SCP2_RAT
ID SCP2_RAT Reviewed; 547 AA.
AC P11915; Q63383; Q642G0;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Sterol carrier protein 2 {ECO:0000305};
DE Short=SCP-2;
DE AltName: Full=Acetyl-CoA C-myristoyltransferase {ECO:0000303|PubMed:8063752, ECO:0000303|PubMed:9325339};
DE EC=2.3.1.155 {ECO:0000269|PubMed:8063752, ECO:0000269|PubMed:9325339};
DE AltName: Full=Non-specific lipid-transfer protein;
DE Short=NSL-TP;
DE AltName: Full=Propanoyl-CoA C-acyltransferase;
DE EC=2.3.1.176 {ECO:0000269|PubMed:9245689, ECO:0000269|PubMed:9325339, ECO:0000269|PubMed:9553048};
DE AltName: Full=SCP-2/3-oxoacyl-CoA thiolase {ECO:0000303|PubMed:8063752};
DE AltName: Full=SCP-2/thiolase {ECO:0000303|PubMed:9325339};
DE EC=2.3.1.16 {ECO:0000269|PubMed:8063752, ECO:0000269|PubMed:9325339};
DE AltName: Full=SCP-chi;
DE AltName: Full=Sterol carrier protein X;
DE Short=SCP-X;
GN Name=Scp2 {ECO:0000312|RGD:3642}; Synonyms=Scp-2;
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].
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=1985920; DOI=10.1016/s0021-9258(18)52481-9;
RA Seedorf U., Assmann G.;
RT "Cloning, expression, and nucleotide sequence of rat liver sterol carrier
RT protein 2 cDNAs.";
RL J. Biol. Chem. 266:630-636(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2034675; DOI=10.1073/pnas.88.10.4338;
RA Mori T., Tsukamoto T., Mori H., Tashiro Y., Fujiki Y.;
RT "Molecular cloning and deduced amino acid sequence of nonspecific lipid
RT transfer protein (sterol carrier protein 2) of rat liver: a higher
RT molecular mass (60 kDa) protein contains the primary sequence of
RT nonspecific lipid transfer protein as its C-terminal part.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4338-4342(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1915369; DOI=10.1111/j.1432-1033.1991.tb16279.x;
RA Ossendorp B.C., van Heusden G.P.H., de Beer A.L.J., Bos K., Schouten G.L.,
RA Wirtz K.W.A.;
RT "Identification of the cDNA clone which encodes the 58-kDa protein
RT containing the amino acid sequence of rat liver non-specific lipid-transfer
RT protein (sterol-carrier protein 2). Homology with rat peroxisomal and
RT mitochondrial 3-oxoacyl-CoA thiolases.";
RL Eur. J. Biochem. 201:233-239(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 33-547.
RC TISSUE=Liver;
RX PubMed=2334427; DOI=10.1016/0006-291x(90)92367-9;
RA Ossendorp B.C., van Heusden G.P.H., Wirtz K.W.A.;
RT "The amino acid sequence of rat liver non-specific lipid transfer protein
RT (sterol carrier protein 2) is present in a high molecular weight protein:
RT evidence from cDNA analysis.";
RL Biochem. Biophys. Res. Commun. 168:631-636(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 275-547.
RC STRAIN=CD Charles River; TISSUE=Liver;
RX PubMed=2340090; DOI=10.1089/dna.1990.9.159;
RA Billheimer J.T., Strehl L.L., Davis G.L., Strauss J.F. III, Davis L.G.;
RT "Characterization of a cDNA encoding rat sterol carrier protein2.";
RL DNA Cell Biol. 9:159-165(1990).
RN [7]
RP PROTEIN SEQUENCE OF 425-547.
RC TISSUE=Liver;
RX PubMed=3115977; DOI=10.1016/s0021-9258(18)45190-3;
RA Pastuszyn A., Noland B.J., Bazan J.F., Fletterick R.J., Scallen T.J.;
RT "Primary sequence and structural analysis of sterol carrier protein 2 from
RT rat liver: homology with immunoglobulins.";
RL J. Biol. Chem. 262:13219-13227(1987).
RN [8]
RP PROTEIN SEQUENCE OF 425-547.
RC TISSUE=Liver;
RX PubMed=3395344; DOI=10.1016/0006-291x(88)90711-5;
RA Morris H.R., Larsen B.S., Billheimer J.T.;
RT "A mass spectrometric study of the structure of sterol carrier protein SCP2
RT from rat liver.";
RL Biochem. Biophys. Res. Commun. 154:476-482(1988).
RN [9]
RP PROTEIN SEQUENCE OF 24-33; 354-363 AND 525-534, CATALYTIC ACTIVITY,
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9325339; DOI=10.1074/jbc.272.41.26023;
RA Antonenkov V.D., Van Veldhoven P.P., Waelkens E., Mannaerts G.P.;
RT "Substrate specificities of 3-oxoacyl-CoA thiolase A and sterol carrier
RT protein 2/3-oxoacyl-CoA thiolase purified from normal rat liver
RT peroxisomes. Sterol carrier protein 2/3-oxoacyl-CoA thiolase is involved in
RT the metabolism of 2-methyl-branched fatty acids and bile acid
RT intermediates.";
RL J. Biol. Chem. 272:26023-26031(1997).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=8063752; DOI=10.1016/s0021-9258(17)31960-9;
RA Seedorf U., Brysch P., Engel T., Schrage K., Assmann G.;
RT "Sterol carrier protein X is peroxisomal 3-oxoacyl coenzyme A thiolase with
RT intrinsic sterol carrier and lipid transfer activity.";
RL J. Biol. Chem. 269:21277-21283(1994).
RN [11]
RP FUNCTION (ISOFORM SCPX), AND CATALYTIC ACTIVITY.
RX PubMed=9245689; DOI=10.1006/bbrc.1997.7007;
RA Wanders R.J., Denis S., Wouters F., Wirtz K.W., Seedorf U.;
RT "Sterol carrier protein X (SCPx) is a peroxisomal branched-chain beta-
RT ketothiolase specifically reacting with 3-oxo-pristanoyl-CoA: a new, unique
RT role for SCPx in branched-chain fatty acid metabolism in peroxisomes.";
RL Biochem. Biophys. Res. Commun. 236:565-569(1997).
RN [12]
RP FUNCTION, 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 [13]
RP CATALYTIC ACTIVITY, FUNCTION (ISOFORM SCPX), AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-8 AND SER-537, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: [Isoform SCPx]: Plays a crucial role in the peroxisomal
CC oxidation of branched-chain fatty acids (PubMed:9325339,
CC PubMed:8063752). Catalyzes the last step of the peroxisomal beta-
CC oxidation of branched chain fatty acids and the side chain of the bile
CC acid intermediates di- and trihydroxycoprostanic acids (DHCA and THCA)
CC (PubMed:9325339, PubMed:8063752). Also active with medium and long
CC straight chain 3-oxoacyl-CoAs (PubMed:9325339, PubMed:10706581).
CC Stimulates the microsomal conversion of 7-dehydrocholesterol to
CC cholesterol and transfers phosphatidylcholine and 7-dehydrocholesterol
CC between membrances, in vitro (PubMed:8063752). Isoforms SCP2 and SCPx
CC cooperate in peroxisomal oxidation of certain naturally occurring
CC tetramethyl-branched fatty acyl-CoAs (PubMed:9553048).
CC {ECO:0000269|PubMed:10706581, ECO:0000269|PubMed:8063752,
CC ECO:0000269|PubMed:9325339, 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 (PubMed:8063752). Also binds
CC fatty acids and fatty acyl Coenzyme A (CoA) such as phytanoyl-CoA.
CC Involved in the regulation phospholipid synthesis in endoplasmic
CC reticulum enhancing the incorporation of exogenous fatty acid into
CC glycerides. Seems to stimulate the rate-limiting step in phosphatidic
CC acid formation mediated by GPAT3 (PubMed:9553048) (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:P22307,
CC ECO:0000250|UniProtKB:P32020, ECO:0000269|PubMed:8063752,
CC ECO:0000269|PubMed:9553048}.
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
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:0000305|PubMed:8063752, ECO:0000305|PubMed:9325339};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566;
CC Evidence={ECO:0000305|PubMed:8063752, ECO:0000305|PubMed:9325339};
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:9325339,
CC ECO:0000269|PubMed:9553048};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16867;
CC Evidence={ECO:0000305|PubMed:10706581, ECO:0000305|PubMed:9325339,
CC ECO:0000305|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:0000269|PubMed:9245689};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10410;
CC Evidence={ECO:0000305|PubMed:9245689};
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:0000269|PubMed:8063752, ECO:0000269|PubMed:9325339};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31205;
CC Evidence={ECO:0000305|PubMed:8063752, ECO:0000305|PubMed:9325339};
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:0000269|PubMed:8063752, ECO:0000269|PubMed:9325339};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18163;
CC Evidence={ECO:0000305|PubMed:8063752, ECO:0000305|PubMed:9325339};
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:0000269|PubMed:9325339};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40344;
CC Evidence={ECO:0000305|PubMed:9325339};
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:0000269|PubMed:9325339};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:46346;
CC Evidence={ECO:0000305|PubMed:9325339};
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:0000269|PubMed:8063752, ECO:0000269|PubMed:9325339};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31113;
CC Evidence={ECO:0000305|PubMed:8063752, ECO:0000305|PubMed:9325339};
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:0000269|PubMed:8063752, ECO:0000269|PubMed:9325339};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31089;
CC Evidence={ECO:0000305|PubMed:8063752, ECO:0000305|PubMed:9325339};
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:0000269|PubMed:9325339};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31185;
CC Evidence={ECO:0000305|PubMed:9325339};
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:0000269|PubMed:8063752, ECO:0000269|PubMed:9325339};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31093;
CC Evidence={ECO:0000305|PubMed:8063752, ECO:0000305|PubMed:9325339};
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:0000269|PubMed:8063752, ECO:0000269|PubMed:9245689};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35281;
CC Evidence={ECO:0000305|PubMed:8063752, ECO:0000305|PubMed:9245689};
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:0000269|PubMed:8063752};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47401;
CC Evidence={ECO:0000305|PubMed:8063752};
CC -!- CATALYTIC ACTIVITY: [Isoform SCPx]:
CC Reaction=7-dehydrocholesterol(in) = 7-dehydrocholesterol(out);
CC Xref=Rhea:RHEA:62960, ChEBI:CHEBI:17759;
CC Evidence={ECO:0000269|PubMed:8063752};
CC -!- CATALYTIC ACTIVITY: [Isoform SCP2]:
CC Reaction=7-dehydrocholesterol(in) = 7-dehydrocholesterol(out);
CC Xref=Rhea:RHEA:62960, ChEBI:CHEBI:17759;
CC Evidence={ECO:0000269|PubMed:8063752};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform SCPx]:
CC Kinetic parameters:
CC KM=4.6 uM for 3-oxooctanoyl-CoA {ECO:0000269|PubMed:9325339};
CC KM=4 uM for 3-oxohexadecanoyl-CoA {ECO:0000269|PubMed:9325339};
CC KM=2.9 uM for 3-oxohexadecanedioyl-CoA {ECO:0000269|PubMed:9325339};
CC KM=3 uM for 3-oxo-2-methylpalmitoyl-CoA {ECO:0000269|PubMed:9325339};
CC KM=2.8 uM for 24-oxo-THC-CoA {ECO:0000269|PubMed:9325339};
CC KM=37.7 uM for CoA {ECO:0000269|PubMed:10706581};
CC Vmax=78 umol/min/mg enzyme towards 3-oxooctanoyl-CoA
CC {ECO:0000269|PubMed:9325339};
CC Vmax=20.8 umol/min/mg enzyme towards 3-oxopalmitoyl-CoA
CC {ECO:0000269|PubMed:9325339};
CC Vmax=29.4 umol/min/mg enzyme towards 3-oxohexadecanedioyl-CoA
CC {ECO:0000269|PubMed:9325339};
CC Vmax=38 umol/min/mg enzyme towards 3-oxo-2-oxohexadecanoyl-CoA
CC {ECO:0000269|PubMed:9325339};
CC Vmax=9.6 umol/min/mg enzyme towards 24-oxo-THC-CoA
CC {ECO:0000269|PubMed:9325339};
CC pH dependence:
CC Optimum pH is 7.6 with 3-oxooctanoyl-CoA and 3-oxo-2-methylpalmitoyl-
CC CoA as substrates (PubMed:9325339). Optimum pH is 9.5 with
CC 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestan-26-oyl-CoA as
CC substrate (PubMed:10706581). {ECO:0000269|PubMed:10706581,
CC ECO:0000269|PubMed:9325339};
CC -!- SUBUNIT: [Isoform SCP2]: Interacts with PEX5; the interaction is
CC essential for peroxisomal import. {ECO:0000250|UniProtKB:P22307}.
CC -!- SUBCELLULAR LOCATION: [Isoform SCP2]: Peroxisome
CC {ECO:0000250|UniProtKB:P32020}. Cytoplasm
CC {ECO:0000250|UniProtKB:P22307}. Mitochondrion
CC {ECO:0000250|UniProtKB:P22307}.
CC -!- SUBCELLULAR LOCATION: [Isoform SCPx]: Peroxisome
CC {ECO:0000269|PubMed:8063752, ECO:0000269|PubMed:9325339}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=SCPx; Synonyms=SCP-2/thiolase {ECO:0000303|PubMed:9325339};
CC IsoId=P11915-1; Sequence=Displayed;
CC Name=SCP2;
CC IsoId=P11915-2; Sequence=VSP_018897;
CC -!- TISSUE SPECIFICITY: Liver > intestine > brain > lung, colon, stomach,
CC spleen, kidney, heart and ovary.
CC -!- TISSUE SPECIFICITY: [Isoform SCPx]: Expressed in liver (at protein
CC level). {ECO:0000269|PubMed:8063752}.
CC -!- TISSUE SPECIFICITY: [Isoform SCP2]: Expressed in liver (at protein
CC level). {ECO:0000269|PubMed:8063752}.
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 -!- MISCELLANEOUS: [Isoform SCP2]: Contains a putative mitochondrial
CC transit peptide at positions 1-20. {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the thiolase-like
CC superfamily. Thiolase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA40623.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA43060.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; M62763; AAA40622.1; -; mRNA.
DR EMBL; M62763; AAA40623.1; ALT_INIT; mRNA.
DR EMBL; M57454; AAA42121.1; -; mRNA.
DR EMBL; M57453; AAA42122.1; -; mRNA.
DR EMBL; M58287; AAA41726.1; -; mRNA.
DR EMBL; BC081713; AAH81713.1; -; mRNA.
DR EMBL; M34728; AAA42120.1; -; mRNA.
DR EMBL; X60654; CAA43060.1; ALT_INIT; mRNA.
DR EMBL; X60654; CAA43061.1; -; mRNA.
DR PIR; A39368; A39368.
DR RefSeq; NP_612517.2; NM_138508.4.
DR AlphaFoldDB; P11915; -.
DR SMR; P11915; -.
DR IntAct; P11915; 1.
DR STRING; 10116.ENSRNOP00000015420; -.
DR SwissLipids; SLP:000001233; -. [P11915-1]
DR iPTMnet; P11915; -.
DR PhosphoSitePlus; P11915; -.
DR jPOST; P11915; -.
DR PaxDb; P11915; -.
DR PRIDE; P11915; -.
DR GeneID; 25541; -.
DR KEGG; rno:25541; -.
DR UCSC; RGD:3642; rat. [P11915-1]
DR CTD; 6342; -.
DR RGD; 3642; Scp2.
DR eggNOG; KOG1406; Eukaryota.
DR eggNOG; KOG4170; Eukaryota.
DR InParanoid; P11915; -.
DR OrthoDB; 661265at2759; -.
DR BioCyc; MetaCyc:MON-14332; -.
DR Reactome; R-RNO-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-RNO-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-RNO-389887; Beta-oxidation of pristanoyl-CoA.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR SABIO-RK; P11915; -.
DR PRO; PR:P11915; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:RGD.
DR GO; GO:0031315; C:extrinsic component of mitochondrial outer membrane; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005782; C:peroxisomal matrix; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0050633; F:acetyl-CoA C-myristoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0015485; F:cholesterol binding; ISO:RGD.
DR GO; GO:0120020; F:cholesterol transfer activity; IDA:UniProtKB.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0036042; F:long-chain fatty acyl-CoA binding; ISO:RGD.
DR GO; GO:0070538; F:oleic acid binding; ISO:RGD.
DR GO; GO:0120019; F:phosphatidylcholine transfer activity; IDA:UniProtKB.
DR GO; GO:1904121; F:phosphatidylethanolamine transfer activity; IDA:RGD.
DR GO; GO:0033814; F:propanoyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0050632; F:propionyl-CoA C2-trimethyltridecanoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR GO; GO:0007568; P:aging; IDA:RGD.
DR GO; GO:0008206; P:bile acid metabolic process; IDA:UniProtKB.
DR GO; GO:0071397; P:cellular response to cholesterol; IEP:RGD.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IDA:UniProtKB.
DR GO; GO:0032367; P:intracellular cholesterol transport; ISS:UniProtKB.
DR GO; GO:1901373; P:lipid hydroperoxide transport; ISO:RGD.
DR GO; GO:0007031; P:peroxisome organization; ISO:RGD.
DR GO; GO:0015914; P:phospholipid transport; IBA:GO_Central.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:RGD.
DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; IDA:RGD.
DR GO; GO:1904109; P:positive regulation of cholesterol import; IDA:RGD.
DR GO; GO:0032385; P:positive regulation of intracellular cholesterol transport; ISO:RGD.
DR GO; GO:0010893; P:positive regulation of steroid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0071071; P:regulation of phospholipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0034699; P:response to luteinizing hormone; IEP:RGD.
DR GO; GO:0006694; P:steroid biosynthetic process; 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 Acetylation; Acyltransferase; Alternative initiation; Cytoplasm;
KW Direct protein sequencing; Lipid metabolism; Lipid transport;
KW Lipid-binding; Mitochondrion; Peroxisome; Phosphoprotein;
KW Reference proteome; Transferase; Transport.
FT CHAIN 1..547
FT /note="Sterol carrier protein 2"
FT /id="PRO_0000034097"
FT DOMAIN 433..543
FT /note="SCP2"
FT MOTIF 545..547
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 40
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 132
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 132
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 168
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 177
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 183
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22307"
FT MOD_RES 183
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 211
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 282
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 341
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 341
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 432
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 432
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 438
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22307"
FT MOD_RES 438
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 443
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 443
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 453
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 453
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 464
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 470
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22307"
FT MOD_RES 470
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 479
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 491
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 492
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 511
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 522
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 534
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 544
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT VAR_SEQ 1..404
FT /note="Missing (in isoform SCP2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018897"
FT CONFLICT 12
FT /note="P -> R (in Ref. 2; AAA40622/CAA43061 and 4;
FT AAH81713)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="R -> A (in Ref. 2; AAA40622 and 4; AAH81713)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="S -> T (in Ref. 1; AAA42122)"
FT /evidence="ECO:0000305"
FT CONFLICT 427..428
FT /note="AG -> SV (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="I -> V (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="E -> D (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="E -> Q (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 488
FT /note="D -> N (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="S -> T (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="A -> N (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="S -> N (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 543
FT /note="D -> G (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT SITE P11915-2:20..21
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:O62742"
SQ SEQUENCE 547 AA; 58813 MW; D0D1B435D2DC6AFB CRC64;
MPSVALNSPR LPRVFVVGVG MTKFMKPGGE NSRDYPDLAK EAGQKALADR QIPYSAVEQA
CVGYVYGEST CGQRAIYHSL GLTGIPIINV NNNCSTGSTA LFMAQQLVQG GLANCVLALG
FEKMEKGSLG TKYSDRSNPL EKHIDVLINK YGMSACPFAP QLFGSAGKEH METYGTKVEH
FAKIGWKNHK HSVNNPYSQF QDEYSLDEIM KSRPVFDFLT VLQCCPTSDG AAAAIVSSEE
FVQKHGLQSK AVEIVAQEMV TDMPSTFEEK SVIKMVGYDM SKEAARKCYE KSGLGPSDVD
VIELHDCFST NELLTYEALG LCPEGQGGAL VDRGDNTYGG KWVINPSGGL ISKGHPLGAT
GLAQCAELCW QLRGEAGKRQ VPGAKVALQH NLGLGGAAVV TLYRMGFPEA ASSFRTHQIS
AAPTSSAGDG FKANLIFKEI EKKLEEEGEE FVKKIGGIFA FKVKDGPGGK EATWVVDVKN
GKGSVLPDSD KKADCTITMA DSDLLALMTG KMNPQSAFFQ GKLKIAGNMG LAMKLQSLQL
QPDKAKL
