ID A0A1I8BGG7_MELHA Unreviewed; 504 AA. AC A0A1I8BGG7; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 27-NOV-2024, 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}; OS Meloidogyne hapla (Root-knot nematode worm). OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae; OC Meloidogyne. OX NCBI_TaxID=6305 {ECO:0000313|Proteomes:UP000095281, ECO:0000313|WBParaSite:MhA1_Contig2306.frz3.gene2}; RN [1] {ECO:0000313|WBParaSite:MhA1_Contig2306.frz3.gene2} RP IDENTIFICATION. RG WormBaseParasite; RL Submitted (NOV-2016) 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 AlphaFoldDB; A0A1I8BGG7; -. DR WBParaSite; MhA1_Contig2306.frz3.gene2; MhA1_Contig2306.frz3.gene2; MhA1_Contig2306.frz3.gene2. DR OMA; PSLYAMM; -. DR Proteomes; UP000095281; Unplaced. 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:000126; Protein CBG20965; 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 35..203 FT /note="Thiolase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00108" FT DOMAIN 246..359 FT /note="Thiolase C-terminal" FT /evidence="ECO:0000259|Pfam:PF22691" FT DOMAIN 392..496 FT /note="SCP2" FT /evidence="ECO:0000259|Pfam:PF02036" SQ SEQUENCE 504 AA; 55582 MW; 43067598F765F5C3 CRC64; MTKFTKPLTS GKDYPELVKE AATASYMYGG SCCGQRALYE IGLTGIPIFN LNNACASGSS GIFLCKQIIE SGNVDLMLAV GFEKMQPGSL ENSPEHLDDR ALPVEKHIQL MADTYGLQAA PITSQMFGNA GREHMEKYGT KREHFAKIAW KNHLHSVHNA KSQFQRHFSL DEVVNARKIY DYMGLFECSP TSDGAAAVII CSEKFIEQNP HLKPQAVEIV GIELGTDEPS VFAENSNIKM VGFDLIKKIS ERLYAKTGVD PSQIQVIELH DCFAPNELIT YEALGLCPIG KAGEIVDKGD NTYGGKWVIN PSGGLISKGH PIGATGIAQA VELCNQLRKR CGARQVNNAV YALQHNIGIG GAGVVAIYKL GFPELAKNNE EMNIKFKSDV IFDEIKERAI QEKDLIKQVG SCFKFIITNS DLNKKREWIV DLKCSPPFVG LSDKSKSKPE VTISLDDEVL INLAKGKLKP DQAFLQRKLK ISGDFKKAMK LKEILDPNRL KSRI //