ID Q9VJ43_DROME Unreviewed; 544 AA. AC Q9VJ43; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 19-JAN-2022, entry version 184. DE RecName: Full=Acetyl-CoA C-myristoyltransferase {ECO:0000256|ARBA:ARBA00024077}; DE EC=2.3.1.155 {ECO:0000256|ARBA:ARBA00024058}; DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073}; DE EC=2.3.1.176 {ECO:0000256|ARBA:ARBA00012352}; DE AltName: Full=Non-specific lipid-transfer protein {ECO:0000256|ARBA:ARBA00017183}; DE AltName: Full=Propanoyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00017737}; DE AltName: Full=SCP-2/3-oxoacyl-CoA thiolase {ECO:0000256|ARBA:ARBA00024112}; DE AltName: Full=SCP-2/thiolase {ECO:0000256|ARBA:ARBA00024137}; DE AltName: Full=SCP-chi {ECO:0000256|ARBA:ARBA00017535}; DE AltName: Full=Sterol carrier protein 2 {ECO:0000256|ARBA:ARBA00014545}; DE AltName: Full=Sterol carrier protein X {ECO:0000256|ARBA:ARBA00014519}; GN Name=ScpX {ECO:0000313|EMBL:AAF53713.1, GN ECO:0000313|FlyBase:FBgn0015808}; GN Synonyms=Dmel\CG17320 {ECO:0000313|EMBL:AAF53713.1}; GN ORFNames=CG17320 {ECO:0000313|EMBL:AAF53713.1, GN ECO:0000313|FlyBase:FBgn0015808}, Dmel_CG17320 GN {ECO:0000313|EMBL:AAF53713.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF53713.1, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:AAF53713.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., RA Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A., RA An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D., RA Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F., RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., RA Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., RA Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E., RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A., RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C., RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G., RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] {ECO:0000313|EMBL:AAF53713.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster RT euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [3] {ECO:0000313|EMBL:AAF53713.1, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfied E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A., Harris N.L., RA Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., RA Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] {ECO:0000313|EMBL:AAF53713.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M., RA Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: a RT genomics perspective."; RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002). RN [5] {ECO:0000313|EMBL:AAF53713.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [6] {ECO:0000313|EMBL:AAL90277.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Berkeley {ECO:0000313|EMBL:AAL90277.1}; RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M., RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R., RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A., RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S., RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:AAF53713.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [8] {ECO:0000313|EMBL:AAF53713.1} RP NUCLEOTIDE SEQUENCE. RA Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S., RA Svirskas R., Rubin G.; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [9] {ECO:0000313|EMBL:AAF53713.1} RP NUCLEOTIDE SEQUENCE. RG Berkeley Drosophila Genome Project; RA Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R., RA Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., Yu C., RA Rubin G.; RT "Drosophila melanogaster release 4 sequence."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. RN [10] {ECO:0000313|EMBL:AAF53713.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin."; RL Science 316:1586-1591(2007). RN [11] {ECO:0000313|EMBL:AAF53713.1, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). RN [12] {ECO:0000313|EMBL:AAF53713.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26109357; DOI=.1534/g3.115.018929; RG FlyBase Consortium; RA Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B., St Pierre S.E., RA Gramates L.S., Zhou P., Schroeder A.J., Falls K., Strelets V., Russo S.M., RA Gelbart W.M.; RT "Gene Model Annotations for Drosophila melanogaster: Impact of High- RT Throughput Data."; RL G3 (Bethesda) 5:1721-1736(2015). RN [13] {ECO:0000313|EMBL:AAF53713.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26109356; DOI=.1534/g3.115.018937; RG FlyBase Consortium; RA Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B., St Pierre S.E., RA Zhou P., Schroeder A.J., Falls K., Emmert D.B., Russo S.M., Gelbart W.M.; RT "Gene Model Annotations for Drosophila melanogaster: The Rule-Benders."; RL G3 (Bethesda) 5:1737-1749(2015). RN [14] {ECO:0000313|EMBL:AAF53713.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=25589440; RA Hoskins R.A., Carlson J.W., Wan K.H., Park S., Mendez I., Galle S.E., RA Booth B.W., Pfeiffer B.D., George R.A., Svirskas R., Krzywinski M., RA Schein J., Accardo M.C., Damia E., Messina G., Mendez-Lago M., RA de Pablos B., Demakova O.V., Andreyeva E.N., Boldyreva L.V., Marra M., RA Carvalho A.B., Dimitri P., Villasante A., Zhimulev I.F., Rubin G.M., RA Karpen G.H., Celniker S.E.; RT "The Release 6 reference sequence of the Drosophila melanogaster genome."; RL Genome Res. 25:445-458(2015). RN [15] {ECO:0000313|EMBL:AAF53713.1} RP NUCLEOTIDE SEQUENCE. RG FlyBase; RL Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxo-(9Z-octadecenoyl)-CoA + CoA = (7Z)-hexadecenoyl-CoA + CC acetyl-CoA; Xref=Rhea:RHEA:47400, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:87695, ChEBI:CHEBI:87698; CC Evidence={ECO:0000256|ARBA:ARBA00024514}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47401; CC Evidence={ECO:0000256|ARBA:ARBA00024514}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxohexadecanedioyl-CoA + CoA = acetyl-CoA + CC tetradecanedioyl-CoA; Xref=Rhea:RHEA:40343, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288, ChEBI:CHEBI:77081, ChEBI:CHEBI:77084; CC Evidence={ECO:0000256|ARBA:ARBA00024540}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40344; CC Evidence={ECO:0000256|ARBA:ARBA00024540}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA; CC Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16; CC Evidence={ECO:0000256|ARBA:ARBA00024485}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566; CC Evidence={ECO:0000256|ARBA:ARBA00024485}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + butanoyl-CoA = 3-oxohexanoyl-CoA + CoA; CC Xref=Rhea:RHEA:31111, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57371, ChEBI:CHEBI:62418; CC Evidence={ECO:0000256|ARBA:ARBA00024476}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31113; CC Evidence={ECO:0000256|ARBA:ARBA00024476}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + decanoyl-CoA = 3-oxododecanoyl-CoA + CoA; CC Xref=Rhea:RHEA:31183, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:61430, ChEBI:CHEBI:62615; CC Evidence={ECO:0000256|ARBA:ARBA00024559}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31185; CC Evidence={ECO:0000256|ARBA:ARBA00024559}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + dodecanoyl-CoA = 3-oxotetradecanoyl-CoA + CoA; CC Xref=Rhea:RHEA:31091, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57375, ChEBI:CHEBI:62543; CC Evidence={ECO:0000256|ARBA:ARBA00024598}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31093; CC Evidence={ECO:0000256|ARBA:ARBA00024598}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + hexadecanoyl-CoA = 3-oxooctadecanoyl-CoA + CoA; CC Xref=Rhea:RHEA:35279, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57379, ChEBI:CHEBI:71407; CC Evidence={ECO:0000256|ARBA:ARBA00024549}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35281; CC Evidence={ECO:0000256|ARBA:ARBA00024549}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + hexanoyl-CoA = 3-oxooctanoyl-CoA + CoA; CC Xref=Rhea:RHEA:31203, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:62619, ChEBI:CHEBI:62620; CC Evidence={ECO:0000256|ARBA:ARBA00024462}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31205; CC Evidence={ECO:0000256|ARBA:ARBA00024462}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + octanoyl-CoA = 3-oxodecanoyl-CoA + CoA; CC Xref=Rhea:RHEA:31087, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57386, ChEBI:CHEBI:62548; CC Evidence={ECO:0000256|ARBA:ARBA00024542}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31089; CC Evidence={ECO:0000256|ARBA:ARBA00024542}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + tetradecanoyl-CoA = 3-oxohexadecanoyl-CoA + CoA; CC Xref=Rhea:RHEA:18161, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:57349, ChEBI:CHEBI:57385; EC=2.3.1.155; CC Evidence={ECO:0000256|ARBA:ARBA00024455}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18163; CC Evidence={ECO:0000256|ARBA:ARBA00024455}; CC -!- CATALYTIC ACTIVITY: CC Reaction=7-dehydrocholesterol(in) = 7-dehydrocholesterol(out); CC Xref=Rhea:RHEA:62960, ChEBI:CHEBI:17759; CC Evidence={ECO:0000256|ARBA:ARBA00024585}; CC -!- CATALYTIC ACTIVITY: CC Reaction=choloyl-CoA + propanoyl-CoA = 3alpha,7alpha,12alpha- CC trihydroxy-24-oxo-5beta-cholestan-26-oyl-CoA + CoA; CC Xref=Rhea:RHEA:16865, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373, CC ChEBI:CHEBI:57392, ChEBI:CHEBI:58507; EC=2.3.1.176; CC Evidence={ECO:0000256|ARBA:ARBA00024509}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16867; CC Evidence={ECO:0000256|ARBA:ARBA00024509}; CC -!- CATALYTIC ACTIVITY: CC Reaction=propanoyl-CoA + tetradecanoyl-CoA = 3-oxo-2- CC methylhexadecanoyl-CoA + CoA; Xref=Rhea:RHEA:46344, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:57392, CC ChEBI:CHEBI:86042; Evidence={ECO:0000256|ARBA:ARBA00024471}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:46346; CC Evidence={ECO:0000256|ARBA:ARBA00024471}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Peroxisome CC {ECO:0000256|ARBA:ARBA00004275}. CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family. CC {ECO:0000256|RuleBase:RU003557}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014134; AAF53713.1; -; Genomic_DNA. DR EMBL; AY089539; AAL90277.1; -; mRNA. DR RefSeq; NP_524715.2; NM_079976.6. DR IntAct; Q9VJ43; 3. DR STRING; 7227.FBpp0080659; -. DR DNASU; 44183; -. DR EnsemblMetazoa; FBtr0081109; FBpp0080659; FBgn0015808. DR GeneID; 44183; -. DR KEGG; dme:Dmel_CG17320; -. DR UCSC; CG17320-RA; d. melanogaster. DR CTD; 44183; -. DR FlyBase; FBgn0015808; ScpX. DR VEuPathDB; VectorBase:FBgn0015808; -. DR eggNOG; KOG1406; Eukaryota. DR eggNOG; KOG4170; Eukaryota. DR GeneTree; ENSGT00940000154327; -. DR HOGENOM; CLU_035425_0_1_1; -. DR OMA; PSLYAMM; -. DR OrthoDB; 661265at2759; -. DR Reactome; R-DME-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol. DR Reactome; R-DME-2046106; alpha-linolenic acid (ALA) metabolism. DR Reactome; R-DME-389887; Beta-oxidation of pristanoyl-CoA. DR Reactome; R-DME-9033241; Peroxisomal protein import. DR BioGRID-ORCS; 44183; 0 hits in 1 CRISPR screen. DR GenomeRNAi; 44183; -. DR Proteomes; UP000000803; Chromosome 2L. DR Bgee; FBgn0015808; Expressed in embryonic/larval hemocyte (Drosophila) and 48 other tissues. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0005777; C:peroxisome; ISS:FlyBase. DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0050633; F:acetyl-CoA C-myristoyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0005548; F:phospholipid transporter activity; ISS:FlyBase. DR GO; GO:0033814; F:propanoyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0050632; F:propionyl-CoA C2-trimethyltridecanoyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0015914; P:phospholipid transport; ISS:FlyBase. DR GO; GO:0032385; P:positive regulation of intracellular cholesterol transport; IBA:GO_Central. DR Gene3D; 3.30.1050.10; -; 1. DR Gene3D; 3.40.47.10; -; 1. DR InterPro; IPR003033; SCP2_sterol-bd_dom. DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf. DR InterPro; IPR016039; Thiolase-like. DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS. DR InterPro; IPR020617; Thiolase_C. DR InterPro; IPR020613; Thiolase_CS. DR InterPro; IPR020616; Thiolase_N. DR Pfam; PF02036; SCP2; 1. DR Pfam; PF02803; Thiolase_C; 1. DR Pfam; PF00108; Thiolase_N; 1. DR SUPFAM; SSF53901; SSF53901; 2. DR SUPFAM; SSF55718; SSF55718; 1. DR PROSITE; PS00098; THIOLASE_1; 1. DR PROSITE; PS00737; THIOLASE_2; 1. PE 1: Evidence at protein level; KW Acyltransferase {ECO:0000256|RuleBase:RU003557, KW ECO:0000313|EMBL:AAF53713.1}; KW Lipid transport {ECO:0000256|ARBA:ARBA00023055}; KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}; KW Peroxisome {ECO:0000256|ARBA:ARBA00023140}; KW Proteomics identification {ECO:0007829|PeptideAtlas:Q9VJ43}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003557}; KW Transport {ECO:0000256|ARBA:ARBA00022448}. FT DOMAIN 6..195 FT /note="Thiolase_N" FT /evidence="ECO:0000259|Pfam:PF00108" FT DOMAIN 275..366 FT /note="Thiolase_C" FT /evidence="ECO:0000259|Pfam:PF02803" FT DOMAIN 430..529 FT /note="SCP2" FT /evidence="ECO:0000259|Pfam:PF02036" SQ SEQUENCE 544 AA; 59008 MW; A14B0A7D2185E9C2 CRC64; MSKTRVYVVG VGMTKFEKPG RQADVCYPDF AREAITKALQ DAGIKYEEVQ QAVAGYVYGD STCGQRAIYE VGMTGIPVYN VNNNCSTGSS ALYLAKQIVE SGNADCVLAL GFEKMERGSL SSKYFDRANP MERHITEMGE LAEIGAGPMA AQIFGNAGKE HMKKYGTKPE HFGKIAWKNH KHSVNNPYSQ FRDEYTLEQI MKSPQVVEGV LTKLQCCPTS DGSGAAILAS EAFVRRHGLE KQAVEIVGME MASDPASTFA DKSLMKIAGT DMTRLATQRL FAKSGYKPQD VQVVELHDCF SANELITYEA LGLCGEGNAG EFIDAGDNTY GGKFVVNPSG GLISKGHPLG ATGLAQCAEL CWQLRGLAEK RQVPNAQLAL QHNLGLGGAV VVALYRLGFP AANSVVRNLT AAGKAATSED GFKVAPLLKL LEQAMQEDKD NLIEKVRAIY GFKVNNGPNG QTGFWVIDAK QGKGKIIFNG TQKCDVTFII SDDDVFELLT GKLPPQKAFF QGKIKIQGNM GFAMKLMDLQ RSAQGRIEEL RSKL //