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Database: UniProt
Entry: A0A485ME42_LYNPA
LinkDB: A0A485ME42_LYNPA
Original site: A0A485ME42_LYNPA 
ID   A0A485ME42_LYNPA        Unreviewed;       549 AA.
AC   A0A485ME42;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
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   ORFNames=LYPA_23C012791 {ECO:0000313|EMBL:VFV19035.1};
OS   Lynx pardinus (Iberian lynx) (Felis pardina).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Lynx.
OX   NCBI_TaxID=191816 {ECO:0000313|EMBL:VFV19035.1, ECO:0000313|Proteomes:UP000386466};
RN   [1] {ECO:0000313|EMBL:VFV19035.1, ECO:0000313|Proteomes:UP000386466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Alioto T., Alioto T.;
RL   Submitted (JAN-2019) 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=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   EMBL; CAAGRJ010001337; VFV19035.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A485ME42; -.
DR   Proteomes; UP000386466; 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: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:UP000386466};
KW   Transferase {ECO:0000256|RuleBase:RU003557};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          15..244
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          288..386
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   DOMAIN          439..540
FT                   /note="SCP2"
FT                   /evidence="ECO:0000259|Pfam:PF02036"
SQ   SEQUENCE   549 AA;  59340 MW;  6166ECC01BE4767D CRC64;
     MLLTAAVVPR PRHRVFVVGV GMTKFLKPGL GNSRDYPDLA KEAGEKALSD AQIPYSVVEQ
     ACVGYVYGDS TCGQRSIYHS LGLTGIPIIN VNNNCATGST ALFIARQLIQ GGMADCVLAL
     GFEKMEKGAL SFFSLSNTSQ RTNPVDKHLE VLIKKYGLCA KPVAPQMFGF AGKEHMEKYG
     TKVEHFAKIG WKNHKHSVNN PNSQFQKEYS LDEVMKSQEV FDYLTILQCC PTSDGAAAAV
     LASETFVQKY GLESKAVEIV AQEMVTDLPS SFEENSIIKM VGFDMSKEAA RKCYEKSGLR
     PSDIDVIELH DCFSVNELLT YEALGLCPEG QGGKLVDRGD NTYGGKWVVN PSGGLISKGH
     PLGATGLAQC AELCWQLRGE AGKRQVPGAK VALQHNLGIG GAVVVTLYKM GFPEAARTHQ
     IEAAPTSSAF DGFKANLVFK EIEKKLEEEG EQFVKKIGGI FAFKVKDGPG GKEATWVVDV
     KNGKGSVLPN SDKKADCTIT MADSDLLALM TGKMNPQSAF FQGKLKITGN MGLAMKLQNL
     QLQPGKAKL
//
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