SAST_MOUSE
ID SAST_MOUSE Reviewed; 265 AA.
AC Q8R197; Q3UWY0;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=S-acyl fatty acid synthase thioesterase, medium chain;
DE EC=3.1.2.14 {ECO:0000250|UniProtKB:Q9NV23};
DE AltName: Full=Oleoyl-ACP hydrolase;
DE AltName: Full=Thioesterase II;
DE AltName: Full=Thioesterase domain-containing protein 1;
GN Name=Olah {ECO:0000312|MGI:MGI:2139018}; Synonyms=Thedc1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg, and Oviduct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
CC -!- FUNCTION: Contributes to the release of free fatty acids from fatty
CC acid synthase (FASN). Has broad substrate specificity, giving rise to a
CC range of free fatty acids with chain lengths between 10 and 16 carbon
CC atoms (C10 - C16). {ECO:0000250|UniProtKB:Q9NV23}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) +
CC holo-[ACP]; Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14;
CC Evidence={ECO:0000250|UniProtKB:Q9NV23};
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:0000250|UniProtKB:P08635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060;
CC Evidence={ECO:0000250|UniProtKB:P08635};
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:0000250|UniProtKB:P08635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000250|UniProtKB:P08635};
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:0000250|UniProtKB:P08635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000250|UniProtKB:P08635};
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;
CC Evidence={ECO:0000250|UniProtKB:P08635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000250|UniProtKB:P08635};
CC -!- SUBUNIT: Interacts (via C-terminus) with FASN.
CC {ECO:0000250|UniProtKB:P08635}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P08635}.
CC -!- SIMILARITY: Belongs to the thioesterase family. {ECO:0000305}.
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DR EMBL; AK087571; BAC39932.1; -; mRNA.
DR EMBL; AK136031; BAE22784.1; -; mRNA.
DR EMBL; BC025001; AAH25001.1; -; mRNA.
DR CCDS; CCDS15647.1; -.
DR RefSeq; NP_666033.1; NM_145921.1.
DR AlphaFoldDB; Q8R197; -.
DR SMR; Q8R197; -.
DR STRING; 10090.ENSMUSP00000110739; -.
DR ESTHER; mouse-AI607300; Thioesterase.
DR PhosphoSitePlus; Q8R197; -.
DR PaxDb; Q8R197; -.
DR PRIDE; Q8R197; -.
DR Antibodypedia; 4213; 50 antibodies from 14 providers.
DR DNASU; 99035; -.
DR Ensembl; ENSMUST00000027955; ENSMUSP00000027955; ENSMUSG00000026645.
DR Ensembl; ENSMUST00000115087; ENSMUSP00000110739; ENSMUSG00000026645.
DR Ensembl; ENSMUST00000194918; ENSMUSP00000141485; ENSMUSG00000026645.
DR GeneID; 99035; -.
DR KEGG; mmu:99035; -.
DR UCSC; uc008idu.1; mouse.
DR CTD; 55301; -.
DR MGI; MGI:2139018; Olah.
DR VEuPathDB; HostDB:ENSMUSG00000026645; -.
DR eggNOG; ENOG502RGSQ; Eukaryota.
DR GeneTree; ENSGT00390000015518; -.
DR HOGENOM; CLU_070456_3_0_1; -.
DR InParanoid; Q8R197; -.
DR OMA; ALCRLIC; -.
DR OrthoDB; 1324961at2759; -.
DR PhylomeDB; Q8R197; -.
DR TreeFam; TF331555; -.
DR BioGRID-ORCS; 99035; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Olah; mouse.
DR PRO; PR:Q8R197; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8R197; protein.
DR Bgee; ENSMUSG00000026645; Expressed in animal zygote and 28 other tissues.
DR Genevisible; Q8R197; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016297; F:acyl-[acyl-carrier-protein] hydrolase activity; ISO:MGI.
DR GO; GO:0047381; F:dodecanoyl-[acyl-carrier-protein] hydrolase activity; ISS:UniProtKB.
DR GO; GO:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; ISS:UniProtKB.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:RHEA.
DR GO; GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; ISS:UniProtKB.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:RHEA.
DR GO; GO:0008610; P:lipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0051792; P:medium-chain fatty acid biosynthetic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR012223; TEII.
DR InterPro; IPR001031; Thioesterase.
DR PANTHER; PTHR11487; PTHR11487; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Hydrolase; Lipid biosynthesis; Lipid metabolism; Reference proteome.
FT CHAIN 1..265
FT /note="S-acyl fatty acid synthase thioesterase, medium
FT chain"
FT /id="PRO_0000180359"
FT ACT_SITE 101
FT /evidence="ECO:0000250|UniProtKB:P08635"
FT ACT_SITE 237
FT /evidence="ECO:0000250|UniProtKB:P08635"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P08635"
SQ SEQUENCE 265 AA; 30250 MW; 8D235D7E82C8C300 CRC64;
METAVYAKST RNEKVLNCLC QKPDALFKLI CFPWAGGGST HFAKWGRKIN GLLEVHAVRL
AGRETRFEEP FSNDIYQIAE EVVTALLPII RDKAFAFFGH SFGSYIAFIT ALHLKEKYKM
EPLHIFVSSA SAPHSEFRPQ VPDINKLSEE QIRDHLLIFG GTPKHLIEDQ DFLKQCIPLL
KADVDIVKKF IFDKPSKALL SRDITCFIGS EDVVKDIEGW KDITSGKFDV LKLPGDHFYL
MEPNNEDFIK NYIVKCLELS SLDYF
