SAST_RAT
ID SAST_RAT Reviewed; 263 AA.
AC P08635;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=S-acyl fatty acid synthase thioesterase, medium chain {ECO:0000303|PubMed:3632637};
DE EC=3.1.2.14 {ECO:0000269|PubMed:8446599};
DE AltName: Full=Medium-chain S-acyl fatty acid synthetase thioester hydrolase {ECO:0000303|PubMed:3105579};
DE AltName: Full=Oleoyl-ACP hydrolase;
DE AltName: Full=Thioesterase II;
DE AltName: Full=Thioesterase domain-containing protein 1;
GN Name=Olah {ECO:0000312|RGD:621115};
GN Synonyms=Mch {ECO:0000303|PubMed:3105579}, Thedc1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Mammary gland;
RX PubMed=3105579; DOI=10.1021/bi00379a023;
RA Safford R., de Silva J., Lucas C., Windust J.H.C., Shedden J., James C.M.,
RA Sidebottom C.M., Slabas A.R., Tombs M.P., Hughes S.G.;
RT "Molecular cloning and sequence analysis of complementary DNA encoding rat
RT mammary gland medium-chain S-acyl fatty acid synthetase thio ester
RT hydrolase.";
RL Biochemistry 26:1358-1364(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RX PubMed=3632637; DOI=10.1042/bj2430597;
RA Naggert J., Williams B., Caslhman D.P., Smith S.;
RT "Cloning and sequencing of the medium-chain S-acyl fatty acid synthetase
RT thioester hydrolase cDNA from rat mammary gland.";
RL Biochem. J. 243:597-601(1987).
RN [3]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RC TISSUE=Mammary gland;
RX PubMed=3567174; DOI=10.1021/bi00379a024;
RA Randhawa Z.I., Smith S.;
RT "Complete amino acid sequence of the medium-chain S-acyl fatty acid
RT synthetase thio ester hydrolase from rat mammary gland.";
RL Biochemistry 26:1365-1373(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 91-121, PROTEIN SEQUENCE OF 65-121, AND
RP ACTIVE SITE.
RC TISSUE=Mammary gland;
RX PubMed=3104035; DOI=10.1111/j.1432-1033.1987.tb10678.x;
RA Randhawa Z.I., Naggert J., Blacher R.W., Smith S.;
RT "Amino acid sequence of the serine active-site region of the medium-chain
RT S-acyl fatty acid synthetase thioester hydrolase from rat mammary gland.";
RL Eur. J. Biochem. 162:577-581(1987).
RN [5]
RP CATALYTIC ACTIVITY, FUNCTION, ACTIVE SITE, INTERACTION WITH FASN, AND
RP MUTAGENESIS OF SER-101; ASP-236; HIS-237; LEU-262; 262-LEU-THR-263 AND
RP THR-263.
RX PubMed=8446599; DOI=10.1073/pnas.90.5.1852;
RA Tai M.H., Chirala S.S., Wakil S.J.;
RT "Roles of Ser101, Asp236, and His237 in catalysis of thioesterase II and of
RT the C-terminal region of the enzyme in its interaction with fatty acid
RT synthase.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:1852-1856(1993).
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:0000269|PubMed:8446599}.
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:0000269|PubMed:8446599};
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:8446599};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060;
CC Evidence={ECO:0000305|PubMed:8446599};
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:8446599};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000305|PubMed:8446599};
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:8446599};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000305|PubMed:8446599};
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:0000269|PubMed:8446599};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000305|PubMed:8446599};
CC -!- SUBUNIT: Interacts (via C-terminus) with FASN.
CC {ECO:0000269|PubMed:8446599}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:3105579}.
CC -!- SIMILARITY: Belongs to the thioesterase family. {ECO:0000305}.
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DR EMBL; M16200; AAA41578.1; -; mRNA.
DR EMBL; Y00311; CAA68411.1; -; mRNA.
DR PIR; A26625; A26625.
DR RefSeq; NP_073196.1; NM_022705.1.
DR RefSeq; XP_008770108.1; XM_008771886.2.
DR RefSeq; XP_008770109.1; XM_008771887.2.
DR RefSeq; XP_017456149.1; XM_017600660.1.
DR AlphaFoldDB; P08635; -.
DR SMR; P08635; -.
DR STRING; 10116.ENSRNOP00000022043; -.
DR SwissLipids; SLP:000000766; -.
DR ESTHER; ratno-sast; Thioesterase.
DR iPTMnet; P08635; -.
DR PaxDb; P08635; -.
DR PRIDE; P08635; -.
DR Ensembl; ENSRNOT00000022043; ENSRNOP00000022043; ENSRNOG00000016403.
DR GeneID; 64669; -.
DR KEGG; rno:64669; -.
DR UCSC; RGD:621115; rat.
DR CTD; 55301; -.
DR RGD; 621115; Olah.
DR eggNOG; ENOG502RGSQ; Eukaryota.
DR GeneTree; ENSGT00390000015518; -.
DR HOGENOM; CLU_070456_3_0_1; -.
DR InParanoid; P08635; -.
DR OMA; ALCRLIC; -.
DR OrthoDB; 1324961at2759; -.
DR PhylomeDB; P08635; -.
DR TreeFam; TF331555; -.
DR PRO; PR:P08635; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000016403; Expressed in ovary and 9 other tissues.
DR Genevisible; P08635; RN.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016297; F:acyl-[acyl-carrier-protein] hydrolase activity; IDA:UniProtKB.
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; IDA: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 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Fatty acid biosynthesis;
KW Fatty acid metabolism; Hydrolase; Lipid biosynthesis; Lipid metabolism;
KW Reference proteome.
FT CHAIN 1..263
FT /note="S-acyl fatty acid synthase thioesterase, medium
FT chain"
FT /id="PRO_0000180360"
FT REGION 262..263
FT /note="Important for interaction with FASN"
FT /evidence="ECO:0000269|PubMed:8446599"
FT ACT_SITE 101
FT /evidence="ECO:0000269|PubMed:3104035,
FT ECO:0000269|PubMed:8446599"
FT ACT_SITE 237
FT /evidence="ECO:0000269|PubMed:8446599"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:3567174"
FT MUTAGEN 101
FT /note="S->A: Loss of thioesterase activity."
FT /evidence="ECO:0000269|PubMed:8446599"
FT MUTAGEN 101
FT /note="S->C: Decreased thioesterase activity."
FT /evidence="ECO:0000269|PubMed:8446599"
FT MUTAGEN 236
FT /note="D->A: Moderately decreased thioesterase activity."
FT /evidence="ECO:0000269|PubMed:8446599"
FT MUTAGEN 237
FT /note="H->A: Loss of thioesterase activity."
FT /evidence="ECO:0000269|PubMed:8446599"
FT MUTAGEN 262..263
FT /note="Missing: Strongly decreased thioesterase activity
FT with FASN-bound fatty acids. No effect on thioesterase
FT activity with free decanoyl coenzyme A."
FT /evidence="ECO:0000269|PubMed:8446599"
FT MUTAGEN 262
FT /note="L->A: Strongly decreased thioesterase activity with
FT FASN-bound fatty acids. No effect on thioesterase activity
FT with free decanoyl coenzyme A."
FT /evidence="ECO:0000269|PubMed:8446599"
FT MUTAGEN 263
FT /note="T->V: No effect on thioesterase activity."
FT /evidence="ECO:0000269|PubMed:8446599"
SQ SEQUENCE 263 AA; 29471 MW; 6AB3681E639D7E02 CRC64;
METAVNAKSP RNEKVLNCLY QNPDAVFKLI CFPWAGGGSI HFAKWGQKIN DSLEVHAVRL
AGRETRLGEP FANDIYQIAD EIVTALLPII QDKAFAFFGH SFGSYIALIT ALLLKEKYKM
EPLHIFVSGA SAPHSTSRPQ VPDLNELTEE QVRHHLLDFG GTPKHLIEDQ DVLRMFIPLL
KADAGVVKKF IFDKPSKALL SLDITGFLGS EDTIKDIEGW QDLTSGKFDV HMLPGDHFYL
MKPDNENFIK NYIAKCLELS SLT
