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Database: UniProt
Entry: A0A4W6FRR9_LATCA
LinkDB: A0A4W6FRR9_LATCA
Original site: A0A4W6FRR9_LATCA 
ID   A0A4W6FRR9_LATCA        Unreviewed;       544 AA.
AC   A0A4W6FRR9;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=scp2a {ECO:0000313|Ensembl:ENSLCAP00010053300.1};
OS   Lates calcarifer (Barramundi) (Holocentrus calcarifer).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangaria incertae sedis; Centropomidae; Lates.
OX   NCBI_TaxID=8187 {ECO:0000313|Ensembl:ENSLCAP00010053300.1, ECO:0000313|Proteomes:UP000314980};
RN   [1] {ECO:0000313|Proteomes:UP000314980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Sai Rama Sridatta P.;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLCAP00010053300.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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}. Peroxisome
CC       {ECO:0000256|ARBA:ARBA00004275}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|RuleBase:RU003557}.
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DR   AlphaFoldDB; A0A4W6FRR9; -.
DR   Ensembl; ENSLCAT00010054666.1; ENSLCAP00010053300.1; ENSLCAG00010024741.1.
DR   GeneTree; ENSGT00940000154327; -.
DR   Proteomes; UP000314980; 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; cd00826; nondecarbox_cond_enzymes; 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 metabolism {ECO:0000256|ARBA:ARBA00023098};
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:UP000314980};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003557};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          27..238
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          282..378
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   DOMAIN          434..535
FT                   /note="SCP2"
FT                   /evidence="ECO:0000259|Pfam:PF02036"
SQ   SEQUENCE   544 AA;  59034 MW;  0D753758DF7FC9F1 CRC64;
     MLATYNKNEE LDFLKKIFEM FSFDKPGAGD NSDYPDMAKE AGQKALADAG IPYSAIEQAC
     VGYVYGDSTC GQRAIYHSLG MTGIPIINVN NNCSTGSTAL FMARQLVQGG LADCVLALGF
     EKMERGSLSS KFMDRTNPMD KHMEVMINCY GMVAAPAAPQ MFGNAGREHM EKYGTKPEHF
     AKIAWKNHKH STNNPYSQFQ DEYSLEQVMN SRKVFDFLTL LQCCPTSDGA GAAVLASEAF
     VRNHHLENQA VEILAQEMVT DLTSTFEENS CIKMVGYDMS RLAAKKCFEA TGLKPSDVDV
     VELHDCFSAN ELITYEALGL CPEGKAGELI DRGDNTYGGK FVVNPSGGLI SKGHPLGATG
     LAQCAELCWQ LRGQAGRRQV PGAKVALQHN IGLGGAVVVG LYRMGFPQET RLHIGAVHTS
     SGSSLEGFKA YPVFKEIEKH LQEEGEQLVK KIGGVFAFKV RDGPGGKEAT WIVDVKSGKG
     SVSNDPDKKA DCTLSMCDED LLDLMTGKLN PQTAFFKGKL KITGNMGMAM KLQNLQVTPG
     KAKL
//
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