ID A0A1I8PL46_STOCA Unreviewed; 542 AA. AC A0A1I8PL46; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 13-SEP-2023, entry version 28. 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 -!- 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}. CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family. CC {ECO:0000256|RuleBase:RU003557}. 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 VEuPathDB; VectorBase:SCAU009051; -. DR OrthoDB; 1799125at2759; -. DR Proteomes; UP000095300; Unassembled WGS sequence. DR GO; GO:0005739; C:mitochondrion; 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 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003557}; KW Transport {ECO:0000256|ARBA:ARBA00022448}. FT DOMAIN 6..231 FT /note="Thiolase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00108" FT DOMAIN 275..366 FT /note="Thiolase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02803" 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 //