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   02-SEP-2026, entry version 157.
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=L-cysteinyl-[protein] + hexadecanoyl-CoA = S-hexadecanoyl-L-
CC         cysteinyl-[protein] + CoA; 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_173570.5.
DR   RefSeq; XP_005247326.1; XM_005247269.2.
DR   RefSeq; XP_047303847.1; XM_047447891.1.
DR   RefSeq; XP_047303848.1; XM_047447892.1.
DR   RefSeq; XP_054201970.1; XM_054345995.1.
DR   RefSeq; XP_054201975.1; XM_054346000.1.
DR   RefSeq; XP_054201976.1; XM_054346001.1.
DR   AlphaFoldDB; Q8IYP9; -.
DR   BioGRID; 129056; 80.
DR   FunCoup; Q8IYP9; 184.
DR   IntAct; Q8IYP9; 38.
DR   STRING; 9606.ENSP00000498556; -.
DR   iPTMnet; Q8IYP9; -.
DR   PhosphoSitePlus; Q8IYP9; -.
DR   SwissPalm; Q8IYP9; -.
DR   BioMuta; ZDHHC23; -.
DR   DMDM; 215274191; -.
DR   jPOST; Q8IYP9; -.
DR   MassIVE; Q8IYP9; -.
DR   PaxDb; 9606-ENSP00000498556; -.
DR   PeptideAtlas; Q8IYP9; -.
DR   ProteomicsDB; 71212; -.
DR   Antibodypedia; 16460; 51 antibodies from 13 providers.
DR   DNASU; 254887; -.
DR   Ensembl; ENST00000330212.7; ENSP00000330485.3; ENSG00000184307.18.
DR   GeneID; 254887; -.
DR   KEGG; hsa:254887; -.
DR   UCSC; uc003eau.4; human.
DR   AGR; HGNC:28654; -.
DR   ClinPGx; PA134960347; -.
DR   CTD; 254887; -.
DR   DisGeNET; 254887; -.
DR   GeneCards; ZDHHC23; -.
DR   HGNC; HGNC:28654; ZDHHC23.
DR   HPA; ENSG00000184307; Tissue enhanced (testis).
DR   MIM; 617334; gene.
DR   OpenTargets; ENSG00000184307; -.
DR   VEuPathDB; HostDB:ENSG00000184307; -.
DR   eggNOG; KOG1311; Eukaryota.
DR   GeneTree; ENSGT00940000156558; -.
DR   InParanoid; Q8IYP9; -.
DR   OMA; GNWSEFM; -.
DR   OrthoDB; 430659at2759; -.
DR   PAN-GO; Q8IYP9; 5 GO annotations based on evolutionary models.
DR   PhylomeDB; Q8IYP9; -.
DR   PathwayCommons; Q8IYP9; -.
DR   SignaLink; Q8IYP9; -.
DR   Agora; ENSG00000184307; -.
DR   BioGRID-ORCS; 254887; 11 hits in 1148 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 133 other cell types or tissues.
DR   ExpressionAtlas; Q8IYP9; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; EXP:UniProtKB.
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   InterPro; IPR039859; PFA4/ZDH16/20/ERF2-like.
DR   PANTHER; PTHR22883:SF475; PALMITOYLTRANSFERASE ZDHHC23; 1.
DR   PANTHER; PTHR22883; ZINC FINGER DHHC DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Golgi apparatus; Lipoprotein; Membrane; Palmitate;
KW   Proteomics identification; Reference proteome; Transferase; Transmembrane;
KW   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
//