ZDH23_HUMAN
ID ZDH23_HUMAN Reviewed; 409 AA.
AC Q8IYP9; D3DN76;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Palmitoyltransferase ZDHHC23 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000269|PubMed:22399288};
DE AltName: Full=Zinc finger DHHC domain-containing protein 23 {ECO:0000312|HGNC:HGNC:28654};
DE Short=DHHC-23;
DE Short=zDHHC23;
GN Name=ZDHHC23 {ECO:0000312|HGNC:HGNC:28654};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-247.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASN-132; ALA-221 AND
RP ARG-274.
RC TISSUE=Testis;
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).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=22399288; DOI=10.1074/jbc.m111.335547;
RA Tian L., McClafferty H., Knaus H.G., Ruth P., Shipston M.J.;
RT "Distinct acyl protein transferases and thioesterases control surface
RT expression of calcium-activated potassium channels.";
RL J. Biol. Chem. 287:14718-14725(2012).
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 (Probable). 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:0000269|PubMed:22399288,
CC ECO:0000305|PubMed:22399288}.
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:0000269|PubMed:22399288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000305|PubMed:22399288};
CC -!- SUBUNIT: Interacts with NOS1. {ECO:0000250|UniProtKB:Q76IC6}.
CC -!- INTERACTION:
CC Q8IYP9; Q8NBF1: GLIS1; NbExp=3; IntAct=EBI-12111024, EBI-12111022;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:22399288}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000305|PubMed:22399288}; 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; AC128687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79617.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79618.1; -; Genomic_DNA.
DR EMBL; BC035230; AAH35230.2; -; mRNA.
DR CCDS; CCDS33827.1; -.
DR RefSeq; NP_775841.2; NM_173570.4.
DR RefSeq; XP_005247326.1; XM_005247269.1.
DR AlphaFoldDB; Q8IYP9; -.
DR BioGRID; 129056; 79.
DR IntAct; Q8IYP9; 5.
DR STRING; 9606.ENSP00000330485; -.
DR iPTMnet; Q8IYP9; -.
DR PhosphoSitePlus; Q8IYP9; -.
DR BioMuta; ZDHHC23; -.
DR DMDM; 215274191; -.
DR EPD; Q8IYP9; -.
DR jPOST; Q8IYP9; -.
DR MassIVE; Q8IYP9; -.
DR MaxQB; Q8IYP9; -.
DR PaxDb; Q8IYP9; -.
DR PeptideAtlas; Q8IYP9; -.
DR PRIDE; Q8IYP9; -.
DR ProteomicsDB; 71212; -.
DR Antibodypedia; 16460; 60 antibodies from 15 providers.
DR DNASU; 254887; -.
DR Ensembl; ENST00000330212.7; ENSP00000330485.3; ENSG00000184307.17.
DR GeneID; 254887; -.
DR KEGG; hsa:254887; -.
DR UCSC; uc003eau.4; human.
DR CTD; 254887; -.
DR DisGeNET; 254887; -.
DR GeneCards; ZDHHC23; -.
DR HGNC; HGNC:28654; ZDHHC23.
DR HPA; ENSG00000184307; Low tissue specificity.
DR MIM; 617334; gene.
DR neXtProt; NX_Q8IYP9; -.
DR OpenTargets; ENSG00000184307; -.
DR PharmGKB; PA134960347; -.
DR VEuPathDB; HostDB:ENSG00000184307; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000156558; -.
DR InParanoid; Q8IYP9; -.
DR OMA; NSCVGEQ; -.
DR OrthoDB; 1261879at2759; -.
DR PhylomeDB; Q8IYP9; -.
DR TreeFam; TF354316; -.
DR PathwayCommons; Q8IYP9; -.
DR SignaLink; Q8IYP9; -.
DR BioGRID-ORCS; 254887; 9 hits in 1069 CRISPR screens.
DR GenomeRNAi; 254887; -.
DR Pharos; Q8IYP9; Tbio.
DR PRO; PR:Q8IYP9; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8IYP9; protein.
DR Bgee; ENSG00000184307; Expressed in sperm and 131 other tissues.
DR ExpressionAtlas; Q8IYP9; baseline and differential.
DR Genevisible; Q8IYP9; HS.
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:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Acyltransferase; Golgi apparatus; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..409
FT /note="Palmitoyltransferase ZDHHC23"
FT /id="PRO_0000212912"
FT TOPO_DOM 1..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 88..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..109
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 110..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..165
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..331
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..409
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 259..309
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 215..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 289
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT VARIANT 132
FT /note="H -> N (in dbSNP:rs17853401)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_047389"
FT VARIANT 221
FT /note="T -> A (in dbSNP:rs17853402)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_047390"
FT VARIANT 247
FT /note="K -> R (in dbSNP:rs11921691)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_047391"
FT VARIANT 274
FT /note="H -> R (in dbSNP:rs17857054)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_047392"
SQ SEQUENCE 409 AA; 45983 MW; 6AD65E37DA8F34AD CRC64;
MTQKGSMKPV KKKKTEEPEL EPLCCCEYID RNGEKNHVAT CLCDCQDLDE GCDRWITCKS
LQPETCERIM DTISDRLRIP WLRGAKKVNI SIIPPLVLLP VFLHVASWHF LLGVVVLTSL
PVLALWYYYL THRRKEQTLF FLSLGLFSLG YMYYVFLQEV VPKGRVGPVQ LAVLTCGLFL
ILLALHRAKK NPGYLSNPAS GDRSLSSSQL ECLSRKGQEK TKGFPGADMS GSLNNRTTKD
DPKGSSKMPA GSPTKAKEDW CAKCQLVRPA RAWHCRICGI CVRRMDHHCV WINSCVGESN
HQAFILALLI FLLTSVYGIT LTLDTICRDR SVFTALFYCP GVYANYSSAL SFTCVWYSVI
ITAGMAYIFL IQLINISYNV TEREVQQALR QKTGRRLLCG LIVDTGLLG
