ZDH18_RAT
ID ZDH18_RAT Reviewed; 386 AA.
AC Q2TGJ1;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Palmitoyltransferase ZDHHC18 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q9NUE0};
DE AltName: Full=Zinc finger DHHC domain-containing protein 18 {ECO:0000312|RGD:1309334};
GN Name=Zdhhc18 {ECO:0000312|RGD:1309334};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Huang C.-H., Chen Y., Ye T.;
RT "A superfamily of membrane-associated DHHC type zinc finger proteins.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Palmitoyltransferase that could catalyze the addition of
CC palmitate onto various protein substrates (By similarity).
CC Palmitoylates HRAS and LCK (By similarity). May also have a
CC palmitoyltransferase activity toward the beta-2 adrenergic
CC receptor/ADRB2 and therefore regulate G protein-coupled receptor
CC signaling (By similarity). {ECO:0000250|UniProtKB:Q5Y5T2,
CC ECO:0000250|UniProtKB:Q9NUE0}.
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:0000250|UniProtKB:Q9NUE0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q9NUE0};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9NUE0}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC ERF2/ZDHHC9 subfamily. {ECO:0000305}.
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DR EMBL; AY886534; AAX73396.1; -; mRNA.
DR RefSeq; NP_001034428.1; NM_001039339.1.
DR AlphaFoldDB; Q2TGJ1; -.
DR SMR; Q2TGJ1; -.
DR STRING; 10116.ENSRNOP00000009235; -.
DR PaxDb; Q2TGJ1; -.
DR PRIDE; Q2TGJ1; -.
DR GeneID; 362613; -.
DR KEGG; rno:362613; -.
DR UCSC; RGD:1309334; rat.
DR CTD; 84243; -.
DR RGD; 1309334; Zdhhc18.
DR eggNOG; KOG1311; Eukaryota.
DR InParanoid; Q2TGJ1; -.
DR OrthoDB; 1264614at2759; -.
DR PhylomeDB; Q2TGJ1; -.
DR PRO; PR:Q2TGJ1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016409; F:palmitoyltransferase activity; ISO:RGD.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; ISO:RGD.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Golgi apparatus; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..386
FT /note="Palmitoyltransferase ZDHHC18"
FT /id="PRO_0000269198"
FT TOPO_DOM 1..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..117
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..275
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 190..240
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..40
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 220
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUE0"
SQ SEQUENCE 386 AA; 41659 MW; 21ED70C27ADD1E1C CRC64;
MKDCEYQQIS PGAAPPPASP GVHRPGPAAP PGPSPGPAPG APRWSVSGSG SGSGSGSGSL
GRRPRRKWEV FPGRNRFYCG GRLMLAGHGG VFALTLLLIL STTILFFIFD CPYLARTLTL
AIPIIAAILF FFVMSCLLQT SFTDPGILPR ATICEAAALE KQIDNTGSST YRPPPRTREV
MINGQMVKLK YCFTCKMFRP PRTSHCSVCD NCVERFDHHC PWVGNCVGRR NYRFFYAFIL
SLSFLTAFIF ACVVTHLTLL SQGSNFLSAL NKTPAGVLEL VICFFSIWSI LGLSGFHTYL
VASNLTTNED IKGSWSSKRG GEASVNPYSH KSIITNCCAV LCGPLPPSLI DRRGFVQSDT
VLPSPIRSDE PACGAKPDAS MVGGHP
