ZDHC4_MOUSE
ID ZDHC4_MOUSE Reviewed; 343 AA.
AC Q9D6H5; Q8R5E0;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Palmitoyltransferase ZDHHC4 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q9NPG8};
DE AltName: Full=Zinc finger DHHC domain-containing protein 4 {ECO:0000312|MGI:MGI:1920131};
DE Short=DHHC-4;
GN Name=Zdhhc4 {ECO:0000312|MGI:MGI:1920131};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 protein substrates including the D(2) dopamine receptor
CC DRD2. {ECO:0000250|UniProtKB:Q9NPG8}.
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:Q9NPG8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q9NPG8};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NPG8}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NPG8};
CC Multi-pass membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9NPG8}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The C-terminal di-lysine motif confers endoplasmic reticulum
CC localization. {ECO:0000250|UniProtKB:Q9NPG8}.
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; AK013609; BAB28929.1; -; mRNA.
DR EMBL; BC019523; AAH19523.1; -; mRNA.
DR EMBL; BC022770; AAH22770.1; -; mRNA.
DR CCDS; CCDS19840.1; -.
DR RefSeq; NP_082655.1; NM_028379.5.
DR RefSeq; XP_006504794.1; XM_006504731.1.
DR RefSeq; XP_006504796.1; XM_006504733.1.
DR RefSeq; XP_006504797.1; XM_006504734.1.
DR RefSeq; XP_006504798.1; XM_006504735.1.
DR RefSeq; XP_006504799.1; XM_006504736.3.
DR AlphaFoldDB; Q9D6H5; -.
DR IntAct; Q9D6H5; 1.
DR MINT; Q9D6H5; -.
DR STRING; 10090.ENSMUSP00000001900; -.
DR PhosphoSitePlus; Q9D6H5; -.
DR SwissPalm; Q9D6H5; -.
DR EPD; Q9D6H5; -.
DR MaxQB; Q9D6H5; -.
DR PaxDb; Q9D6H5; -.
DR PeptideAtlas; Q9D6H5; -.
DR PRIDE; Q9D6H5; -.
DR ProteomicsDB; 274975; -.
DR Antibodypedia; 24908; 53 antibodies from 15 providers.
DR Ensembl; ENSMUST00000001900; ENSMUSP00000001900; ENSMUSG00000001844.
DR Ensembl; ENSMUST00000161915; ENSMUSP00000124813; ENSMUSG00000001844.
DR GeneID; 72881; -.
DR KEGG; mmu:72881; -.
DR UCSC; uc009ajz.2; mouse.
DR CTD; 55146; -.
DR MGI; MGI:1920131; Zdhhc4.
DR VEuPathDB; HostDB:ENSMUSG00000001844; -.
DR eggNOG; KOG1312; Eukaryota.
DR GeneTree; ENSGT00920000149163; -.
DR HOGENOM; CLU_042181_4_0_1; -.
DR InParanoid; Q9D6H5; -.
DR OMA; QHCPLVA; -.
DR OrthoDB; 445686at2759; -.
DR PhylomeDB; Q9D6H5; -.
DR TreeFam; TF330931; -.
DR BioGRID-ORCS; 72881; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Zdhhc4; mouse.
DR PRO; PR:Q9D6H5; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9D6H5; protein.
DR Bgee; ENSMUSG00000001844; Expressed in spermatocyte and 248 other tissues.
DR ExpressionAtlas; Q9D6H5; baseline and differential.
DR Genevisible; Q9D6H5; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IBA:GO_Central.
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; Cell membrane; Endoplasmic reticulum; Golgi apparatus;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..343
FT /note="Palmitoyltransferase ZDHHC4"
FT /id="PRO_0000212866"
FT TOPO_DOM 1..2
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..100
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..255
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 149..199
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT MOTIF 340..343
FT /note="Di-lysine motif"
FT /evidence="ECO:0000250|UniProtKB:Q9NPG8"
FT ACT_SITE 179
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
SQ SEQUENCE 343 AA; 39528 MW; 1EAB40177DDD218C CRC64;
MDFLVLFLFY LAFLLICVVL ICIFTKSQRL KAVVLGGAQV CSRVIPQCLQ RAVQTLLHQL
FHTRHPTFIV LHLLLQGLVY AEYTCEVFGY CRELEFSLPY LLLPYVLLSV NLVFFTLTCA
ANPGTITKAN ESFLLQVYKF DDVMFPKNSR CPTCDLRKPA RSKHCRLCDR CVHRFDHHCV
WVNNCIGAWN TRYFLIYLLT LTASAATIAT VTAAFLLRLV TVSDLYQETY LDDVGHFQAV
DTVFLIQHLF LAFPRIVFLL GFVIVLSMLL AGYLCFALYL AATNQTTNEW YKGDWAWCQR
WPLVAWSPSA EPRIHQNIHS HGFRSNLREI FLPATPSYKK KEK
