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Database: UniProt
Entry: G3IAW7_CRIGR
LinkDB: G3IAW7_CRIGR
Original site: G3IAW7_CRIGR 
ID   G3IAW7_CRIGR            Unreviewed;       413 AA.
AC   G3IAW7;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN   ORFNames=I79_020749 {ECO:0000313|EMBL:EGW12444.1};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW12444.1, ECO:0000313|Proteomes:UP000001075};
RN   [1] {ECO:0000313|Proteomes:UP000001075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX   PubMed=21804562; DOI=10.1038/nbt.1932;
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA   Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA   Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA   Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL   Nat. Biotechnol. 29:735-741(2011).
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; JH001767; EGW12444.1; -; Genomic_DNA.
DR   RefSeq; XP_007650747.1; XM_007652557.1.
DR   AlphaFoldDB; G3IAW7; -.
DR   STRING; 10029.G3IAW7; -.
DR   PaxDb; 10029-XP_007625941-1; -.
DR   GeneID; 100772972; -.
DR   CTD; 64429; -.
DR   eggNOG; KOG1314; Eukaryota.
DR   InParanoid; G3IAW7; -.
DR   OMA; GCIHAAI; -.
DR   OrthoDB; 6683at2759; -.
DR   Proteomes; UP000001075; Unassembled WGS sequence.
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:RHEA.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   InterPro; IPR036028; SH3-like_dom_sf.
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   SUPFAM; SSF50044; SH3-domain; 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:UP000001075};
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        53..73
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;  47555 MW;  A558EE6B3EEBAACA CRC64;
     MGTFCSVIKF ENLQELKRLC HWGPIIALGV IAICSTMAMI DSVLWYWPLH TTGGSVNFIM
     LINWTVMIVY NYFNAMFTGP GFVPRGWKPE NPQDSMYLQY CKVCQAYKAP RSHHCRKCNR
     CIMKMDHHCP WINNCCGHQN HASFTLFLLL VPLGCIHAAF IFVMTMYTQL YNRLSFGWNT
     VKIDMSAARR DPLPIIPFGL AAFAATLFAL GLALGTTIAV GMLFFIQIKI ILRNKTSIES
     WIEEKAKDRI QYYQLDEVFV FPYDLGSKWK NFKQVFTWSG VPEGDGLEWP TRKDCHPYSL
     TREQLKQKAD KRVRSVRYKV IEDYSGACCP LNRGIKTFFT SPCTEEPRIQ LQKGELILAT
     RGLRYWLYGD KILDDSFVEG TSRIRGWFPR NCVEKCPCDG ESDPAPEGEK KNR
//
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