /evidence="ECO:0000305"
FT   STRAND          4..8
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   STRAND          20..25
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   STRAND          31..39
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   STRAND          45..53
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   TURN            62..64
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   STRAND          69..72
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   HELIX           79..82
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   STRAND          85..88
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   STRAND          102..112
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   STRAND          119..130
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   STRAND          135..141
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   STRAND          144..150
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   STRAND          152..154
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   STRAND          159..163
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   HELIX           173..179
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   TURN            180..182
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   STRAND          184..189
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   STRAND          191..193
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   HELIX           206..216
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   STRAND          224..231
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   HELIX           233..244
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   STRAND          246..255
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   STRAND          265..267
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   STRAND          270..272
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   HELIX           279..281
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   HELIX           302..304
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   HELIX           311..313
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   STRAND          318..323
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   STRAND          327..329
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   HELIX           331..344
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   STRAND          351..355
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   STRAND          372..375
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   TURN            376..379
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   STRAND          380..383
FT                   /evidence="ECO:0007829|PDB:3K2I"
FT   HELIX           388..409
FT                   /evidence="ECO:0007829|PDB:3K2I"
SQ   SEQUENCE   421 AA;  46327 MW;  41BBE5AA826A9F2C CRC64;
     MSATLILEPP GRCCWNEPVR IAVRGLAPEQ RVTLRASLRD EKGALFRAHA RYCADARGEL
     DLERAPALGG SFAGLEPMGL LWALEPEKPF WRFLKRDVQI PFVVELEVLD GHDPEPGRLL
     CQAQHERHFL PPGVRRQSVR AGRVRATLFL PPGPGPFPGI IDIFGIGGGL LEYRASLLAG
     HGFATLALAY YNFEDLPNNM DNISLEYFEE AVCYMLQHPQ VKGPGIGLLG ISLGADICLS
     MASFLKNVSA TVSINGSGIS GNTAINYKHS SIPPLGYDLR RIKVAFSGLV DIVDIRNALV
     GGYKNPSMIP IEKAQGPILL IVGQDDHNWR SELYAQTVSE RLQAHGKEKP QIICYPGTGH
     YIEPPYFPLC PASLHRLLNK HVIWGGEPRA HSKAQEDAWK QILAFFCKHL GGTQKTAVPK
     L
//