ID   A0A1I8PL46_STOCA        Unreviewed;       542 AA.
AC   A0A1I8PL46;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-NOV-2024, entry version 33.
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=106095367 {ECO:0000313|EnsemblMetazoa:SCAU009051-PA};
OS   Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Stomoxys.
OX   NCBI_TaxID=35570 {ECO:0000313|EnsemblMetazoa:SCAU009051-PA, ECO:0000313|Proteomes:UP000095300};
RN   [1] {ECO:0000313|EnsemblMetazoa:SCAU009051-PA}
RP   IDENTIFICATION.
RC   STRAIN=USDA {ECO:0000313|EnsemblMetazoa:SCAU009051-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) 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: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=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:ARBA00024485};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566;
CC         Evidence={ECO:0000256|ARBA:ARBA00024485};
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:ARBA00024476};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31113;
CC         Evidence={ECO:0000256|ARBA:ARBA00024476};
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:ARBA00024559};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31185;
CC         Evidence={ECO:0000256|ARBA:ARBA00024559};
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:ARBA00024598};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31093;
CC         Evidence={ECO:0000256|ARBA:ARBA00024598};
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:ARBA00024549};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35281;
CC         Evidence={ECO:0000256|ARBA:ARBA00024549};
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:ARBA00024462};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31205;
CC         Evidence={ECO:0000256|ARBA:ARBA00024462};
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:ARBA00024542};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31089;
CC         Evidence={ECO:0000256|ARBA:ARBA00024542};
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: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       Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
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   RefSeq; XP_013118054.1; XM_013262600.1.
DR   AlphaFoldDB; A0A1I8PL46; -.
DR   STRING; 35570.A0A1I8PL46; -.
DR   EnsemblMetazoa; SCAU009051-RA; SCAU009051-PA; SCAU009051.
DR   GeneID; 106095367; -.
DR   KEGG; scac:106095367; -.
DR   CTD; 44183; -.
DR   VEuPathDB; VectorBase:SCAU009051; -.
DR   OrthoDB; 1799125at2759; -.
DR   Proteomes; UP000095300; Unassembled WGS sequence.
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:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   CDD; cd00829; SCP-x_thiolase; 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   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   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          6..231
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          270..386
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF22691"
FT   DOMAIN          428..528
FT                   /note="SCP2"
FT                   /evidence="ECO:0000259|Pfam:PF02036"
SQ   SEQUENCE   542 AA;  58982 MW;  7AE609C27AE14939 CRC64;
     MVKTRVYVVG VGMTKFEKPG RRSDVDYPDF AKEAITKALA DAKISYNEVQ QATVGYVYGD
     STSGQRALYE VGMTGIPVFN VNNNCSTGSS ALYLGKQIIE SGNADCVLAF GFEKMERGSL
     SAKYFDRANP MEHHISIMSE LAEIGPGPMA AQIFGNAGKE HMKKYGTKPE HFGKIAWKNH
     KHSVNNPYSQ FRDEYTLEQI MKSPTVVEGV LTKLQCCPTS DGAGAAILAS EAFVHRFGLE
     AQAVEIVGME MASDPESTFK DRSLMKIAGY DMTKMAAQRL FGKCGYKPTD VQVVELHDCF
     SANELITYEA LGLCPEGGAG EMIDRGDNTY GGKYVINPSG GLISKGHPLG ATGLAQCAEM
     CWQLRGLAEK RQVKDCKLAL QHNLGLGGAV VVTLYRLGFP TAAGVKYNLT SATHPDGEGF
     KVTPLLKLLE QAMQEDQDNL IEKVRAIYGF KVTNGPGGQI GFWTINAKEG KGKITYNGKE
     KCDVTFVISD EDVTELMTGK LPPQKAFFQG KVKIQGNMGL AMKLMDLQRS AQGRIDALRA
     KL
//