ZDH23_MOUSE
ID ZDH23_MOUSE Reviewed; 425 AA.
AC Q5Y5T3; A6H5Y4; Q3UH65; Q3UVA2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Palmitoyltransferase ZDHHC23 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q8IYP9};
DE AltName: Full=DHHC-containing protein 11 {ECO:0000312|EMBL:AAU89703.1};
DE AltName: Full=Zinc finger DHHC domain-containing protein 23 {ECO:0000312|MGI:MGI:2685625};
DE Short=DHHC-23;
DE Short=zDHHC23;
GN Name=Zdhhc23 {ECO:0000312|MGI:MGI:2685625}; Synonyms=Gm779;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15603741; DOI=10.1016/j.neuron.2004.12.005;
RA Fukata M., Fukata Y., Adesnik H., Nicoll R.A., Bredt D.S.;
RT "Identification of PSD-95 palmitoylating enzymes.";
RL Neuron 44:987-996(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone, and Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 and be involved in a variety
CC of cellular processes. Palmitoyltransferase that mediates
CC palmitoylation of KCNMA1, regulating localization of KCNMA1 to the
CC plasma membrane. May be involved in NOS1 regulation and targeting to
CC the synaptic membrane. {ECO:0000250|UniProtKB:Q8IYP9}.
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:Q8IYP9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q8IYP9};
CC -!- SUBUNIT: Interacts with NOS1. {ECO:0000250|UniProtKB:Q76IC6}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8IYP9}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q8IYP9}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Neuronal soma and dendrites.
CC {ECO:0000250|UniProtKB:Q76IC6}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain.
CC {ECO:0000269|PubMed:15603741}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE27992.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY668949; AAU89703.1; -; mRNA.
DR EMBL; AK137472; BAE23368.1; -; mRNA.
DR EMBL; AK147553; BAE27992.1; ALT_INIT; mRNA.
DR EMBL; BC139052; AAI39053.1; -; mRNA.
DR EMBL; BC145684; AAI45685.1; -; mRNA.
DR CCDS; CCDS28180.1; -.
DR RefSeq; NP_001007461.1; NM_001007460.1.
DR RefSeq; XP_006522373.1; XM_006522310.3.
DR RefSeq; XP_006522374.1; XM_006522311.3.
DR RefSeq; XP_017172544.1; XM_017317055.1.
DR RefSeq; XP_017172545.1; XM_017317056.1.
DR AlphaFoldDB; Q5Y5T3; -.
DR STRING; 10090.ENSMUSP00000128650; -.
DR iPTMnet; Q5Y5T3; -.
DR PhosphoSitePlus; Q5Y5T3; -.
DR SwissPalm; Q5Y5T3; -.
DR PaxDb; Q5Y5T3; -.
DR PRIDE; Q5Y5T3; -.
DR ProteomicsDB; 274974; -.
DR Antibodypedia; 16460; 60 antibodies from 15 providers.
DR DNASU; 332175; -.
DR Ensembl; ENSMUST00000165648; ENSMUSP00000128650; ENSMUSG00000036304.
DR Ensembl; ENSMUST00000231700; ENSMUSP00000156253; ENSMUSG00000036304.
DR GeneID; 332175; -.
DR KEGG; mmu:332175; -.
DR UCSC; uc007zgp.1; mouse.
DR CTD; 254887; -.
DR MGI; MGI:2685625; Zdhhc23.
DR VEuPathDB; HostDB:ENSMUSG00000036304; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000156558; -.
DR HOGENOM; CLU_055455_0_0_1; -.
DR InParanoid; Q5Y5T3; -.
DR OMA; NSCVGEQ; -.
DR OrthoDB; 1261879at2759; -.
DR PhylomeDB; Q5Y5T3; -.
DR TreeFam; TF354316; -.
DR BioGRID-ORCS; 332175; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q5Y5T3; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q5Y5T3; protein.
DR Bgee; ENSMUSG00000036304; Expressed in lumbar dorsal root ganglion and 124 other tissues.
DR ExpressionAtlas; Q5Y5T3; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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: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:0072659; P:protein localization to plasma membrane; IMP:MGI.
DR GO; GO:0018345; P:protein palmitoylation; IMP:MGI.
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 Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..425
FT /note="Palmitoyltransferase ZDHHC23"
FT /id="PRO_0000212913"
FT TOPO_DOM 1..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 82..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..102
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 103..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..159
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..343
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 249..299
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 422..425
FT /note="Interaction with NOS1"
FT /evidence="ECO:0000250"
FT ACT_SITE 279
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT CONFLICT 131
FT /note="Q -> E (in Ref. 2; BAE23368)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 425 AA; 48150 MW; 36004314B450A243 CRC64;
MKPVKKKKTE EPELEPLCCC EYIDRNGEKN HVAACLCDCQ DLDEGCDRWL TCQSLRPETC
ERITDTISDR LRIPWLRGAK KVNISIVPPL VLLPVFLHVA SWHFLLGVVV LTSLPMLALW
YYYLTHRRKE QTLFFLSLGL FSLGYMYYVF LREVVPQGRV GPTQLALLTC GLLLILLALY
RAKKNPGYLS NDKSPSNSQI ECPVKKGQEK TKGFPGTDAS GSLNNRTLKD DVRGSSRVGL
DSPAKVKEDW CAKCQLVRPA RAWHCRICGI CVRRMDHHCV WINSCVGESN HQAFILALSI
FLLTSVYGIS LTLNTICRDR SLFTALFYCP GVYANYSSAL SFTCVWYSVI ITAGMAYIFL
IQLINISYNV TEREVQQALR QKTGRRLLCG LIVDTGQYNR GFLRNWLQFS TLGTHTVHTP
AEDIV
