SCP2_MOUSE
ID SCP2_MOUSE Reviewed; 547 AA.
AC P32020; A2APS2; A2APS3; Q9DBM7;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 3.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Sterol carrier protein 2 {ECO:0000305};
DE Short=SCP-2;
DE AltName: Full=Acetyl-CoA C-myristoyltransferase;
DE EC=2.3.1.155 {ECO:0000250|UniProtKB:P11915};
DE AltName: Full=Non-specific lipid-transfer protein {ECO:0000305};
DE Short=NSL-TP;
DE AltName: Full=Propanoyl-CoA C-acyltransferase;
DE EC=2.3.1.176 {ECO:0000269|PubMed:10706581, ECO:0000269|PubMed:9553048};
DE AltName: Full=SCP-2/3-oxoacyl-CoA thiolase;
DE AltName: Full=SCP-2/thiolase;
DE EC=2.3.1.16 {ECO:0000269|PubMed:9553048};
DE AltName: Full=SCP-chi;
DE AltName: Full=Sterol carrier protein X;
DE Short=SCP-X;
GN Name=Scp2 {ECO:0000312|MGI:MGI:98254}; Synonyms=Scp-2;
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 [MRNA].
RC TISSUE=Liver;
RX PubMed=8428655; DOI=10.1016/0378-1119(93)90120-r;
RA Seedorf U., Raabe M., Assmann G.;
RT "Cloning, expression and sequences of mouse sterol-carrier protein-x-
RT encoding cDNAs and a related pseudogene.";
RL Gene 123:165-172(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver, and Mammary gland;
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 [5]
RP PROTEIN SEQUENCE OF 525-534, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 405-547, AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=1709640; DOI=10.1016/s0021-9258(18)92901-7;
RA Moncecchi D.T., Pastuszyn A., Scallen T.J.;
RT "cDNA sequence and bacterial expression of mouse liver sterol carrier
RT protein-2.";
RL J. Biol. Chem. 266:9885-9892(1991).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=8751375; DOI=10.1159/000134355;
RA Raabe M., Seedorf U., Hameister H., Ellinghaus P., Assmann G.;
RT "Structure and chromosomal assignment of the murine sterol carrier protein
RT 2 gene (Scp2) and two related pseudogenes by in situ hybridization.";
RL Cytogenet. Cell Genet. 73:279-281(1996).
RN [8]
RP DISRUPTION PHENOTYPE, FUNCTION (ISOFORM SCPX), AND CATALYTIC ACTIVITY.
RX PubMed=9553048; DOI=10.1101/gad.12.8.1189;
RA Seedorf U., Raabe M., Ellinghaus P., Kannenberg F., Fobker M., Engel T.,
RA Denis S., Wouters F., Wirtz K.W., Wanders R.J., Maeda N., Assmann G.;
RT "Defective peroxisomal catabolism of branched fatty acyl coenzyme A in mice
RT lacking the sterol carrier protein-2/sterol carrier protein-x gene
RT function.";
RL Genes Dev. 12:1189-1201(1998).
RN [9]
RP FUNCTION (ISOFORM SCP2), AND SUBCELLULAR LOCATION (ISOFORM SCP2).
RX PubMed=11003606; DOI=10.1152/ajpcell.2000.279.4.c1259;
RA Starodub O., Jolly C.A., Atshaves B.P., Roths J.B., Murphy E.J., Kier A.B.,
RA Schroeder F.;
RT "Sterol carrier protein-2 localization in endoplasmic reticulum and role in
RT phospholipid formation.";
RL Am. J. Physiol. 279:C1259-C1269(2000).
RN [10]
RP FUNCTION (ISOFORM SCPX), AND CATALYTIC ACTIVITY.
RX PubMed=10706581;
RA Ferdinandusse S., Denis S., van Berkel E., Dacremont G., Wanders R.J.;
RT "Peroxisomal fatty acid oxidation disorders and 58 kDa sterol carrier
RT protein X (SCPx). Activity measurements in liver and fibroblasts using a
RT newly developed method.";
RL J. Lipid Res. 41:336-342(2000).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-173, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y.,
RA Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT "Substrate and functional diversity of lysine acetylation revealed by a
RT proteomics survey.";
RL Mol. Cell 23:607-618(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-40; LYS-132; LYS-168; LYS-183;
RP LYS-211; LYS-282; LYS-341; LYS-432; LYS-438; LYS-443; LYS-453; LYS-464;
RP LYS-470; LYS-479; LYS-492; LYS-511; LYS-522; LYS-534 AND LYS-544, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-7; LYS-132; LYS-177; LYS-183;
RP LYS-341; LYS-432; LYS-438; LYS-443; LYS-453; LYS-470 AND LYS-491, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [17]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=26901662; DOI=10.1371/journal.pone.0149728;
RA Li N.C., Fan J., Papadopoulos V.;
RT "Sterol Carrier Protein-2, a Nonspecific Lipid-Transfer Protein, in
RT Intracellular Cholesterol Trafficking in Testicular Leydig Cells.";
RL PLoS ONE 11:e0149728-e0149728(2016).
CC -!- FUNCTION: [Isoform SCPx]: Plays a crucial role in the peroxisomal
CC oxidation of branched-chain fatty acids (PubMed:10706581). Catalyzes
CC the last step of the peroxisomal beta-oxidation of branched chain fatty
CC acids and the side chain of the bile acid intermediates di- and
CC trihydroxycoprostanic acids (DHCA and THCA) (PubMed:10706581). Also
CC active with medium and long straight chain 3-oxoacyl-CoAs (By
CC similarity). Stimulates the microsomal conversion of 7-
CC dehydrocholesterol to cholesterol and transfers phosphatidylcholine and
CC 7-dehydrocholesterol between membrances, in vitro (By similarity).
CC Isoforms SCP2 and SCPx cooperate in peroxisomal oxidation of certain
CC naturally occurring tetramethyl-branched fatty acyl-CoAs
CC (PubMed:9553048). {ECO:0000250|UniProtKB:P11915,
CC ECO:0000269|PubMed:10706581, ECO:0000269|PubMed:9553048}.
CC -!- FUNCTION: [Isoform SCP2]: Mediates the transfer of all common
CC phospholipids, cholesterol and gangliosides from the endoplasmic
CC reticulum to the plasma membrane. May play a role in regulating
CC steroidogenesis (By similarity). Stimulates the microsomal conversion
CC of 7-dehydrocholesterol to cholesterol (By similarity). Also binds
CC fatty acids and fatty acyl Coenzyme A (CoA) such as phytanoyl-CoA
CC (PubMed:9553048). Involved in the regulation phospholipid synthesis in
CC endoplasmic reticulum enhancing the incorporation of exogenous fatty
CC acid into glycerides (PubMed:11003606). Seems to stimulate the rate-
CC limiting step in phosphatidic acid formation mediated by GPAT3
CC (PubMed:11003606). Isoforms SCP2 and SCPx cooperate in peroxisomal
CC oxidation of certain naturally occurring tetramethyl-branched fatty
CC acyl-CoAs (PubMed:9553048). {ECO:0000250|UniProtKB:P11915,
CC ECO:0000250|UniProtKB:P22307, ECO:0000269|PubMed:11003606,
CC ECO:0000269|PubMed:9553048}.
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
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:0000269|PubMed:10706581, ECO:0000269|PubMed:9553048};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16867;
CC Evidence={ECO:0000269|PubMed:10706581, ECO:0000269|PubMed:9553048};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
CC Reaction=4,8,12-trimethyltridecanoyl-CoA + propanoyl-CoA = 3-
CC oxopristanoyl-CoA + CoA; Xref=Rhea:RHEA:10408, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57291, ChEBI:CHEBI:57351, ChEBI:CHEBI:57392;
CC EC=2.3.1.176; Evidence={ECO:0000305|PubMed:10706581};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10410;
CC Evidence={ECO:0000305|PubMed:10706581};
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:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
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:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31205;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
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:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18163;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
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:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40344;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
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:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:46346;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
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:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31113;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
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:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31089;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
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:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31185;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
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:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31093;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
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:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35281;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
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:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47401;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
CC Reaction=7-dehydrocholesterol(in) = 7-dehydrocholesterol(out);
CC Xref=Rhea:RHEA:62960, ChEBI:CHEBI:17759;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- CATALYTIC ACTIVITY: [Isoform SCP2]:
CC Reaction=7-dehydrocholesterol(in) = 7-dehydrocholesterol(out);
CC Xref=Rhea:RHEA:62960, ChEBI:CHEBI:17759;
CC Evidence={ECO:0000250|UniProtKB:P11915};
CC -!- SUBUNIT: [Isoform SCP2]: Interacts with PEX5; the interaction is
CC essential for peroxisomal import. {ECO:0000250|UniProtKB:P22307}.
CC -!- SUBCELLULAR LOCATION: [Isoform SCP2]: Cytoplasm
CC {ECO:0000269|PubMed:11003606, ECO:0000269|PubMed:26901662}. Peroxisome
CC {ECO:0000269|PubMed:11003606, ECO:0000269|PubMed:26901662}. Endoplasmic
CC reticulum {ECO:0000269|PubMed:11003606}. Mitochondrion
CC {ECO:0000269|PubMed:11003606, ECO:0000269|PubMed:26901662}.
CC -!- SUBCELLULAR LOCATION: [Isoform SCPx]: Peroxisome
CC {ECO:0000269|PubMed:26901662}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=SCPx;
CC IsoId=P32020-1; Sequence=Displayed;
CC Name=SCP2;
CC IsoId=P32020-2; Sequence=VSP_018895;
CC -!- TISSUE SPECIFICITY: Present at low levels in all tissues examined but
CC expressed predominantly in the liver.
CC -!- TISSUE SPECIFICITY: [Isoform SCPx]: In testis, highly expressed in the
CC interstitial connective tissue, an area rich in interstitial cells of
CC Leydig, but it is barely expressed in the germ cells of the
CC seminiferous tubule. {ECO:0000269|PubMed:26901662}.
CC -!- TISSUE SPECIFICITY: [Isoform SCP2]: In testis, expressed in the
CC interstitial connective tissue, an area rich in interstitial cells of
CC Leydig at lower levels than isoform SCPx.
CC {ECO:0000269|PubMed:26901662}.
CC -!- PTM: [Isoform SCP2]: preSCP2, a protein with a molecular mass of about
CC 15 kDa, is processed into its mature form (SCP2) by proteolytic
CC cleavage of a 20 residue leader sequence after translocation into
CC peroxisomes. {ECO:0000250|UniProtKB:O62742}.
CC -!- DISRUPTION PHENOTYPE: Knockouts are viable and fertile
CC (PubMed:9553048). Mutants show alterations in hepatic gene expression,
CC peroxisome proliferation, hypolipidemia, impaired body weight control
CC and neuropathy (PubMed:9553048). {ECO:0000269|PubMed:9553048}.
CC -!- MISCELLANEOUS: [Isoform SCP2]: Contains a putative mitochondrial
CC transit peptide at positions 1-20. {ECO:0000303|PubMed:26901662}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the thiolase-like
CC superfamily. Thiolase family. {ECO:0000305}.
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; M91458; AAA40098.1; -; mRNA.
DR EMBL; AK002425; BAB22092.2; -; mRNA.
DR EMBL; AK004860; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL844206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018384; AAH18384.1; -; mRNA.
DR EMBL; BC034613; AAH34613.1; -; mRNA.
DR EMBL; M62361; AAA40099.1; -; mRNA.
DR EMBL; X91150; CAA62592.1; -; Genomic_DNA.
DR CCDS; CCDS18446.1; -. [P32020-1]
DR PIR; A40015; A40015.
DR PIR; JU0157; JU0157.
DR RefSeq; NP_035457.1; NM_011327.4. [P32020-1]
DR AlphaFoldDB; P32020; -.
DR SMR; P32020; -.
DR BioGRID; 203108; 9.
DR IntAct; P32020; 3.
DR MINT; P32020; -.
DR STRING; 10090.ENSMUSP00000030340; -.
DR SwissLipids; SLP:000000495; -.
DR iPTMnet; P32020; -.
DR PhosphoSitePlus; P32020; -.
DR SwissPalm; P32020; -.
DR EPD; P32020; -.
DR jPOST; P32020; -.
DR MaxQB; P32020; -.
DR PaxDb; P32020; -.
DR PeptideAtlas; P32020; -.
DR PRIDE; P32020; -.
DR ProteomicsDB; 293582; -. [P32020-1]
DR ProteomicsDB; 293583; -. [P32020-2]
DR TopDownProteomics; P32020-1; -. [P32020-1]
DR Antibodypedia; 19167; 481 antibodies from 33 providers.
DR DNASU; 20280; -.
DR Ensembl; ENSMUST00000030340; ENSMUSP00000030340; ENSMUSG00000028603. [P32020-1]
DR Ensembl; ENSMUST00000106701; ENSMUSP00000102312; ENSMUSG00000028603. [P32020-2]
DR GeneID; 20280; -.
DR KEGG; mmu:20280; -.
DR UCSC; uc008uas.2; mouse. [P32020-1]
DR CTD; 6342; -.
DR MGI; MGI:98254; Scp2.
DR VEuPathDB; HostDB:ENSMUSG00000028603; -.
DR eggNOG; KOG1406; Eukaryota.
DR eggNOG; KOG4170; Eukaryota.
DR GeneTree; ENSGT00940000154327; -.
DR HOGENOM; CLU_035425_0_1_1; -.
DR InParanoid; P32020; -.
DR OMA; PSLYAMM; -.
DR OrthoDB; 661265at2759; -.
DR PhylomeDB; P32020; -.
DR TreeFam; TF300574; -.
DR BRENDA; 2.3.1.176; 3474.
DR Reactome; R-MMU-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-MMU-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-MMU-389887; Beta-oxidation of pristanoyl-CoA.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR BioGRID-ORCS; 20280; 5 hits in 77 CRISPR screens.
DR ChiTaRS; Scp2; mouse.
DR PRO; PR:P32020; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P32020; protein.
DR Bgee; ENSMUSG00000028603; Expressed in proximal tubule and 67 other tissues.
DR ExpressionAtlas; P32020; baseline and differential.
DR Genevisible; P32020; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; ISO:MGI.
DR GO; GO:0031315; C:extrinsic component of mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005782; C:peroxisomal matrix; ISS:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0050633; F:acetyl-CoA C-myristoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; ISO:MGI.
DR GO; GO:0120020; F:cholesterol transfer activity; ISS:UniProtKB.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0036042; F:long-chain fatty acyl-CoA binding; ISO:MGI.
DR GO; GO:0070538; F:oleic acid binding; ISO:MGI.
DR GO; GO:0120019; F:phosphatidylcholine transfer activity; ISS:UniProtKB.
DR GO; GO:1904121; F:phosphatidylethanolamine transfer activity; ISO:MGI.
DR GO; GO:0008526; F:phosphatidylinositol transfer activity; ISO:MGI.
DR GO; GO:0033814; F:propanoyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0050632; F:propionyl-CoA C2-trimethyltridecanoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR GO; GO:0007568; P:aging; ISO:MGI.
DR GO; GO:0008206; P:bile acid metabolic process; ISS:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0032959; P:inositol trisphosphate biosynthetic process; ISO:MGI.
DR GO; GO:0032367; P:intracellular cholesterol transport; ISS:UniProtKB.
DR GO; GO:1901373; P:lipid hydroperoxide transport; ISO:MGI.
DR GO; GO:0015914; P:phospholipid transport; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; ISO:MGI.
DR GO; GO:1904109; P:positive regulation of cholesterol import; ISO:MGI.
DR GO; GO:0032385; P:positive regulation of intracellular cholesterol transport; ISO:MGI.
DR GO; GO:0010893; P:positive regulation of steroid biosynthetic process; ISO:MGI.
DR GO; GO:0045940; P:positive regulation of steroid metabolic process; ISO:MGI.
DR GO; GO:0006701; P:progesterone biosynthetic process; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0071071; P:regulation of phospholipid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006694; P:steroid biosynthetic process; ISO:MGI.
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 Acetylation; Acyltransferase; Alternative initiation; Cytoplasm;
KW Direct protein sequencing; Endoplasmic reticulum; Lipid metabolism;
KW Lipid transport; Lipid-binding; Mitochondrion; Peroxisome; Phosphoprotein;
KW Reference proteome; Transferase; Transport.
FT CHAIN 1..547
FT /note="Sterol carrier protein 2"
FT /id="PRO_0000034093"
FT DOMAIN 433..543
FT /note="SCP2"
FT MOTIF 545..547
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:26901662"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11915"
FT MOD_RES 7
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939"
FT MOD_RES 40
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 132
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 132
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 168
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 173
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:16916647"
FT MOD_RES 177
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 183
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 183
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 211
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 282
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 341
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 341
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 432
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 432
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 438
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 438
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 443
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 443
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 453
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 453
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 464
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 470
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 470
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 479
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 491
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 492
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 511
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 522
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 534
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 544
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 1..404
FT /note="Missing (in isoform SCP2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018895"
FT CONFLICT 232
FT /note="A -> C (in Ref. 1; AAA40098)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="V -> A (in Ref. 6; AAA40099)"
FT /evidence="ECO:0000305"
FT SITE P32020-2:20..21
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:O62742"
SQ SEQUENCE 547 AA; 59126 MW; 37BA2E730D9CB105 CRC64;
MPSVALKSPR LRRVFVVGVG MTKFMKPGGE NSRDYPDMAK EAGQKALEDA QIPYSAVEQA
CVGYVYGDST SGQRAIYHSL GLTGIPIINV NNNCSTGSTA LFMAHQLIQG GLANCVLALG
FEKMERGSIG TKFSDRTTPT DKHIEVLIDK YGLSAHPITP QMFGYAGKEH MEKYGTKVEH
FAKIGWKNHK HSVNNTYSQF QDEYSLEEVM KSKPVFDFLT ILQCCPTSDG AAAAILSSEE
FVQQYGLQSK AVEIVAQEMM TDLPSTFEEK SIIKVVGYDM SKEAARRCYE KSGLTPNDVD
VIELHDCFSV NELITYEALG LCPEGQGGTL VDRGDNTYGG KWVINPSGGL ISKGHPLGAT
GLAQCAELCW QLRGEAGKRQ VPGAKVALQH NLGLGGAVVV TLYRMGFPEA ASSFRTHQVS
AAPTSSAGDG FKANLVFKEI EKKLEEEGEQ FVKKIGGIFA FKVKDGPGGK EATWVVDVKN
GKGSVLPNSD KKADCTITMA DSDLLALMTG KMNPQSAFFQ GKLKIAGNMG LAMKLQNLQL
QPGKAKL
