ID A0AA35XCI7_GEOBA Unreviewed; 400 AA. AC A0AA35XCI7; DT 24-JAN-2024, integrated into UniProtKB/TrEMBL. DT 24-JAN-2024, sequence version 1. DT 24-JUL-2024, entry version 4. 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 -!- 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}. Peroxisome CC {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 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; IPR020617; Thiolase_C. 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; PF02803; Thiolase_C; 1. DR SUPFAM; SSF55718; SCP-like; 1. DR SUPFAM; SSF53901; Thiolase-like; 2. DR PROSITE; PS00737; THIOLASE_2; 1. PE 4: Predicted; KW Lipid transport {ECO:0000256|ARBA:ARBA00023055}; KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}; KW Peroxisome {ECO:0000256|ARBA:ARBA00023140}; KW Reference proteome {ECO:0000313|Proteomes:UP001174909}; KW Transport {ECO:0000256|ARBA:ARBA00022448}. FT DOMAIN 144..244 FT /note="Thiolase C-terminal" FT /evidence="ECO:0000259|Pfam:PF02803" 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 //