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 //