ID A0A670I7T1_PODMU Unreviewed; 540 AA.
AC A0A670I7T1;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 17.
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};
GN Name=SCP2 {ECO:0000313|Ensembl:ENSPMRP00000007719.1};
OS Podarcis muralis (Wall lizard) (Lacerta muralis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Laterata;
OC Lacertibaenia; Lacertidae; Podarcis.
OX NCBI_TaxID=64176 {ECO:0000313|Ensembl:ENSPMRP00000007719.1, ECO:0000313|Proteomes:UP000472272};
RN [1] {ECO:0000313|Ensembl:ENSPMRP00000007719.1, ECO:0000313|Proteomes:UP000472272}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30819892; DOI=10.1073/pnas.1820320116;
RA Andrade P., Pinho C., Perez I de Lanuza G., Afonso S., Brejcha J.,
RA Rubin C.J., Wallerman O., Pereira P., Sabatino S.J., Bellati A.,
RA Pellitteri-Rosa D., Bosakova Z., Bunikis I., Carretero M.A., Feiner N.,
RA Marsik P., Pauperio F., Salvi D., Soler L., While G.M., Uller T., Font E.,
RA Andersson L., Carneiro M.;
RT "Regulatory changes in pterin and carotenoid genes underlie balanced color
RT polymorphisms in the wall lizard.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:5633-5642(2019).
RN [2] {ECO:0000313|Ensembl:ENSPMRP00000007719.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 = 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:0000256|ARBA:ARBA00024540};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40344;
CC Evidence={ECO:0000256|ARBA:ARBA00024540};
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=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:0000256|ARBA:ARBA00024485};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566;
CC Evidence={ECO:0000256|ARBA:ARBA00024485};
CC -!- CATALYTIC ACTIVITY:
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:0000256|ARBA:ARBA00024476};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31113;
CC Evidence={ECO:0000256|ARBA:ARBA00024476};
CC -!- CATALYTIC ACTIVITY:
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:0000256|ARBA:ARBA00024559};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31185;
CC Evidence={ECO:0000256|ARBA:ARBA00024559};
CC -!- CATALYTIC ACTIVITY:
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:0000256|ARBA:ARBA00024598};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31093;
CC Evidence={ECO:0000256|ARBA:ARBA00024598};
CC -!- CATALYTIC ACTIVITY:
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:0000256|ARBA:ARBA00024549};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35281;
CC Evidence={ECO:0000256|ARBA:ARBA00024549};
CC -!- CATALYTIC ACTIVITY:
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:0000256|ARBA:ARBA00024462};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31205;
CC Evidence={ECO:0000256|ARBA:ARBA00024462};
CC -!- CATALYTIC ACTIVITY:
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:0000256|ARBA:ARBA00024542};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31089;
CC Evidence={ECO:0000256|ARBA:ARBA00024542};
CC -!- CATALYTIC ACTIVITY:
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:0000256|ARBA:ARBA00024455};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18163;
CC Evidence={ECO:0000256|ARBA:ARBA00024455};
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=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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Peroxisome
CC {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|RuleBase:RU003557}.
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DR AlphaFoldDB; A0A670I7T1; -.
DR Ensembl; ENSPMRT00000008262.1; ENSPMRP00000007719.1; ENSPMRG00000005215.1.
DR GeneTree; ENSGT00940000154327; -.
DR OMA; PSLYAMM; -.
DR OrthoDB; 1799125at2759; -.
DR Proteomes; UP000472272; Chromosome 6.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0050633; F:acetyl-CoA C-myristoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
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: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 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; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
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; PF02803; Thiolase_C; 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 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
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:UP000472272};
KW Transferase {ECO:0000256|RuleBase:RU003557};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 10..236
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 279..377
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT DOMAIN 430..531
FT /note="SCP2"
FT /evidence="ECO:0000259|Pfam:PF02036"
SQ SEQUENCE 540 AA; 58613 MW; FF5C3554058543C6 CRC64;
MAPSRLGRRV FVVGVGMTKF EKPGSRENFD YPDMAKEAGQ KALADAGVPY SSVEQACVGY
VYGDSTCGQR AIYHSLGLTG IPIMNVNNNC STGSTALFMA RQLVQGGMAN CVLALGFEKM
ARGSLSSQFM DRVNPMDKHM EVMISKYDLA AAPVAPQLFG NAGKEHMEKY GSKQEHFAKI
AWKNHKHSTN NPNSQFQKEY SLDEVLQSRK VFDYLTILQC CPTSDGAAAA VLASEEFVRK
NGLESRAVEI VAQEMMTDLP STFVENSLIK AVGFDMTKEA AKRCYSKAGL KPEDVDVIEL
HDCFSANELI TYEALGLCPE GGAGELIDRG DNTYGGKWVI NPSGGLISKG HPLGATGLAQ
CAELCWQLRG EAGKRQVPCA KVALQHNLGL GGAVVITLYR MGFPEAARNR QIQAIPTRAA
VDGFKADFVF KEIEKKLQEE GEQYVKKIGG IFAFKVKEGP GGKEATWVVD VKNGKGCVDF
DSDKKADCTI TMADADLLAL MTGKMNPQTA FFQGKLKISG NMGMAMKLQN LQLQPVKAKL
//
