ACO11_HUMAN
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 03-AUG-2022, entry version 182.
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; 23.
DR IntAct; Q8WXI4; 15.
DR STRING; 9606.ENSP00000360366; -.
DR SwissLipids; SLP:000001186; -. [Q8WXI4-2]
DR iPTMnet; Q8WXI4; -.
DR PhosphoSitePlus; Q8WXI4; -.
DR BioMuta; ACOT11; -.
DR DMDM; 21363000; -.
DR EPD; Q8WXI4; -.
DR jPOST; Q8WXI4; -.
DR MassIVE; Q8WXI4; -.
DR MaxQB; Q8WXI4; -.
DR PaxDb; Q8WXI4; -.
DR PeptideAtlas; Q8WXI4; -.
DR PRIDE; Q8WXI4; -.
DR ProteomicsDB; 75066; -. [Q8WXI4-1]
DR ProteomicsDB; 75067; -. [Q8WXI4-2]
DR Antibodypedia; 33192; 257 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 CTD; 26027; -.
DR DisGeNET; 26027; -.
DR GeneCards; ACOT11; -.
DR HGNC; HGNC:18156; ACOT11.
DR HPA; ENSG00000162390; Tissue enhanced (choroid plexus, 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; 776852at2759; -.
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 1073 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 179 other tissues.
DR Genevisible; Q8WXI4; HS.
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:0036042; F:long-chain fatty acyl-CoA binding; IBA:GO_Central.
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; IBA:GO_Central.
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 Gene3D; 3.30.530.20; -; 1.
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; PTHR11049; 1.
DR Pfam; PF03061; 4HBT; 2.
DR Pfam; PF01852; START; 1.
DR SMART; SM00234; START; 1.
DR SUPFAM; SSF54637; SSF54637; 2.
DR PROSITE; PS51770; HOTDOG_ACOT; 2.
DR PROSITE; PS50848; START; 1.
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
