ACOT4_HUMAN
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 03-AUG-2022, entry version 156.
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; Q8N9L9; -.
DR PeptideAtlas; Q8N9L9; -.
DR PRIDE; Q8N9L9; -.
DR ProteomicsDB; 72555; -.
DR Antibodypedia; 33; 86 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 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; EDLPNNM; -.
DR OrthoDB; 1260385at2759; -.
DR PhylomeDB; Q8N9L9; -.
DR TreeFam; TF314911; -.
DR BioCyc; MetaCyc:HS16863-MON; -.
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 UniPathway; UPA00094; -.
DR BioGRID-ORCS; 122970; 7 hits in 1059 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 116 other tissues.
DR Genevisible; Q8N9L9; HS.
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; -; 1.
DR Gene3D; 3.40.50.1820; -; 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 Pfam; PF08840; BAAT_C; 1.
DR Pfam; PF04775; Bile_Hydr_Trans; 1.
DR PIRSF; PIRSF016521; Acyl-CoA_hydro; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
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
