ID   ACO11_HUMAN             Reviewed;         607 AA.
AC   Q8WXI4; B1AQ22; D3DQ50; O75187; Q52LP1; Q53ER9; Q96DI1; Q9H883;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   24-JAN-2024, entry version 190.
DE   RecName: Full=Acyl-coenzyme A thioesterase 11 {ECO:0000305|PubMed:22897136};
DE            Short=Acyl-CoA thioesterase 11 {ECO:0000305|PubMed:22897136};
DE            EC=3.1.2.- {ECO:0000269|PubMed:22897136};
DE   AltName: Full=Acyl-CoA thioester hydrolase 11;
DE   AltName: Full=Adipose-associated thioesterase;
DE   AltName: Full=Brown fat-inducible thioesterase;
DE            Short=BFIT;
DE   AltName: Full=Palmitoyl-coenzyme A thioesterase {ECO:0000305|PubMed:22897136};
DE            EC=3.1.2.2 {ECO:0000269|PubMed:22897136};
DE   Flags: Precursor;
GN   Name=ACOT11; Synonyms=BFIT, KIAA0707, THEA;
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] (ISOFORMS 1 AND 2).
RX   PubMed=11696000; DOI=10.1042/bj3600135;
RA   Adams S.H., Chui C., Schilbach S.L., Yu X.X., Goddard A.D., Grimaldi J.C.,
RA   Lee J., Dowd P., Colman S., Lewin D.A.;
RT   "BFIT, a unique acyl-CoA thioesterase induced in thermogenic brown adipose
RT   tissue: cloning, organization of the human gene and assessment of a
RT   potential link to obesity.";
RL   Biochem. J. 360:135-142(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA   Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA   Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. X. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 5:169-176(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Thyroid;
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), AND VARIANT ASP-202.
RC   TISSUE=Heart;
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=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain, and Skin;
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   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, PATHWAY, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=22897136; DOI=10.1021/bi3008824;
RA   Chen D., Latham J., Zhao H., Bisoffi M., Farelli J., Dunaway-Mariano D.;
RT   "Human brown fat inducible thioesterase variant 2 cellular localization and
RT   catalytic function.";
RL   Biochemistry 51:6990-6999(2012).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 339-543.
RX   PubMed=21738568; DOI=10.1371/journal.pone.0019521;
RA   Thorsell A.G., Lee W.H., Persson C., Siponen M.I., Nilsson M., Busam R.D.,
RA   Kotenyova T., Schuler H., Lehtio L.;
RT   "Comparative structural analysis of lipid binding START domains.";
RL   PLoS ONE 6:E19521-E19521(2011).
CC   -!- FUNCTION: Has an acyl-CoA thioesterase activity with a preference for
CC       the long chain fatty acyl-CoA thioesters hexadecanoyl-CoA/palmitoyl-CoA
CC       and tetradecanoyl-CoA/myristoyl-CoA which are the main substrates in
CC       the mitochondrial beta-oxidation pathway.
CC       {ECO:0000269|PubMed:22897136}.
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:22897136};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC         Evidence={ECO:0000305|PubMed:22897136};
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:22897136};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC         Evidence={ECO:0000305|PubMed:22897136};
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:22897136};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC         Evidence={ECO:0000305|PubMed:22897136};
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:0000269|PubMed:22897136};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40112;
CC         Evidence={ECO:0000305|PubMed:22897136};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Note=kcat is 5 min(-1) for the hydrolysis of hexadecanoyl-CoA
CC         (PubMed:22897136). kcat is 3.5 min(-1) for the hydrolysis of
CC         tetradecanoyl-CoA (PubMed:22897136). kcat is 2.3 min(-1) for the
CC         hydrolysis of dodecanoyl-CoA (PubMed:22897136). kcat is 0.2 min(-1)
CC         for the hydrolysis of butanoyl-CoA (PubMed:22897136).
CC         {ECO:0000269|PubMed:22897136};
CC   -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC       {ECO:0000305|PubMed:22897136}.
CC   -!- INTERACTION:
CC       Q8WXI4-2; Q53TS8: C2CD6; NbExp=3; IntAct=EBI-17721098, EBI-739879;
CC       Q8WXI4-2; Q9NP86: CABP5; NbExp=3; IntAct=EBI-17721098, EBI-10311131;
CC       Q8WXI4-2; Q9NQT4: EXOSC5; NbExp=3; IntAct=EBI-17721098, EBI-371876;
CC       Q8WXI4-2; Q8WXD5: GEMIN6; NbExp=3; IntAct=EBI-17721098, EBI-752301;
CC       Q8WXI4-2; Q8WUI4-6: HDAC7; NbExp=3; IntAct=EBI-17721098, EBI-12094670;
CC       Q8WXI4-2; O14964: HGS; NbExp=3; IntAct=EBI-17721098, EBI-740220;
CC       Q8WXI4-2; O15481: MAGEB4; NbExp=3; IntAct=EBI-17721098, EBI-751857;
CC       Q8WXI4-2; Q13064: MKRN3; NbExp=3; IntAct=EBI-17721098, EBI-2340269;
CC       Q8WXI4-2; P51687: SUOX; NbExp=3; IntAct=EBI-17721098, EBI-3921347;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000269|PubMed:22897136}. Cytoplasm {ECO:0000269|PubMed:22897136}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=BFIT1;
CC         IsoId=Q8WXI4-1; Sequence=Displayed;
CC       Name=2; Synonyms=BFIT2;
CC         IsoId=Q8WXI4-2; Sequence=VSP_000160;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is predominantly expressed in skeletal
CC       muscle, liver, testis, stomach, spleen, lung and brain. Isoform 2 is
CC       predominantly expressed in kidney, uterus, hibernoma and white adipose
CC       tissue.
CC   -!- INDUCTION: By cold exposure and repressed by heat exposure.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA31682.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF416921; AAL40937.1; -; mRNA.
DR   EMBL; AF416922; AAL40938.1; -; mRNA.
DR   EMBL; AB014607; BAA31682.1; ALT_INIT; mRNA.
DR   EMBL; AK023937; BAB14734.1; -; mRNA.
DR   EMBL; AK223570; BAD97290.1; -; mRNA.
DR   EMBL; AC099796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL590093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471059; EAX06682.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX06683.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX06684.1; -; Genomic_DNA.
DR   EMBL; BC001517; AAH01517.1; -; mRNA.
DR   EMBL; BC093844; AAH93844.1; -; mRNA.
DR   EMBL; BC093846; AAH93846.1; -; mRNA.
DR   CCDS; CCDS592.1; -. [Q8WXI4-1]
DR   CCDS; CCDS593.1; -. [Q8WXI4-2]
DR   PIR; T00351; T00351.
DR   RefSeq; NP_056362.1; NM_015547.3. [Q8WXI4-1]
DR   RefSeq; NP_671517.1; NM_147161.3. [Q8WXI4-2]
DR   PDB; 3FO5; X-ray; 2.00 A; A/B=339-543.
DR   PDB; 6VVQ; X-ray; 3.09 A; A/B/C/D=339-543.
DR   PDBsum; 3FO5; -.
DR   PDBsum; 6VVQ; -.
DR   AlphaFoldDB; Q8WXI4; -.
DR   SMR; Q8WXI4; -.
DR   BioGRID; 117495; 24.
DR   IntAct; Q8WXI4; 14.
DR   STRING; 9606.ENSP00000360366; -.
DR   SwissLipids; SLP:000001186; -. [Q8WXI4-2]
DR   GlyGen; Q8WXI4; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8WXI4; -.
DR   PhosphoSitePlus; Q8WXI4; -.
DR   SwissPalm; Q8WXI4; -.
DR   BioMuta; ACOT11; -.
DR   DMDM; 21363000; -.
DR   EPD; Q8WXI4; -.
DR   jPOST; Q8WXI4; -.
DR   MassIVE; Q8WXI4; -.
DR   MaxQB; Q8WXI4; -.
DR   PaxDb; 9606-ENSP00000360366; -.
DR   PeptideAtlas; Q8WXI4; -.
DR   ProteomicsDB; 75066; -. [Q8WXI4-1]
DR   ProteomicsDB; 75067; -. [Q8WXI4-2]
DR   Pumba; Q8WXI4; -.
DR   Antibodypedia; 33192; 267 antibodies from 30 providers.
DR   DNASU; 26027; -.
DR   Ensembl; ENST00000343744.7; ENSP00000340260.2; ENSG00000162390.18. [Q8WXI4-2]
DR   Ensembl; ENST00000371316.3; ENSP00000360366.3; ENSG00000162390.18. [Q8WXI4-1]
DR   GeneID; 26027; -.
DR   KEGG; hsa:26027; -.
DR   MANE-Select; ENST00000343744.7; ENSP00000340260.2; NM_147161.4; NP_671517.1. [Q8WXI4-2]
DR   UCSC; uc001cxl.3; human. [Q8WXI4-1]
DR   AGR; HGNC:18156; -.
DR   CTD; 26027; -.
DR   DisGeNET; 26027; -.
DR   GeneCards; ACOT11; -.
DR   HGNC; HGNC:18156; ACOT11.
DR   HPA; ENSG00000162390; Tissue enhanced (intestine).
DR   MIM; 606803; gene.
DR   neXtProt; NX_Q8WXI4; -.
DR   OpenTargets; ENSG00000162390; -.
DR   PharmGKB; PA38303; -.
DR   VEuPathDB; HostDB:ENSG00000162390; -.
DR   eggNOG; KOG2763; Eukaryota.
DR   GeneTree; ENSGT00940000156460; -.
DR   HOGENOM; CLU_035725_0_0_1; -.
DR   InParanoid; Q8WXI4; -.
DR   OMA; YEQCEVI; -.
DR   OrthoDB; 316366at2759; -.
DR   PhylomeDB; Q8WXI4; -.
DR   TreeFam; TF328368; -.
DR   PathwayCommons; Q8WXI4; -.
DR   Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR   SignaLink; Q8WXI4; -.
DR   UniPathway; UPA00199; -.
DR   BioGRID-ORCS; 26027; 13 hits in 1153 CRISPR screens.
DR   ChiTaRS; ACOT11; human.
DR   EvolutionaryTrace; Q8WXI4; -.
DR   GeneWiki; ACOT11; -.
DR   GenomeRNAi; 26027; -.
DR   Pharos; Q8WXI4; Tbio.
DR   PRO; PR:Q8WXI4; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q8WXI4; Protein.
DR   Bgee; ENSG00000162390; Expressed in apex of heart and 181 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; 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:0008289; F:lipid binding; IEA:InterPro.
DR   GO; GO:0052816; F:long-chain acyl-CoA hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR   GO; GO:0006631; P:fatty acid metabolic process; NAS:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
DR   GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   GO; GO:0009409; P:response to cold; ISS:BHF-UCL.
DR   GO; GO:0009266; P:response to temperature stimulus; ISS:UniProtKB.
DR   CDD; cd03442; BFIT_BACH; 2.
DR   CDD; cd08913; START_STARD14-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; ACYL COENZYME A THIOESTER HYDROLASE; 1.
DR   PANTHER; PTHR11049:SF1; ACYL-COENZYME A THIOESTERASE 11; 1.
DR   Pfam; PF03061; 4HBT; 2.
DR   Pfam; PF01852; START; 1.
DR   SMART; SM00234; 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; Q8WXI4; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Fatty acid metabolism;
KW   Hydrolase; Lipid metabolism; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Repeat; Serine esterase; Transit peptide.
FT   TRANSIT         1..13
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           14..607
FT                   /note="Acyl-coenzyme A thioesterase 11"
FT                   /id="PRO_0000053813"
FT   DOMAIN          43..155
FT                   /note="HotDog ACOT-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT   DOMAIN          216..329
FT                   /note="HotDog ACOT-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01106"
FT   DOMAIN          375..585
FT                   /note="START"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00197"
FT   BINDING         91..93
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         120..122
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         271..273
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VHQ9"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VHQ9"
FT   VAR_SEQ         544..607
FT                   /note="CCWVRVSLTELVSASGFYSWGLESRSKGRRSDGWNGKLAGGHLSTLKAIPVA
FT                   KINSRFGYLQDT -> VSYYNQATPGVLNYVTTNVAGLSSEFYTTFKACEQFLLDNRND
FT                   LAPSLQTL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11696000,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|Ref.4"
FT                   /id="VSP_000160"
FT   VARIANT         11
FT                   /note="R -> W (in dbSNP:rs34630746)"
FT                   /id="VAR_048190"
FT   VARIANT         165
FT                   /note="P -> L (in dbSNP:rs2304306)"
FT                   /id="VAR_022119"
FT   VARIANT         202
FT                   /note="G -> D (in dbSNP:rs1702003)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_022120"
FT   VARIANT         212
FT                   /note="M -> I (in dbSNP:rs2304305)"
FT                   /id="VAR_022121"
FT   VARIANT         536
FT                   /note="R -> H (in dbSNP:rs12403630)"
FT                   /id="VAR_048191"
FT   CONFLICT        255
FT                   /note="S -> R (in Ref. 7; AAH01517)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        348
FT                   /note="R -> W (in Ref. 4; BAD97290)"
FT                   /evidence="ECO:0000305"
FT   HELIX           347..363
FT                   /evidence="ECO:0007829|PDB:3FO5"
FT   TURN            370..372
FT                   /evidence="ECO:0007829|PDB:3FO5"
FT   STRAND          375..378
FT                   /evidence="ECO:0007829|PDB:3FO5"
FT   HELIX           381..383
FT                   /evidence="ECO:0007829|PDB:3FO5"
FT   HELIX           384..399
FT                   /evidence="ECO:0007829|PDB:3FO5"
FT   STRAND          405..410
FT                   /evidence="ECO:0007829|PDB:3FO5"
FT   STRAND          413..419
FT                   /evidence="ECO:0007829|PDB:3FO5"
FT   STRAND          424..434
FT                   /evidence="ECO:0007829|PDB:3FO5"
FT   HELIX           436..444
FT                   /evidence="ECO:0007829|PDB:3FO5"
FT   HELIX           446..451
FT                   /evidence="ECO:0007829|PDB:3FO5"
FT   STRAND          458..466
FT                   /evidence="ECO:0007829|PDB:3FO5"
FT   STRAND          469..476
FT                   /evidence="ECO:0007829|PDB:3FO5"
FT   STRAND          486..495
FT                   /evidence="ECO:0007829|PDB:3FO5"
FT   STRAND          504..512
FT                   /evidence="ECO:0007829|PDB:3FO5"
FT   STRAND          514..516
FT                   /evidence="ECO:0007829|PDB:6VVQ"
FT   STRAND          522..524
FT                   /evidence="ECO:0007829|PDB:3FO5"
FT   STRAND          528..538
FT                   /evidence="ECO:0007829|PDB:3FO5"
FT   STRAND          541..543
FT                   /evidence="ECO:0007829|PDB:3FO5"
SQ   SEQUENCE   607 AA;  68492 MW;  12F2BCAB8AAC18EC CRC64;
     MIQNVGNHLR RGLASVFSNR TSRKSALRAG NDSAMADGEG YRNPTEVQMS QLVLPCHTNQ
     RGELSVGQLL KWIDTTACLS AERHAGCPCV TASMDDIYFE HTISVGQVVN IKAKVNRAFN
     SSMEVGIQVA SEDLCSEKQW NVCKALATFV ARREITKVKL KQITPRTEEE KMEHSVAAER
     RRMRLVYADT IKDLLANCAI QGDLESRDCS RMVPAEKTRV ESVELVLPPH ANHQGNTFGG
     QIMAWMENVA TIAASRLCRA HPTLKAIEMF HFRGPSQVGD RLVLKAIVNN AFKHSMEVGV
     CVEAYRQEAE THRRHINSAF MTFVVLDADD QPQLLPWIRP QPGDGERRYR EASARKKIRL
     DRKYIVSCKQ TEVPLSVPWD PSNQVYLSYN NVSSLKMLVA KDNWVLSSEI SQVRLYTLED
     DKFLSFHMEM VVHVDAAQAF LLLSDLRQRP EWDKHYRSVE LVQQVDEDDA IYHVTSPALG
     GHTKPQDFVI LASRRKPCDN GDPYVIALRS VTLPTHRETP EYRRGETLCS GFCLWREGDQ
     LTKCCWVRVS LTELVSASGF YSWGLESRSK GRRSDGWNGK LAGGHLSTLK AIPVAKINSR
     FGYLQDT
//