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ZDH12_RAT
ID   ZDH12_RAT               Reviewed;         267 AA.
AC   Q6DGF5; Q2TGJ7;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Palmitoyltransferase ZDHHC12 {ECO:0000305};
DE            EC=2.3.1.225 {ECO:0000250|UniProtKB:Q8VC90};
DE   AltName: Full=DHHC domain-containing cysteine-rich protein 12 {ECO:0000250|UniProtKB:Q96GR4};
DE            Short=DHHC-12 {ECO:0000250|UniProtKB:Q96GR4};
DE   AltName: Full=Zinc finger DHHC domain-containing protein 12 {ECO:0000312|RGD:1306593};
GN   Name=Zdhhc12 {ECO:0000312|RGD:1306593};
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.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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: Palmitoyltransferase that could catalyze the addition of
CC       palmitate onto various protein substrates. Has a palmitoyltransferase
CC       activity toward gephyrin/GPHN, regulating its clustering at synapses
CC       and its function in gamma-aminobutyric acid receptor clustering.
CC       Thereby, indirectly regulates GABAergic synaptic transmission.
CC       {ECO:0000250|UniProtKB:Q8VC90}.
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:Q8VC90};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC         Evidence={ECO:0000250|UniProtKB:Q8VC90};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q8VC90}; Multi-pass membrane protein
CC       {ECO:0000255}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q96GR4}; 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       {ECO:0000305}.
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DR   EMBL; AY886528; AAX73390.1; -; mRNA.
DR   EMBL; BC076393; AAH76393.1; -; mRNA.
DR   RefSeq; NP_001013257.1; NM_001013239.1.
DR   AlphaFoldDB; Q6DGF5; -.
DR   SMR; Q6DGF5; -.
DR   STRING; 10116.ENSRNOP00000039802; -.
DR   PaxDb; Q6DGF5; -.
DR   GeneID; 366014; -.
DR   KEGG; rno:366014; -.
DR   UCSC; RGD:1306593; rat.
DR   CTD; 84885; -.
DR   RGD; 1306593; Zdhhc12.
DR   VEuPathDB; HostDB:ENSRNOG00000015791; -.
DR   eggNOG; KOG1311; Eukaryota.
DR   HOGENOM; CLU_031257_2_0_1; -.
DR   InParanoid; Q6DGF5; -.
DR   OMA; RRCRYCM; -.
DR   OrthoDB; 1440636at2759; -.
DR   PhylomeDB; Q6DGF5; -.
DR   PRO; PR:Q6DGF5; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000015791; Expressed in ovary and 19 other tissues.
DR   Genevisible; Q6DGF5; RN.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR   GO; GO:0097116; P:gephyrin clustering involved in postsynaptic density assembly; ISS:UniProtKB.
DR   GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:UniProtKB.
DR   GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; 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; Endoplasmic reticulum; Golgi apparatus; Lipoprotein;
KW   Membrane; Palmitate; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..267
FT                   /note="Palmitoyltransferase ZDHHC12"
FT                   /id="PRO_0000212886"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..43
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        65..140
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        162..178
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        200..267
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          97..147
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   ACT_SITE        127
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VC90"
SQ   SEQUENCE   267 AA;  31029 MW;  7D1435B5FC81A7F7 CRC64;
     MALWPLLNSG MLVRTGHTVL TWGITLVLFL HDTELRQWEE QGELFLPLTF LLLVLGSLLL
     YLAVSLMDPG YVTAQPQPQE EPKEEQTAMV PQAIPLRRCR YCLVLQPLRA RHCRECRRCV
     RRYDHHCPWM ENCVGERNHP LFVAYLALQL VVLLWGLYLA WSGLQFFQPW GLWLRSTGLL
     FTTFLLLSFF ALVVSLLLAS HLYLVARNTT TWEFISSHRI AYLRQRTSNP FDRGPTRNLA
     HFFCGWPSGP WETLWAEEEE EGSSQVV
 
 
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