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Database: UniProt
Entry: A0A2Y9QN01_TRIMA
LinkDB: A0A2Y9QN01_TRIMA
Original site: A0A2Y9QN01_TRIMA 
ID   A0A2Y9QN01_TRIMA        Unreviewed;       543 AA.
AC   A0A2Y9QN01;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=LOC101347488 {ECO:0000313|RefSeq:XP_023582826.1};
OS   Trichechus manatus latirostris (Florida manatee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX   NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023582826.1};
RN   [1] {ECO:0000313|RefSeq:XP_023582826.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-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=4,8,12-trimethyltridecanoyl-CoA + propanoyl-CoA = 3-
CC         oxopristanoyl-CoA + CoA; Xref=Rhea:RHEA:10408, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57291, ChEBI:CHEBI:57351, ChEBI:CHEBI:57392;
CC         EC=2.3.1.176; Evidence={ECO:0000256|ARBA:ARBA00029348};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10410;
CC         Evidence={ECO:0000256|ARBA:ARBA00029348};
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   -!- SUBUNIT: Interacts with PEX5; the interaction is essential for
CC       peroxisomal import. {ECO:0000256|ARBA:ARBA00024049}.
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   RefSeq; XP_023582826.1; XM_023727058.1.
DR   AlphaFoldDB; A0A2Y9QN01; -.
DR   STRING; 127582.A0A2Y9QN01; -.
DR   KEGG; tmu:101347488; -.
DR   InParanoid; A0A2Y9QN01; -.
DR   OrthoDB; 1799125at2759; -.
DR   Proteomes; UP000248480; 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:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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 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:UP000248480};
KW   Transferase {ECO:0000256|RuleBase:RU003557};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          14..238
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          282..380
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   DOMAIN          433..534
FT                   /note="SCP2"
FT                   /evidence="ECO:0000259|Pfam:PF02036"
SQ   SEQUENCE   543 AA;  58580 MW;  1F00E9DB9E7EAE9F CRC64;
     MSPVPSKSAG LRRVFVVGVG MTEFVKPVDN SRDYPDLAEE AGQKALADAQ IPYSAVEQAC
     VGYVYGDSTC GQRAVYHSLG LTGIPIINVN NNCSTGSTAL FMGRQLIQGG VADCVLALGF
     EKMDKGPLGV KFPDRTIPLD KHLEVMVNKY GMSAHPVASQ MFGRAGEEHM EKYGTKIEHF
     AKIGWKNHKH SVNNPYSQSQ KEYSLDEVME SREVFNFLTV LQCCPTSDGA AAAVLASEAF
     VQKYGLQSKA VEILAQEMVT DLPSSFEEKS VIKMVGFDMT KEAARKCYEK SGLRPSDIDV
     IELHDCFSSN ELLSYEALGL CPEGQGGKLV DRGDNTYGGK WVINPSGGLI AKGHPLGATG
     LGQCAELCWQ LRGEAGKRQV PGAKVALQHN IGLGGAVVVT VYKMGFPEAA RTHQIEAVPT
     SSAFDGFKAN LVFKEIEKKL EEEGEEFVKK IGGIFAFKVK DGPGGKEATW VVDVKNGKGS
     VHPNSDKKAD CTITMADSDL LALMTGKMNP QSAFFQGKLK ITGNMGMAMK LQNLQLQPGK
     AKL
//
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