SCP2_CHICK
ID SCP2_CHICK Reviewed; 547 AA.
AC Q07598;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Sterol carrier protein 2;
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;
DE Flags: Fragment;
GN Name=SCP2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=White leghorn; TISSUE=Liver;
RX PubMed=8323294; DOI=10.1006/abbi.1993.1351;
RA Pfeifer S.M., Sakuragi N., Ryan A., Johnson A.L., Deeley R.G.,
RA Billheimer J.T., Baker M.E., Strauss J.F. III;
RT "Chicken sterol carrier protein 2/sterol carrier protein x: cDNA cloning
RT reveals evolutionary conservation of structure and regulated expression.";
RL Arch. Biochem. Biophys. 304:287-293(1993).
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 -!- 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=Q07598-1; Sequence=Displayed;
CC Name=SCP2;
CC IsoId=Q07598-2; Sequence=VSP_018898;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the liver, intestine
CC and ovarian granulosa cells.
CC -!- DEVELOPMENTAL STAGE: [Isoform SCPx]: Levels remain unchanged during day
CC 20 embryo to 4 weeks post-hatch. {ECO:0000269|PubMed:8323294}.
CC -!- DEVELOPMENTAL STAGE: [Isoform SCP2]: A 10-fold increase in expression
CC levels is seen by 1 week post-hatch and declines slightly between 3 and
CC 4 weeks post-hatch. {ECO:0000269|PubMed:8323294}.
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}.
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DR EMBL; L09231; AAA02488.1; -; mRNA.
DR PIR; S34744; S34744.
DR RefSeq; NP_001292129.1; NM_001305200.1.
DR AlphaFoldDB; Q07598; -.
DR SMR; Q07598; -.
DR STRING; 9031.ENSGALP00000017306; -.
DR PaxDb; Q07598; -.
DR PRIDE; Q07598; -.
DR GeneID; 396550; -.
DR KEGG; gga:396550; -.
DR CTD; 6342; -.
DR VEuPathDB; HostDB:geneid_396550; -.
DR eggNOG; KOG1406; Eukaryota.
DR eggNOG; KOG4170; Eukaryota.
DR InParanoid; Q07598; -.
DR OrthoDB; 661265at2759; -.
DR PhylomeDB; Q07598; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
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: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; IEA:UniProtKB-EC.
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:0006869; P:lipid transport; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Acyltransferase; Alternative initiation; Cytoplasm; Endoplasmic reticulum;
KW Lipid metabolism; Lipid transport; Lipid-binding; Mitochondrion;
KW Peroxisome; Reference proteome; Transferase; Transport.
FT CHAIN <1..547
FT /note="Sterol carrier protein 2"
FT /id="PRO_0000034089"
FT DOMAIN 433..543
FT /note="SCP2"
FT MOTIF 545..547
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT SITE 494
FT /note="Essential for transport of lipids"
FT /evidence="ECO:0000250"
FT VAR_SEQ <1..407
FT /note="Missing (in isoform SCP2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018898"
FT NON_TER 1
SQ SEQUENCE 547 AA; 58691 MW; CAFCDDE4A1C1B3B8 CRC64;
ARVCEERGGP AAIMQRRVFV VGVGMTKFAK PSENSVDYPD LAKEAGQKAL ADAGIPYSAV
EQACVGYVYG DSTCGQRAIY HGLGLTGIPI INVNNNCATG STALFMSRQL VEGGLADCVL
ALGFERMAKG SLASGFSDRT NPMDKHLEIM INKYGLASAP ITPQMFANAG KEHMEKYGTN
PEYFAKIAWK NHSHSTNNPY SQFQKKYTLD EVLQSRKVFD FLTVLQCCPT SNGAAAAILA
SEDFVKRHKL QPQAVEILAQ VMATDYPSTF EENSCMKMVG YDMTKKAAEK CFKKAGLKPT
DVDVIELHDC FSVNEFITYE ALGLCPEGKA CDLIDRGDNT YGGKWVINPS GGLISKGHPL
GATGLAQSAE LCWQLRGLAG RREVGGARRA LQHNLGLGGA VVVTLYAMGF PGAASDGGVT
AVPLSAAVDG FKSHLVFKEI EKKLQEEGEQ FVKKIGGVFA FKIKDGPGGK EATWVVDVKN
GKGSVAVNSD KKADCTITMA DTDLLALMTG KMNPQTAFFQ GKLKISGNMG MAMKLQNLQL
QPGKAKL
