ID A0A7N9AQI6_9TELE Unreviewed; 528 AA.
AC A0A7N9AQI6;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 18-JUN-2025, entry version 21.
DE RecName: Full=Sterol carrier protein 2 {ECO:0000256|ARBA:ARBA00014545};
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=Acetyl-CoA C-myristoyltransferase {ECO:0000256|ARBA:ARBA00032093};
DE AltName: Full=Non-specific lipid-transfer protein {ECO:0000256|ARBA:ARBA00030851};
DE AltName: Full=Propanoyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00032316};
DE AltName: Full=SCP-2/3-oxoacyl-CoA thiolase {ECO:0000256|ARBA:ARBA00030531};
DE AltName: Full=SCP-2/thiolase {ECO:0000256|ARBA:ARBA00031275};
DE AltName: Full=SCP-chi {ECO:0000256|ARBA:ARBA00031346};
DE AltName: Full=Sterol carrier protein X {ECO:0000256|ARBA:ARBA00033178};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000037459.1, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000037459.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: Mediates the transfer of all common phospholipids,
CC cholesterol and gangliosides from the endoplasmic reticulum to the
CC plasma membrane. May play a role in regulating steroidogenesis.
CC Stimulates the microsomal conversion of 7-dehydrocholesterol to
CC cholesterol. Also binds fatty acids and fatty acyl Coenzyme A (CoA)
CC such as phytanoyl-CoA. Involved in the regulation phospholipid
CC synthesis in endoplasmic reticulum enhancing the incorporation of
CC exogenous fatty acid into glycerides. Seems to stimulate the rate-
CC limiting step in phosphatidic acid formation mediated by GPAT3.
CC Isoforms SCP2 and SCPx cooperate in peroxisomal oxidation of certain
CC naturally occurring tetramethyl-branched fatty acyl-CoAs.
CC {ECO:0000256|ARBA:ARBA00045738}.
CC -!- FUNCTION: Plays a crucial role in the peroxisomal oxidation of
CC branched-chain fatty acids. Catalyzes the last step of the peroxisomal
CC beta-oxidation of branched chain fatty acids and the side chain of the
CC bile acid intermediates di- and trihydroxycoprostanic acids (DHCA and
CC THCA). Also active with medium and long straight chain 3-oxoacyl-CoAs.
CC Stimulates the microsomal conversion of 7-dehydrocholesterol to
CC cholesterol and transfers phosphatidylcholine and 7-dehydrocholesterol
CC between membrances, in vitro. Isoforms SCP2 and SCPx cooperate in
CC peroxisomal oxidation of certain naturally occurring tetramethyl-
CC branched fatty acyl-CoAs. {ECO:0000256|ARBA:ARBA00045994}.
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 = tetradecanedioyl-CoA +
CC acetyl-CoA; Xref=Rhea:RHEA:40343, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:77081, ChEBI:CHEBI:77084;
CC Evidence={ECO:0000256|ARBA:ARBA00049306};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40344;
CC Evidence={ECO:0000256|ARBA:ARBA00049306};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-dehydrocholesterol(in) = 7-dehydrocholesterol(out);
CC Xref=Rhea:RHEA:62960, ChEBI:CHEBI:17759;
CC Evidence={ECO:0000256|ARBA:ARBA00029287};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + acetyl-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:ARBA00049178};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566;
CC Evidence={ECO:0000256|ARBA:ARBA00049178};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + acetyl-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:ARBA00048553};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31113;
CC Evidence={ECO:0000256|ARBA:ARBA00048553};
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=decanoyl-CoA + acetyl-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:ARBA00048004};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31185;
CC Evidence={ECO:0000256|ARBA:ARBA00048004};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + acetyl-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:ARBA00049270};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31093;
CC Evidence={ECO:0000256|ARBA:ARBA00049270};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + acetyl-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:ARBA00049268};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35281;
CC Evidence={ECO:0000256|ARBA:ARBA00049268};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexanoyl-CoA + acetyl-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:ARBA00048001};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31205;
CC Evidence={ECO:0000256|ARBA:ARBA00048001};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=octanoyl-CoA + acetyl-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:ARBA00049542};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31089;
CC Evidence={ECO:0000256|ARBA:ARBA00049542};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=tetradecanoyl-CoA + acetyl-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:ARBA00047485};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18163;
CC Evidence={ECO:0000256|ARBA:ARBA00047485};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Peroxisome
CC {ECO:0000256|ARBA:ARBA00004275}.
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DR AlphaFoldDB; A0A7N9AQI6; -.
DR Ensembl; ENSMAMT00000054567.1; ENSMAMP00000037459.1; ENSMAMG00000000798.2.
DR GeneTree; ENSGT00940000154327; -.
DR Proteomes; UP000261640; Unplaced.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd00826; nondecarbox_cond_enzymes; 1.
DR FunFam; 3.40.47.10:FF:000016; Non-specific lipid-transfer protein; 1.
DR FunFam; 3.30.1050.10:FF:000001; Putative Non-specific lipid-transfer protein; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.30.1050.10; SCP2 sterol-binding domain; 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; IPR055140; Thiolase_C_2.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; NF006102; PRK08256.1; 1.
DR PANTHER; PTHR42870; ACETYL-COA C-ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR42870:SF1; NON-SPECIFIC LIPID-TRANSFER PROTEIN-LIKE 2; 1.
DR Pfam; PF02036; SCP2; 1.
DR Pfam; PF22691; Thiolase_C_1; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR SUPFAM; SSF55718; SCP-like; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
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 Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 21..224
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 263..379
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF22691"
FT DOMAIN 420..519
FT /note="SCP2"
FT /evidence="ECO:0000259|Pfam:PF02036"
SQ SEQUENCE 528 AA; 57006 MW; 5213DE544652C34A CRC64;
MLTLSNSVCV KFDKPGANDY PDMAKKAGQR ALEDARIPYS AIEQACVGYV YGDSTCGQRA
IYHGLGLTGI PIINVNNNCS TGSTALFMAR QLVLGGLADC VLALGFEKME RGSLSSKYMD
RTNPMDKHME VMINRYGMVA APAAPQMFGN AGREHMEKYG TKPEHFAKIA WKNHKHSTNN
PYSQFQDEYT LEQVMNSRKV FDFLTLLQCC PTSDGAGAAI LASEGFVRKH GLENQAVEIV
AQEMVTDLAS TFEENSCIKM VGYDMSRQAA KKCYESSGLK PSDVDVIELH DCFSANELIT
YEALGLCTEG KAGELIDRGD NTYGGKFVIN PSGGLISKGH PLGATGLAQC AELCWQLRGQ
AGRRQVPGAK VALQHNIGLG GAVVVTLYKM GFPQNARSHL SAVPTGSDSG LEGFKAYPVF
KEIKKQLKKE GEQLVKKIGG VFAFQVKDGP GGKEGTWVVD VKNGKGSVTT GKKADCTISM
SDEDLLDLMT GKLNPQTAFF KGKLKITGNM GMALKLQNLQ VTPGKAKL
//
