ID G3H067_CRIGR Unreviewed; 751 AA.
AC G3H067;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN ORFNames=I79_003542 {ECO:0000313|EMBL:EGW03441.1};
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:EGW03441.1, 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=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|RuleBase:RU079119};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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|RuleBase:RU079119}.
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DR EMBL; JH000088; EGW03441.1; -; Genomic_DNA.
DR AlphaFoldDB; G3H067; -.
DR STRING; 10029.G3H067; -.
DR eggNOG; KOG1032; Eukaryota.
DR InParanoid; G3H067; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043226; C:organelle; IEA:UniProt.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd13220; PH-GRAM_GRAMDC; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR23319:SF1; PROTEIN ASTER-C; 1.
DR PANTHER; PTHR23319; UNCHARACTERIZED; 1.
DR Pfam; PF01529; DHHC; 1.
DR Pfam; PF02893; GRAM; 1.
DR SMART; SM00568; GRAM; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU079119};
KW Membrane {ECO:0000256|RuleBase:RU079119};
KW Reference proteome {ECO:0000313|Proteomes:UP000001075};
KW Transferase {ECO:0000256|RuleBase:RU079119, ECO:0000313|EMBL:EGW03441.1};
KW Transmembrane {ECO:0000256|RuleBase:RU079119};
KW Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT TRANSMEM 290..312
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 460..477
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 483..502
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 511..529
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 541..558
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 665..686
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT DOMAIN 2..65
FT /note="GRAM"
FT /evidence="ECO:0000259|SMART:SM00568"
FT REGION 115..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 751 AA; 85229 MW; 07F38BAEE122ADB6 CRC64;
MAVTRARYDL VLVTIDYACA LQRDILLQGR LYLSENWLCF YSNIFRWETT ISIALKNITF
MTKEKTARLI PNAIQIITEG EKSLTRQEFW QLLQQNYGTE LGLNAEEMEN LSLSIEENVQ
PRSPERNSVD DSGERDEKFS KAISFTQESI SRVSETESLD GNSPKRGLGK EESQSEKHLK
KSLSLVSEKR LSRTPSKSLD LNKNEYLSLD KSSTSDSVDE ESDLLMEESV LNQSIEDPGK
LSSLRRRRRT LNRTAETAPK PSSQRSPIDV GFEAKGDITG KRKTVDSCDA VLIMVMSVFL
LLLVVLNVTL FLKLSKIEHA AQSFYQLHLQ EEKSFSLASD RFSSTENIQK NKDQAHHLKG
VLQDSIVMLE QVQTLKGNMK PVKKKKTEEP ELEPLCCCEY IDRNGEKNHV AACLCDCQDL
DEGCDRWLSC KSVRPETCER ITDTISDRLR IPWLRGAKKV NISIVPPLVL LPVFLHVASW
HFLLGVVVLI SLPMLALWYY YLTHRRKEQT LFFLSLGLFS LGYMYYVFLR EVVPKGRVGP
TQLALLTFGL FLILLALYRA KKDPGYLSNP ACNDKAPSNS QIECPIKKGQ EKTKGFPGTD
TSGSLNNRTL KDDIKGSSRV GLDSPAKVKE DWCAKCQLVR PARAWHCRIC GICVRRMDHH
CVCSALSFTC VWYSVIITAG MAYIFLIQLI NISYNVTERE VQQALRQKTG RRLLCGLIVD
TGQYNRGFLR NWYQFSTLGA HTAHIPAEDI V
//