ID A0AA35XCI7_GEOBA Unreviewed; 400 AA. AC A0AA35XCI7; DT 24-JAN-2024, integrated into UniProtKB/TrEMBL. DT 24-JAN-2024, sequence version 1. DT 27-NOV-2024, entry version 6. DE RecName: Full=Sterol carrier protein 2 {ECO:0000256|ARBA:ARBA00014545}; DE EC=2.3.1.155 {ECO:0000256|ARBA:ARBA00024058}; DE EC=2.3.1.176 {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 ORFNames=GBAR_LOCUS28677 {ECO:0000313|EMBL:CAI8052434.1}; OS Geodia barretti (Barrett's horny sponge). OC Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha; OC Tetractinellida; Astrophorina; Geodiidae; Geodia. OX NCBI_TaxID=519541 {ECO:0000313|EMBL:CAI8052434.1, ECO:0000313|Proteomes:UP001174909}; RN [1] {ECO:0000313|EMBL:CAI8052434.1} RP NUCLEOTIDE SEQUENCE. RA Steffen K., Cardenas P.; RL Submitted (MAR-2023) to the EMBL/GenBank/DDBJ databases. 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:CAI8052434.1}. 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 EMBL; CASHTH010004013; CAI8052434.1; -; Genomic_DNA. DR Proteomes; UP001174909; Unassembled WGS sequence. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell. DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. 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 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; IPR055140; Thiolase_C_2. DR InterPro; IPR020613; Thiolase_CS. 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 SUPFAM; SSF55718; SCP-like; 1. DR SUPFAM; SSF53901; Thiolase-like; 2. 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 Reference proteome {ECO:0000313|Proteomes:UP001174909}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Transport {ECO:0000256|ARBA:ARBA00022448}. FT DOMAIN 132..255 FT /note="Thiolase C-terminal" FT /evidence="ECO:0000259|Pfam:PF22691" FT DOMAIN 296..392 FT /note="SCP2" FT /evidence="ECO:0000259|Pfam:PF02036" SQ SEQUENCE 400 AA; 42891 MW; A23CB4B1A89B112E CRC64; MDRHVDVLAN THGIAAAPIT PQMFASAGKE HMQKYGTTAE HMAKIAWKNH KHSVNNPNSQ FRKEYSLDEI RSSRMVHEPL TMLQCCPTSD GSACAILCSE EFAKKHGLTD KAVEILAIEM ATDLPSTFSE RSCMKMVGYD MTRMASDKAY KKAGLCPRDV QVVELHDCFS ANELISYEAL GLCQEGRAGE MVDHGNNTYG GKYVVNPSGG LISKGHPLGA TGLAQCAELC WQLRGEAGKR QVPGAKVGLQ HNIGLGGAVV VALYRLGYPS TRSAVGMAPA GGSSLQCDPV FDLIAEKVKE EGASMVKKIK GSFLFKIKGS DGKVYEWLVD LKSPPGSVTK GTGLKGNCTI AMTDSNFMDL VTGKIGAQKA FFEGKLKISG NTALALKLQT VMPKPGQAKL //