ZDHC7_RAT
ID ZDHC7_RAT Reviewed; 308 AA.
AC Q923G5; Q2TGK0;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Palmitoyltransferase ZDHHC7 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q91WU6};
DE AltName: Full=Acyltransferase ZDHHC7 {ECO:0000250|UniProtKB:Q91WU6};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q91WU6};
DE AltName: Full=Sertoli cell gene with a zinc finger domain protein {ECO:0000303|PubMed:11796495};
DE AltName: Full=Zinc finger DHHC domain-containing protein 7 {ECO:0000312|RGD:620205};
DE Short=DHHC7 {ECO:0000312|EMBL:AAX73387.1};
GN Name=Zdhhc7 {ECO:0000312|RGD:620205};
GN Synonyms=Serz {ECO:0000303|PubMed:11796495};
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], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11796495; DOI=10.1210/endo.143.2.8618;
RA Chaudhary J., Skinner M.K.;
RT "Identification of a novel gene product, Sertoli cell gene with a zinc
RT finger domain, that is important for FSH activation of testicular Sertoli
RT cells.";
RL Endocrinology 143:426-435(2002).
RN [2]
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.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Golgi-localized palmitoyltransferase that catalyzes the
CC addition of palmitate onto various protein substrates and therefore
CC functions in several unrelated biological processes. Has no stringent
CC fatty acid selectivity and in addition to palmitate can also transfer
CC onto target proteins myristate from tetradecanoyl-CoA and stearate from
CC octadecanoyl-CoA (By similarity). Palmitoylates sex steroid hormone
CC receptors, including ESR1, PGR and AR, thereby regulating their
CC targeting to the plasma membrane and their function in rapid
CC intracellular signaling upon binding of sex hormones. Palmitoylates
CC GNAQ, a heterotrimeric G protein, regulating its dynamic localization
CC at the plasma membrane and is thereby involved in GNAQ-dependent G
CC protein-coupled receptor signaling pathways. Functions also in ligand-
CC induced cell death by regulating the FAS signaling pathway through the
CC palmitoylation and stabilization of the receptor at the plasma
CC membrane. In epithelial cells, palmitoylates SCRIB and regulates its
CC localization to the plasma membrane, regulating indirectly cell
CC polarity and differentiation. Also palmitoylates JAM3 and promotes its
CC expression at tight junctions and regulates its function in cell
CC migration (By similarity). Palmitoylates the glucose transporter
CC GLUT4/SLC2A4 and controls the insulin-dependent translocation of GLUT4
CC to the plasma membrane. In brain, could also palmitoylate SNAP25 and
CC DLG4/PSD95. Could also palmitoylate DNAJC5 and regulate its
CC localization to the Golgi membrane. Could also palmitoylate NCDN (By
CC similarity). May play a role in follicle stimulation hormone (FSH)
CC activation of testicular Sertoli cells (PubMed:11796495).
CC {ECO:0000250|UniProtKB:Q91WU6, ECO:0000250|UniProtKB:Q9NXF8,
CC ECO:0000269|PubMed:11796495}.
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:Q91WU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q91WU6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + tetradecanoyl-CoA = CoA + S-
CC tetradecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59736, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:15433, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:143199;
CC Evidence={ECO:0000250|UniProtKB:Q91WU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737;
CC Evidence={ECO:0000250|UniProtKB:Q91WU6};
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:0000250|UniProtKB:Q91WU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741;
CC Evidence={ECO:0000250|UniProtKB:Q91WU6};
CC -!- SUBUNIT: Homooligomers. Heterooligomers with ZDHHC3.
CC {ECO:0000250|UniProtKB:Q91WU6}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9NXF8}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Present in Sertoli cells (at
CC protein level). {ECO:0000269|PubMed:11796495}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- PTM: Autopalmitoylated. {ECO:0000250|UniProtKB:Q91WU6}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AY040615; AAK91508.1; -; mRNA.
DR EMBL; AY886525; AAX73387.1; -; mRNA.
DR EMBL; BC061769; AAH61769.1; -; mRNA.
DR RefSeq; NP_596885.1; NM_133394.1.
DR AlphaFoldDB; Q923G5; -.
DR SMR; Q923G5; -.
DR STRING; 10116.ENSRNOP00000023405; -.
DR PaxDb; Q923G5; -.
DR PRIDE; Q923G5; -.
DR Ensembl; ENSRNOT00000023405; ENSRNOP00000023405; ENSRNOG00000017342.
DR GeneID; 170906; -.
DR KEGG; rno:170906; -.
DR UCSC; RGD:620205; rat.
DR CTD; 55625; -.
DR RGD; 620205; Zdhhc7.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000156519; -.
DR HOGENOM; CLU_048061_1_1_1; -.
DR InParanoid; Q923G5; -.
DR OMA; WYSMING; -.
DR OrthoDB; 1491968at2759; -.
DR PhylomeDB; Q923G5; -.
DR TreeFam; TF319798; -.
DR Reactome; R-RNO-9009391; Extra-nuclear estrogen signaling.
DR PRO; PR:Q923G5; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000017342; Expressed in duodenum and 19 other tissues.
DR Genevisible; Q923G5; RN.
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:0019705; F:protein-cysteine S-myristoyltransferase activity; IEA:RHEA.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; IEA:RHEA.
DR GO; GO:0044381; P:glucose import in response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0009895; P:negative regulation of catabolic process; ISS:UniProtKB.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:UniProtKB.
DR GO; GO:0030859; P:polarized epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; ISS:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR GO; GO:1902044; P:regulation of Fas signaling pathway; ISS:UniProtKB.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0150106; P:regulation of protein localization to cell-cell junction; ISS:UniProtKB.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISS:UniProtKB.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Golgi apparatus; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..308
FT /note="Palmitoyltransferase ZDHHC7"
FT /id="PRO_0000212876"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..75
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..217
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 130..180
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 160
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
SQ SEQUENCE 308 AA; 35231 MW; 7943CCA1E52EAF38 CRC64;
MQPSGHRLRD IEHHPLLTDN DNYDSASSSS SEADMADRVW FIRDGCGMVC AVMTWLLVVY
ADFVVTFVML LPSKDFWYSV VNGVLFNCLA VLALSSHLRT MLTDPGAVPK GNATKEYMES
LQLKPGEVIY KCPKCCCIKP ERAHHCSICK RCIRKMDHHC PWVNNCVGEK NQRFFVLFTM
YIALSSIHAL ILCGLQFISC VRGQWTECSD FSPPITVILL VFLCLEGLLF FTFTAVMFGT
QIHSICNDET EIERLKSEKP TWERRLRWEG MKSVFGGPPS LLWMNPFVGF RFRRLQMRTR
KGGPEFSV
