ZDH23_RAT
ID ZDH23_RAT Reviewed; 429 AA.
AC Q76IC6; Q2TGI7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Palmitoyltransferase ZDHHC23 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q8IYP9};
DE AltName: Full=NNOS-interacting DHHC domain-containing protein with dendritic mRNA {ECO:0000303|PubMed:15105416};
DE AltName: Full=Zinc finger DHHC domain-containing protein 23 {ECO:0000312|RGD:1303254};
DE Short=DHHC-23;
DE Short=zDHHC23;
GN Name=Zdhhc23 {ECO:0000312|RGD:1303254};
GN Synonyms=Nidd {ECO:0000303|PubMed:15105416};
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] (ISOFORMS L AND S), DEVELOPMENTAL STAGE, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH NOS1, AND FUNCTION.
RX PubMed=15105416; DOI=10.1074/jbc.m401471200;
RA Saitoh F., Tian Q.B., Okano A., Sakagami H., Kondo H., Suzuki T.;
RT "NIDD, a novel DHHC-containing protein, targets neuronal nitric-oxide
RT synthase (nNOS) to the synaptic membrane through a PDZ-dependent
RT interaction and regulates nNOS activity.";
RL J. Biol. Chem. 279:29461-29468(2004).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(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 (Probable). Palmitoyltransferase that mediates
CC palmitoylation of KCNMA1, regulating localization of KCNMA1 to the
CC plasma membrane (By similarity). May be involved in NOS1 regulation and
CC targeting to the synaptic membrane (PubMed:15105416).
CC {ECO:0000250|UniProtKB:Q8IYP9, ECO:0000269|PubMed:15105416,
CC ECO:0000305|PubMed:15105416}.
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:0000269|PubMed:15105416}.
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:0000269|PubMed:15105416}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=L;
CC IsoId=Q76IC6-1; Sequence=Displayed;
CC Name=S;
CC IsoId=Q76IC6-2; Sequence=VSP_016279;
CC -!- TISSUE SPECIFICITY: Expressed in the brain (at protein level), with
CC highest levels in olfactory bulb, piriform cortex and hippocampus.
CC {ECO:0000269|PubMed:15105416}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during the first week after
CC birth. {ECO:0000269|PubMed:15105416}.
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; AB098078; BAD16732.1; -; mRNA.
DR EMBL; AY886538; AAX73400.1; -; mRNA.
DR EMBL; AABR06068599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_998792.2; NM_213627.2. [Q76IC6-1]
DR RefSeq; XP_008766961.1; XM_008768739.2. [Q76IC6-1]
DR RefSeq; XP_008766962.1; XM_008768740.2. [Q76IC6-1]
DR AlphaFoldDB; Q76IC6; -.
DR STRING; 10116.ENSRNOP00000036655; -.
DR iPTMnet; Q76IC6; -.
DR PhosphoSitePlus; Q76IC6; -.
DR PaxDb; Q76IC6; -.
DR PRIDE; Q76IC6; -.
DR GeneID; 363783; -.
DR KEGG; rno:363783; -.
DR UCSC; RGD:1303254; rat. [Q76IC6-1]
DR CTD; 254887; -.
DR RGD; 1303254; Zdhhc23.
DR VEuPathDB; HostDB:ENSRNOG00000060348; -.
DR eggNOG; KOG1311; Eukaryota.
DR HOGENOM; CLU_055455_0_0_1; -.
DR InParanoid; Q76IC6; -.
DR OMA; LPDDCSD; -.
DR OrthoDB; 1261879at2759; -.
DR TreeFam; TF354316; -.
DR PRO; PR:Q76IC6; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000060348; Expressed in liver and 20 other tissues.
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; ISO:RGD.
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 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Golgi apparatus; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..429
FT /note="Palmitoyltransferase ZDHHC23"
FT /id="PRO_0000212914"
FT TOPO_DOM 1..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..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..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..347
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..429
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 253..303
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 212..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..429
FT /note="Interaction with NOS1"
FT /evidence="ECO:0000269|PubMed:15105416"
FT COMPBIAS 217..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 283
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT VAR_SEQ 286..322
FT /note="Missing (in isoform S)"
FT /evidence="ECO:0000303|PubMed:15105416"
FT /id="VSP_016279"
FT CONFLICT 260
FT /note="L -> V (in Ref. 1; BAD16732)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 429 AA; 48473 MW; C9E06073A39CB44D CRC64;
MKPVKKKKTE EPELEPLCCC EYIDRNGEKN HVAACLCDCQ DLDEGCDRWL TCKSLRPETC
ERITDTISDR LRIPWLRGAK KVNISILPPL VLLPVLLRVA SWHFLLGVVV LTSLPMLALW
YYYLTHRRKE QTLFFLSLGL FSLGYMYYVF LQEVVPQGHV GPAQLALLTC GLFLILVALY
RAKKNPGYLS NPACNDKSPS NSQIECPIKK GQEKTKGFPG TDTSGSLNNR TLKDDAKGSS
RVGLDSPAKS KEDWCAKCQL VRPARAWHCR ICGICVRRMD HHCVWINSCV GESNHQAFIL
ALSIFLLTSV YGISLTLNTI CRDRSLFTAL FYCPGVYANY SSALSFTCVW YSVIITAGMA
YIFLIQLINI SYNVTEREVQ QALRQKTGRR LLCGLIVDTG QYNRGFLRNW LQFSTLGTRT
VHTPAEDIV
