SCP2_BOVIN
ID SCP2_BOVIN Reviewed; 543 AA.
AC P07857; Q3SYV0;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 25-MAY-2022, entry version 143.
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;
DE Short=NSL-TP;
DE AltName: Full=Propanoyl-CoA C-acyltransferase;
DE EC=2.3.1.176 {ECO:0000250|UniProtKB:P11915};
DE AltName: Full=SCP-2/3-oxoacyl-CoA thiolase;
DE AltName: Full=SCP-2/thiolase;
DE EC=2.3.1.16 {ECO:0000250|UniProtKB:P11915};
DE AltName: Full=SCP-chi;
DE AltName: Full=SCPX;
DE AltName: Full=Sterol carrier protein X;
DE Short=SCP-X;
GN Name=SCP2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 421-541.
RC TISSUE=Liver;
RX PubMed=3977925; DOI=10.1016/s0006-291x(85)80163-7;
RA Westerman J., Wirtz K.W.A.;
RT "The primary structure of the nonspecific lipid transfer protein (sterol
RT carrier protein 2) from bovine liver.";
RL Biochem. Biophys. Res. Commun. 127:333-338(1985).
CC -!- FUNCTION: [Isoform SCPx]: Plays a crucial role in the peroxisomal
CC oxidation of branched-chain fatty acids. Catalyzes the last step of the
CC peroxisomal beta-oxidation of branched chain fatty acids and the side
CC chain of the bile acid intermediates di- and trihydroxycoprostanic
CC acids (DHCA and THCA) (By similarity). Also active with medium and long
CC straight chain 3-oxoacyl-CoAs. Stimulates the microsomal conversion of
CC 7-dehydrocholesterol to cholesterol and transfers phosphatidylcholine
CC and 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 (By
CC similarity). {ECO:0000250|UniProtKB:P11915,
CC ECO:0000250|UniProtKB:P22307, ECO:0000250|UniProtKB:P32020}.
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 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. Isoforms SCP2 and SCPx cooperate in
CC peroxisomal oxidation of certain naturally occurring tetramethyl-
CC branched fatty acyl-CoAs (By similarity).
CC {ECO:0000250|UniProtKB:P11915, ECO:0000250|UniProtKB:P22307,
CC ECO:0000250|UniProtKB:P32020}.
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:0000250|UniProtKB:P22307};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16867;
CC Evidence={ECO:0000250|UniProtKB:P22307};
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: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:P22307};
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:0000250|UniProtKB:P11915};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10410;
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]: Peroxisome
CC {ECO:0000250|UniProtKB:P32020}. Cytoplasm
CC {ECO:0000250|UniProtKB:P22307}. Mitochondrion
CC {ECO:0000250|UniProtKB:P22307}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P32020}. Mitochondrion
CC {ECO:0000250|UniProtKB:P32020}.
CC -!- SUBCELLULAR LOCATION: [Isoform SCPx]: Peroxisome
CC {ECO:0000250|UniProtKB:P11915}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=SCPx;
CC IsoId=P07857-1; Sequence=Displayed;
CC Name=SCP2;
CC IsoId=P07857-2; Sequence=VSP_018894;
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}.
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DR EMBL; BC103370; AAI03371.1; -; mRNA.
DR RefSeq; NP_001029162.2; NM_001033990.3. [P07857-1]
DR AlphaFoldDB; P07857; -.
DR SMR; P07857; -.
DR STRING; 9913.ENSBTAP00000004879; -.
DR PaxDb; P07857; -.
DR PeptideAtlas; P07857; -.
DR PRIDE; P07857; -.
DR GeneID; 508918; -.
DR KEGG; bta:508918; -.
DR CTD; 6342; -.
DR eggNOG; KOG1406; Eukaryota.
DR eggNOG; KOG4170; Eukaryota.
DR InParanoid; P07857; -.
DR OrthoDB; 661265at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005782; C:peroxisomal matrix; ISS:UniProtKB.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IBA:GO_Central.
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:0120020; F:cholesterol transfer activity; ISS:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0120019; F:phosphatidylcholine transfer activity; ISS:UniProtKB.
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:0008206; P:bile acid metabolic process; ISS:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0032367; P:intracellular cholesterol transport; ISS:UniProtKB.
DR GO; GO:1901373; P:lipid hydroperoxide transport; IDA:UniProtKB.
DR GO; GO:0032385; P:positive regulation of intracellular cholesterol transport; IDA:UniProtKB.
DR GO; GO:0071071; P:regulation of phospholipid biosynthetic process; ISS:UniProtKB.
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..543
FT /note="Sterol carrier protein 2"
FT /id="PRO_0000045842"
FT DOMAIN 429..539
FT /note="SCP2"
FT MOTIF 541..543
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 39
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 167
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 172
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 182
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22307"
FT MOD_RES 182
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 281
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 340
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 340
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 428
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 428
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 434
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22307"
FT MOD_RES 434
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 439
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 439
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 449
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 449
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 460
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 466
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P22307"
FT MOD_RES 466
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 475
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 487
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 488
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 507
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 518
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 530
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT MOD_RES 540
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P32020"
FT VAR_SEQ 1..403
FT /note="Missing (in isoform SCP2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018894"
FT SITE P07857-2:20..21
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:O62742"
SQ SEQUENCE 543 AA; 58577 MW; 4EFAE214F4A2CA99 CRC64;
MSLVASQSPL RNRVFVVGVG MTKFTKPGVE NRDYPDLAKE AGQKALADAQ IPYSAVEQAC
IGYVYGDSTS GQRAIYHSLG LTGIPIINVN NNCSTGSTAL FMARQLIQGG LADCVLALGF
EKMVKGPIAV NIQDKANPID KHIEVMVNKY GLSPSPVAPQ MFGNAGKEHM EKYGTTLEHF
AKIGWKNHKH SVNNPYSQFQ KEYSLDEVMT SRKIFDFLTV LQCCPTSDGA AAAILASEAF
VQKHNLKPKA VEILAQEMVT DMPSSFEGKS IIKMVGFDMS KEAARRCYEK SGLRPSDIDV
IELHDCFSAN ELITYEALGL CPEGQGGKLV ERGDNTYGGK WVINPSGGLI SKGHPLGATG
LAQCVELCWH LRGEAGKRQV PGAKVALQHN IGIGGAVVVT LYKMGFPEAA RTHQIEAAPT
SSSVDGFKAN LVFKEIEKKL EDEGEQFVKK IGGIFAFKVK DGPGGKEATW VVDVKNGKGS
VLPNSDKKAD CTITMADSDL LALMTGKMNP QTAFFQGKLK INGNMGLAMK LQNLQLQPGK
AKL
