ID   ACO12_HUMAN             Reviewed;         555 AA.
AC   Q8WYK0; B3KVK9; Q5FWE9;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   24-JAN-2024, entry version 173.
DE   RecName: Full=Acetyl-coenzyme A thioesterase {ECO:0000305};
DE            EC=3.1.2.1 {ECO:0000269|PubMed:16951743};
DE   AltName: Full=Acyl-CoA thioester hydrolase 12;
DE   AltName: Full=Acyl-coenzyme A thioesterase 12;
DE            Short=Acyl-CoA thioesterase 12;
DE   AltName: Full=Cytoplasmic acetyl-CoA hydrolase 1;
DE            Short=CACH-1;
DE            Short=hCACH-1;
DE   AltName: Full=START domain-containing protein 15;
DE            Short=StARD15;
GN   Name=ACOT12; Synonyms=CACH, CACH1, STARD15;
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,
RP   ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Liver;
RX   PubMed=16951743;
RA   Suematsu N., Isohashi F.;
RT   "Molecular cloning and functional expression of human cytosolic acetyl-CoA
RT   hydrolase.";
RL   Acta Biochim. Pol. 53:553-561(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Chondrosarcoma;
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   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   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 7-316 IN COMPLEX WITH COENZYME A.
RG   Structural genomics consortium (SGC);
RT   "Human acyl-coenzyme A thioesterase 12.";
RL   Submitted (NOV-2007) to the PDB data bank.
RN   [8]
RP   VARIANT HIS-190.
RX   PubMed=21248752; DOI=10.1038/nature09639;
RA   Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA   Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA   Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA   Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA   Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA   Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA   Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA   Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT   "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT   PBRM1 in renal carcinoma.";
RL   Nature 469:539-542(2011).
CC   -!- FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids
CC       and coenzyme A (CoASH), regulating their respective intracellular
CC       levels (PubMed:16951743). Preferentially hydrolyzes acetyl-CoA
CC       (PubMed:16951743). {ECO:0000269|PubMed:16951743}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + H2O = acetate + CoA + H(+); Xref=Rhea:RHEA:20289,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=3.1.2.1;
CC         Evidence={ECO:0000269|PubMed:16951743};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20290;
CC         Evidence={ECO:0000305|PubMed:16951743};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=butanoyl-CoA + H2O = butanoate + CoA + H(+);
CC         Xref=Rhea:RHEA:40111, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17968, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371;
CC         Evidence={ECO:0000250|UniProtKB:Q99NB7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40112;
CC         Evidence={ECO:0000250|UniProtKB:Q99NB7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + hexanoyl-CoA = CoA + H(+) + hexanoate;
CC         Xref=Rhea:RHEA:40115, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17120, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620;
CC         Evidence={ECO:0000250|UniProtKB:Q99NB7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40116;
CC         Evidence={ECO:0000250|UniProtKB:Q99NB7};
CC   -!- ACTIVITY REGULATION: Inhibited by ADP. Active in the presence of ATP
CC       (PubMed:16951743). Cold labile, it dissociates into inactive monomers
CC       at low temperature (By similarity). {ECO:0000250|UniProtKB:Q99NB7,
CC       ECO:0000269|PubMed:16951743}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=150 uM for acetyl-CoA {ECO:0000269|PubMed:16951743};
CC         Note=kcat is 7000 sec(-1) for the hydrolysis of acetyl-CoA.
CC         {ECO:0000269|PubMed:16951743};
CC   -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC       {ECO:0000305|PubMed:16951743}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000250|UniProtKB:Q99NB7}.
CC   -!- INTERACTION:
CC       Q8WYK0; Q8WYK0: ACOT12; NbExp=3; IntAct=EBI-11954993, EBI-11954993;
CC       Q8WYK0; O00154-4: ACOT7; NbExp=3; IntAct=EBI-11954993, EBI-12007918;
CC       Q8WYK0; P50221: MEOX1; NbExp=3; IntAct=EBI-11954993, EBI-2864512;
CC       Q8WYK0; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11954993, EBI-16439278;
CC       Q8WYK0; P41227: NAA10; NbExp=3; IntAct=EBI-11954993, EBI-747693;
CC       Q8WYK0; Q9BSU3: NAA11; NbExp=3; IntAct=EBI-11954993, EBI-2585120;
CC       Q8WYK0; Q02548: PAX5; NbExp=3; IntAct=EBI-11954993, EBI-296331;
CC       Q8WYK0; P26367: PAX6; NbExp=3; IntAct=EBI-11954993, EBI-747278;
CC       Q8WYK0; Q04864-2: REL; NbExp=3; IntAct=EBI-11954993, EBI-10829018;
CC       Q8WYK0; Q96BR9: ZBTB8A; NbExp=4; IntAct=EBI-11954993, EBI-742740;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16951743}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8WYK0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8WYK0-2; Sequence=VSP_055785, VSP_055786;
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DR   EMBL; AB078619; BAB84022.1; -; mRNA.
DR   EMBL; AK122960; BAG53821.1; -; mRNA.
DR   EMBL; AC008411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC010623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471084; EAW95875.1; -; Genomic_DNA.
DR   EMBL; BC089437; AAH89437.1; -; mRNA.
DR   EMBL; BC075010; AAH75010.1; -; mRNA.
DR   EMBL; BC075011; AAH75011.1; -; mRNA.
DR   CCDS; CCDS4055.1; -. [Q8WYK0-1]
DR   RefSeq; NP_570123.1; NM_130767.2. [Q8WYK0-1]
DR   PDB; 3B7K; X-ray; 2.70 A; A/B/C=7-316.
DR   PDB; 4MOB; X-ray; 2.40 A; A=7-336.
DR   PDB; 4MOC; X-ray; 2.50 A; A=7-336.
DR   PDBsum; 3B7K; -.
DR   PDBsum; 4MOB; -.
DR   PDBsum; 4MOC; -.
DR   AlphaFoldDB; Q8WYK0; -.
DR   SMR; Q8WYK0; -.
DR   BioGRID; 126405; 15.
DR   IntAct; Q8WYK0; 14.
DR   STRING; 9606.ENSP00000303246; -.
DR   SwissLipids; SLP:000001187; -.
DR   TCDB; 9.B.371.2.1; the paai thioesterase (pte) family.
DR   iPTMnet; Q8WYK0; -.
DR   PhosphoSitePlus; Q8WYK0; -.
DR   BioMuta; ACOT12; -.
DR   DMDM; 25008183; -.
DR   jPOST; Q8WYK0; -.
DR   MassIVE; Q8WYK0; -.
DR   PaxDb; 9606-ENSP00000303246; -.
DR   PeptideAtlas; Q8WYK0; -.
DR   ProteomicsDB; 62810; -.
DR   ProteomicsDB; 75162; -. [Q8WYK0-1]
DR   Antibodypedia; 24697; 206 antibodies from 24 providers.
DR   DNASU; 134526; -.
DR   Ensembl; ENST00000307624.8; ENSP00000303246.3; ENSG00000172497.9. [Q8WYK0-1]
DR   Ensembl; ENST00000513751.1; ENSP00000421628.1; ENSG00000172497.9. [Q8WYK0-2]
DR   GeneID; 134526; -.
DR   KEGG; hsa:134526; -.
DR   MANE-Select; ENST00000307624.8; ENSP00000303246.3; NM_130767.3; NP_570123.1.
DR   UCSC; uc003khl.5; human. [Q8WYK0-1]
DR   AGR; HGNC:24436; -.
DR   CTD; 134526; -.
DR   DisGeNET; 134526; -.
DR   GeneCards; ACOT12; -.
DR   HGNC; HGNC:24436; ACOT12.
DR   HPA; ENSG00000172497; Tissue enriched (liver).
DR   MIM; 614315; gene.
DR   neXtProt; NX_Q8WYK0; -.
DR   OpenTargets; ENSG00000172497; -.
DR   PharmGKB; PA142672657; -.
DR   VEuPathDB; HostDB:ENSG00000172497; -.
DR   eggNOG; KOG2763; Eukaryota.
DR   GeneTree; ENSGT00940000160328; -.
DR   HOGENOM; CLU_035725_0_0_1; -.
DR   InParanoid; Q8WYK0; -.
DR   OMA; DPHYMSC; -.
DR   OrthoDB; 316366at2759; -.
DR   PhylomeDB; Q8WYK0; -.
DR   TreeFam; TF328368; -.
DR   BRENDA; 3.1.2.1; 2681.
DR   PathwayCommons; Q8WYK0; -.
DR   Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR   SignaLink; Q8WYK0; -.
DR   UniPathway; UPA00199; -.
DR   BioGRID-ORCS; 134526; 98 hits in 1142 CRISPR screens.
DR   ChiTaRS; ACOT12; human.
DR   EvolutionaryTrace; Q8WYK0; -.
DR   GeneWiki; ACOT12; -.
DR   GenomeRNAi; 134526; -.
DR   Pharos; Q8WYK0; Tbio.
DR   PRO; PR:Q8WYK0; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q8WYK0; Protein.
DR   Bgee; ENSG00000172497; Expressed in right lobe of liver and 67 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0003986; F:acetyl-CoA hydrolase activity; ISS:HGNC-UCL.
DR   GO; GO:0047617; F:acyl-CoA hydrolase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:Ensembl.
DR   GO; GO:0006637; P:acyl-CoA metabolic process; ISS:HGNC-UCL.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03442; BFIT_BACH; 2.
DR   CDD; cd08914; START_STARD15-like; 1.
DR   Gene3D; 3.30.530.20; -; 1.
DR   Gene3D; 3.10.129.10; Hotdog Thioesterase; 2.
DR   InterPro; IPR040170; Cytosol_ACT.
DR   InterPro; IPR033120; HOTDOG_ACOT.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR023393; START-like_dom_sf.
DR   InterPro; IPR002913; START_lipid-bd_dom.
DR   InterPro; IPR006683; Thioestr_dom.
DR   PANTHER; PTHR11049:SF3; ACETYL-COENZYME A THIOESTERASE; 1.
DR   PANTHER; PTHR11049; ACYL COENZYME A THIOESTER HYDROLASE; 1.
DR   Pfam; PF03061; 4HBT; 2.
DR   Pfam; PF01852; START; 1.
DR   SUPFAM; SSF55961; Bet v1-like; 1.
DR   SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
DR   PROSITE; PS51770; HOTDOG_ACOT; 2.
DR   PROSITE; PS50848; START; 1.
DR   Genevisible; Q8WYK0; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Fatty acid metabolism;
KW   Hydrolase; Lipid metabolism; Reference proteome; Repeat; Serine esterase.
FT   CHAIN           1..555
FT                   /note="Acetyl-coenzyme A thioesterase"
FT                   /id="PRO_0000053809"
FT   DOMAIN          5..117
FT                   /note="HotDog ACOT-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT   DOMAIN          179..294
FT                   /note="HotDog ACOT-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT   DOMAIN          340..549
FT                   /note="START"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT   BINDING         53..55
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT   BINDING         82..84
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT   BINDING         144
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000269|Ref.7"
FT   BINDING         234..236
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT   MOD_RES         33
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DBK0"
FT   MOD_RES         159
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DBK0"
FT   MOD_RES         228
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DBK0"
FT   VAR_SEQ         166..167
FT                   /note="DL -> GQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_055785"
FT   VAR_SEQ         168..555
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_055786"
FT   VARIANT         190
FT                   /note="L -> H (found in a clear cell renal carcinoma case;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:21248752"
FT                   /id="VAR_064691"
FT   VARIANT         230
FT                   /note="V -> I (in dbSNP:rs34607174)"
FT                   /id="VAR_048192"
FT   VARIANT         403
FT                   /note="A -> T (in dbSNP:rs10371)"
FT                   /id="VAR_048193"
FT   STRAND          9..14
FT                   /evidence="ECO:0007829|PDB:4MOB"
FT   HELIX           17..19
FT                   /evidence="ECO:0007829|PDB:4MOB"
FT   STRAND          24..26
FT                   /evidence="ECO:0007829|PDB:4MOB"
FT   HELIX           28..47
FT                   /evidence="ECO:0007829|PDB:4MOB"
FT   STRAND          51..56
FT                   /evidence="ECO:0007829|PDB:4MOB"
FT   STRAND          69..80
FT                   /evidence="ECO:0007829|PDB:4MOB"
FT   STRAND          82..95
FT                   /evidence="ECO:0007829|PDB:4MOB"
FT   TURN            96..98
FT                   /evidence="ECO:0007829|PDB:4MOB"
FT   STRAND          101..113
FT                   /evidence="ECO:0007829|PDB:4MOB"
FT   STRAND          116..118
FT                   /evidence="ECO:0007829|PDB:4MOB"
FT   HELIX           131..160
FT                   /evidence="ECO:0007829|PDB:4MOB"
FT   HELIX           171..173
FT                   /evidence="ECO:0007829|PDB:4MOB"
FT   HELIX           179..181
FT                   /evidence="ECO:0007829|PDB:4MOB"
FT   STRAND          183..188
FT                   /evidence="ECO:0007829|PDB:4MOB"
FT   HELIX           191..193
FT                   /evidence="ECO:0007829|PDB:4MOB"
FT   STRAND          198..200
FT                   /evidence="ECO:0007829|PDB:4MOB"
FT   HELIX           202..221
FT                   /evidence="ECO:0007829|PDB:4MOB"
FT   STRAND          222..230
FT                   /evidence="ECO:0007829|PDB:4MOB"
FT   STRAND          244..255
FT                   /evidence="ECO:0007829|PDB:4MOB"
FT   STRAND          258..268
FT                   /evidence="ECO:0007829|PDB:4MOB"
FT   HELIX           270..274
FT                   /evidence="ECO:0007829|PDB:4MOB"
FT   STRAND          279..291
FT                   /evidence="ECO:0007829|PDB:4MOB"
FT   STRAND          293..295
FT                   /evidence="ECO:0007829|PDB:4MOC"
FT   HELIX           308..325
FT                   /evidence="ECO:0007829|PDB:4MOB"
SQ   SEQUENCE   555 AA;  62034 MW;  707560D55504732C CRC64;
     MERPAPGEVV MSQAIQPAHA TARGELSAGQ LLKWIDTTAC LAAEKHAGVS CVTASVDDIQ
     FEETARVGQV ITIKAKVTRA FSTSMEISIK VMVQDMLTGI EKLVSVAFST FVAKPVGKEK
     IHLKPVTLLT EQDHVEHNLA AERRKVRLQH EDTFNNLMKE SSKFDDLIFD EEEGAVSTRG
     TSVQSIELVL PPHANHHGNT FGGQIMAWME TVATISASRL CWAHPFLKSV DMFKFRGPST
     VGDRLVFTAI VNNTFQTCVE VGVRVEAFDC QEWAEGRGRH INSAFLIYNA ADDKENLITF
     PRIQPISKDD FRRYRGAIAR KRIRLGRKYV ISHKEEVPLC IHWDISKQAS LSDSNVEALK
     KLAAKRGWEV TSTVEKIKIY TLEEHDVLSV WVEKHVGSPA HLAYRLLSDF TKRPLWDPHF
     VSCEVIDWVS EDDQLYHITC PILNDDKPKD LVVLVSRRKP LKDGNTYTVA VKSVILPSVP
     PSPQYIRSEI ICAGFLIHAI DSNSCIVSYF NHMSASILPY FAGNLGGWSK SIEETAASCI
     QFLENPPDDG FVSTF
//