ID A0A7L4ARC1_9CHAR Unreviewed; 502 AA. AC A0A7L4ARC1; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 27-NOV-2024, entry version 15. 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}; DE Flags: Fragment; GN Name=Scp2 {ECO:0000313|EMBL:NXW28207.1}; GN ORFNames=PHASIM_R00346 {ECO:0000313|EMBL:NXW28207.1}; OS Phaetusa simplex (large-billed tern). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Neoaves; Charadriiformes; Laridae; OC Phaetusa. OX NCBI_TaxID=297813 {ECO:0000313|EMBL:NXW28207.1, ECO:0000313|Proteomes:UP000556165}; RN [1] {ECO:0000313|EMBL:NXW28207.1, ECO:0000313|Proteomes:UP000556165} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B10K-DU-009-16 {ECO:0000313|EMBL:NXW28207.1}; RC TISSUE=Muscle {ECO:0000313|EMBL:NXW28207.1}; RA Zhang G.; RT "Bird 10,000 Genomes (B10K) Project - Family phase."; RL Submitted (SEP-2019) 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:NXW28207.1}. 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; VZZW01000100; NXW28207.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7L4ARC1; -. DR Proteomes; UP000556165; 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; cd00826; nondecarbox_cond_enzymes; 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 Reference proteome {ECO:0000313|Proteomes:UP000556165}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Transport {ECO:0000256|ARBA:ARBA00022448}. FT DOMAIN 2..197 FT /note="Thiolase N-terminal" FT /evidence="ECO:0000259|Pfam:PF00108" FT DOMAIN 229..352 FT /note="Thiolase C-terminal" FT /evidence="ECO:0000259|Pfam:PF22691" FT DOMAIN 392..493 FT /note="SCP2" FT /evidence="ECO:0000259|Pfam:PF02036" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:NXW28207.1" FT NON_TER 502 FT /evidence="ECO:0000313|EMBL:NXW28207.1" SQ SEQUENCE 502 AA; 53829 MW; D840EB332DBA70B7 CRC64; GQKALADAGI PYSAVQQACV GYVYGDSTCG QRAIYHGLGL TGIPIINVNN NCATGSTALF MARQLVEGGL ADCVLALGFE RMAKGSLASG FSDRTNPMDK HLEIMINKYG LASAPIAPQM FANAGKEHME KYGTNPEYFA KIAWKNHSHS TNNPYSQFQK EYTLDEVLHS RKIFDFLTVL QCCPTSNGAA AAILASETFV KRHKLQPKAV EILAQVMATD FPSTFEENSC MKMVGYDMTK KAAEKCFEKA GLKPTDVDVI ELHDCFSVNE FITYEALGLC PEGRACDLID RGDNTYGGKW VINPSGGLIS KGHPLGATGL AQCAELCWQL RGLAGRRQVP GAKVALQHNL GLGGAVVVTL YGMGFPGAAS TGRIAAVPLS AAVDGFKSHL VFKEIEKKLQ EEGEQFVKKI GGVFAFKIKD GPGGKEATWI VDVKNGKGSV AVNSDKKADC TITMADTDLL ALMTGKMNPQ TAFFQGKLKV SGNMGMAMKL QNLQLQPGKA KL //