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Database: UniProt
Entry: A0A2A3EMZ3_APICC
LinkDB: A0A2A3EMZ3_APICC
Original site: A0A2A3EMZ3_APICC 
ID   A0A2A3EMZ3_APICC        Unreviewed;       539 AA.
AC   A0A2A3EMZ3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=APICC_05390 {ECO:0000313|EMBL:PBC32864.1};
OS   Apis cerana cerana (Oriental honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Apis.
OX   NCBI_TaxID=94128 {ECO:0000313|EMBL:PBC32864.1, ECO:0000313|Proteomes:UP000242457};
RN   [1] {ECO:0000313|EMBL:PBC32864.1, ECO:0000313|Proteomes:UP000242457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Pupae without intestine {ECO:0000313|EMBL:PBC32864.1};
RA   Diao Q., Sun L., Zheng H., Zheng H., Xu S., Wang S., Zeng Z., Hu F., Su S.,
RA   Wu J.;
RT   "Genomic and transcriptomic analysis on Apis cerana provide comprehensive
RT   insights into honey bee biology.";
RL   Submitted (JUL-2014) 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   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|RuleBase:RU003557}.
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DR   EMBL; KZ288212; PBC32864.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A3EMZ3; -.
DR   STRING; 94128.A0A2A3EMZ3; -.
DR   Proteomes; UP000242457; 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   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:UP000242457};
KW   Transferase {ECO:0000256|RuleBase:RU003557};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          7..231
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          275..373
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   DOMAIN          433..525
FT                   /note="SCP2"
FT                   /evidence="ECO:0000259|Pfam:PF02036"
SQ   SEQUENCE   539 AA;  59010 MW;  85670290D706798C CRC64;
     MSPRMKIYVI GVGMTKFEKP GKRENFDYPD MAKEAVTKAL QDARISYDTV KAACVGYVYG
     DSTCGQRALY DVGLTGCPIY NVNNNCSTGS TALLMAKQII ETGSADCVLA LGFEKMEKGS
     LVSKFLDRTN PMDKHVELMS NIAGINESPI TAQLFGNAGL EHMKKYGTKP EHFAKIAYKN
     HLHSVNNPYS QFQEKYSLEQ IMSSPTVFGP LTKLQCCPTS DGSAAVILAN ADFVHKHKLE
     SQAVEIIAME MCTDLASTFT EKSSIKLIGY DMTRNAAEKV FTQTSYKPSD VDVIELHDCF
     SINELITYEA LGLCPPGQGG KLVDAGDNTY GGKFVINPSG GLISKGHPLG ATGLAQCAEL
     SWQLRGQAGK RQVPKAKLAL QHNIGLGGAV VVALYRMGFP QQFEKTKKNS SATPDPNQFK
     ANALFKLLEI AMQDDEDNLI EKVRGVYGFK VNNGTTEGYW IVDAKTGKGK IEYYGKSKPD
     VVITINDMDI VDFISGKLNP QKAFFQGKIK IQGNMGMAMK LIELQKRAAK KIELLRSKL
//
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