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Database: UniProt
Entry: A0A0D9QYL5_CHLSB
LinkDB: A0A0D9QYL5_CHLSB
Original site: A0A0D9QYL5_CHLSB 
ID   A0A0D9QYL5_CHLSB        Unreviewed;       413 AA.
AC   A0A0D9QYL5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN   Name=ZDHHC6 {ECO:0000313|Ensembl:ENSCSAP00000001454.1};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000001454.1, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000001454.1, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000001454.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-cysteinyl-[protein] + octadecanoyl-CoA = CoA + S-
CC         octadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59740, Rhea:RHEA-
CC         COMP:10131, Rhea:RHEA-COMP:15434, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:143200;
CC         Evidence={ECO:0000256|ARBA:ARBA00023536};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741;
CC         Evidence={ECO:0000256|ARBA:ARBA00023536};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC         hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-
CC         COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151;
CC         EC=2.3.1.225; Evidence={ECO:0000256|ARBA:ARBA00023340};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC         Evidence={ECO:0000256|ARBA:ARBA00023340};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC       {ECO:0000256|RuleBase:RU079119}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00008574, ECO:0000256|RuleBase:RU079119}.
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DR   EMBL; AQIB01042435; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007962303.1; XM_007964112.1.
DR   RefSeq; XP_007962304.1; XM_007964113.1.
DR   AlphaFoldDB; A0A0D9QYL5; -.
DR   STRING; 60711.ENSCSAP00000001454; -.
DR   Ensembl; ENSCSAT00000003165.1; ENSCSAP00000001454.1; ENSCSAG00000005132.1.
DR   GeneID; 103216530; -.
DR   KEGG; csab:103216530; -.
DR   CTD; 64429; -.
DR   eggNOG; KOG1314; Eukaryota.
DR   GeneTree; ENSGT00940000155642; -.
DR   OMA; GCIHAAI; -.
DR   OrthoDB; 6683at2759; -.
DR   BioGRID-ORCS; 103216530; 0 hits in 9 CRISPR screens.
DR   Proteomes; UP000029965; Chromosome 9.
DR   Bgee; ENSCSAG00000005132; Expressed in adrenal cortex and 7 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; IEA:Ensembl.
DR   GO; GO:0010636; P:positive regulation of mitochondrial fusion; IEA:Ensembl.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR12246:SF18; PALMITOYLTRANSFERASE; 1.
DR   PANTHER; PTHR12246; PALMITOYLTRANSFERASE ZDHHC16; 1.
DR   Pfam; PF01529; DHHC; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PROSITE; PS50216; DHHC; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU079119};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU079119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU079119};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM        25..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        59..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        146..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        195..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          313..398
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
SQ   SEQUENCE   413 AA;  47739 MW;  D9DEBC5ABF58EB3D CRC64;
     MGTFCSVIKF ENLQELKRLC HWGPIIALGV IAICSTMAMI DSVLWYWPLH TTGGSVNFIM
     LINWTVMILY NYFNAMFVGP GFVPLRWKPE ISQDTMYLQY CKVCQAYKAP RSHHCRKCNR
     CVMKMDHHCP WINNCCGYQN HASFTLFLLL APLGCIHAAF IFVMTMYTQL YNRLSFGWNT
     VKIDMSAARR DPLPIVPFGL AAFATTLFAL GLALGTTIAV GMLFFIQMKI ILKNKTSIES
     WIEEKAKDRI QYYQLDEVFV FPYDMGSRWR NFKQVFTWSG VPEGDGLEWP VREGCHQYSL
     TIEQLKQKAD KRVRSVRYKV IEDYSGACCP LNKGIKTFFT SPCTEEPRIR LQKGEFILAT
     RGLRYWLYGD KILDDSFIEG VSRIRGWFPR KCVEKCPCDA ETDQAPEGEK KNR
//
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