ZDHC1_MOUSE
ID ZDHC1_MOUSE Reviewed; 484 AA.
AC Q8R0N9; Q0VE36; Q8BJ24;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Palmitoyltransferase ZDHHC1 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000269|PubMed:23687301};
DE AltName: Full=Zinc finger DHHC domain-containing protein 1 {ECO:0000312|MGI:MGI:1918046};
GN Name=Zdhhc1 {ECO:0000312|MGI:MGI:1918046};
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=Hypothalamus;
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=Brain, and Colon;
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 [3]
RP TISSUE SPECIFICITY.
RC TISSUE=Pancreas;
RX PubMed=10395086; DOI=10.1023/a:1006932522197;
RA Putilina T., Wong P., Gentleman S.;
RT "The DHHC domain: a new highly conserved cysteine-rich motif.";
RL Mol. Cell. Biochem. 195:219-226(1999).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=23687301; DOI=10.1074/jbc.m112.431676;
RA Oku S., Takahashi N., Fukata Y., Fukata M.;
RT "In silico screening for palmitoyl substrates reveals a role for DHHC1/3/10
RT (zDHHC1/3/11)-mediated neurochondrin palmitoylation in its targeting to
RT Rab5-positive endosomes.";
RL J. Biol. Chem. 288:19816-19829(2013).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25299331; DOI=10.1016/j.chom.2014.09.006;
RA Zhou Q., Lin H., Wang S., Wang S., Ran Y., Liu Y., Ye W., Xiong X.,
RA Zhong B., Shu H.B., Wang Y.Y.;
RT "The ER-associated protein ZDHHC1 is a positive regulator of DNA virus-
RT triggered, MITA/STING-dependent innate immune signaling.";
RL Cell Host Microbe 16:450-461(2014).
CC -!- FUNCTION: Palmitoyltransferase that could catalyze the addition of
CC palmitate onto various protein substrates (PubMed:23687301). Has a
CC palmitoyltransferase activity toward NCDN and regulates NCDN
CC association with endosome membranes through this palmitoylation
CC (PubMed:23687301). {ECO:0000269|PubMed:23687301}.
CC -!- FUNCTION: Has also a palmitoyltransferase activity-independent function
CC in DNA virus-triggered and CGAS-mediated innate immune response
CC (PubMed:25299331). Functions as an activator of STING1 by promoting its
CC cGAMP-induced oligomerization and the recruitment of downstream
CC signaling components (PubMed:25299331). {ECO:0000269|PubMed:25299331}.
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:23687301};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000305|PubMed:23687301};
CC -!- SUBUNIT: Interacts with STING1; ZDHHC1 constitutively interacts with
CC STING1 and in presence of DNA viruses activates it by promoting its
CC cGAMP-induced oligomerization and the recruitment of downstream
CC signaling components. {ECO:0000250|UniProtKB:Q8WTX9}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:23687301};
CC Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:Q8WTX9}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus {ECO:0000250|UniProtKB:Q8WTX9}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in fetal lung and heart.
CC Expressed at lower levels in fetal liver and brain. Also detected in
CC adult islet cells of pancreas, Leydig cells of testis, retina and
CC molecular layer of cerebellum. {ECO:0000269|PubMed:10395086}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice are viable, fertile and
CC do not display overt phenotype (PubMed:25299331). Composition and
CC number of major immune cells is normal but mice are more susceptible to
CC DNA-virus infection and death than their wild-type counterpart
CC (PubMed:25299331). {ECO:0000269|PubMed:25299331}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AK038593; BAC30059.1; -; mRNA.
DR EMBL; BC026570; AAH26570.2; -; mRNA.
DR EMBL; BC119378; AAI19379.1; -; mRNA.
DR CCDS; CCDS22603.1; -.
DR RefSeq; NP_780369.1; NM_175160.3.
DR RefSeq; XP_006531420.1; XM_006531357.3.
DR RefSeq; XP_011246802.1; XM_011248500.2.
DR RefSeq; XP_011246803.1; XM_011248501.2.
DR AlphaFoldDB; Q8R0N9; -.
DR STRING; 10090.ENSMUSP00000036471; -.
DR PhosphoSitePlus; Q8R0N9; -.
DR SwissPalm; Q8R0N9; -.
DR PaxDb; Q8R0N9; -.
DR PRIDE; Q8R0N9; -.
DR ProteomicsDB; 302052; -.
DR Antibodypedia; 56070; 149 antibodies from 22 providers.
DR DNASU; 70796; -.
DR Ensembl; ENSMUST00000044286; ENSMUSP00000036471; ENSMUSG00000039199.
DR Ensembl; ENSMUST00000212303; ENSMUSP00000148381; ENSMUSG00000039199.
DR GeneID; 70796; -.
DR KEGG; mmu:70796; -.
DR UCSC; uc009ndd.1; mouse.
DR CTD; 29800; -.
DR MGI; MGI:1918046; Zdhhc1.
DR VEuPathDB; HostDB:ENSMUSG00000039199; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000159191; -.
DR HOGENOM; CLU_020283_0_1_1; -.
DR InParanoid; Q8R0N9; -.
DR OMA; HRKCTSK; -.
DR OrthoDB; 1216670at2759; -.
DR PhylomeDB; Q8R0N9; -.
DR TreeFam; TF317498; -.
DR BioGRID-ORCS; 70796; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Zdhhc1; mouse.
DR PRO; PR:Q8R0N9; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8R0N9; protein.
DR Bgee; ENSMUSG00000039199; Expressed in superior frontal gyrus and 77 other tissues.
DR Genevisible; Q8R0N9; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016409; F:palmitoyltransferase activity; IDA:MGI.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0140374; P:antiviral innate immune response; IMP:UniProtKB.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IDA:UniProtKB.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:UniProtKB.
DR GO; GO:1905668; P:positive regulation of protein localization to endosome; IMP:UniProtKB.
DR GO; GO:0032461; P:positive regulation of protein oligomerization; IMP:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; IDA: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 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Endosome; Golgi apparatus;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..484
FT /note="Palmitoyltransferase ZDHHC1"
FT /id="PRO_0000212858"
FT TOPO_DOM 1..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..74
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..238
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..484
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 131..181
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 1..268
FT /note="Mediates interaction with STING1"
FT /evidence="ECO:0000250|UniProtKB:Q8WTX9"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
SQ SEQUENCE 484 AA; 52979 MW; F80783E2EF8B2E68 CRC64;
MNICNKPSNK TAPEKSVWTA PSQDSGPSPE LQGQRSRRNG WSWPPHPLQI VAWLLYLFFA
VIGFGVLVPL LPHHWVPAGY ACMGAIFAGH LVVHLTAVSI DPADANVRDK SYSGPLPIFN
RSQHAHVIED LHCNLCDVDV SARSKHCSAC NKCVCGFDHH CKWLNNCVGE RNYRLFLHSV
ASALLGVLLL VLVATYVFVE FFVNPMRLRT NQHFEVLKNH TDVWFVFLPA APVETQAPAI
LALAALLILL GLLSTALLGH LLCFHIYLMW HKLTTYEYIV QHRPAQEAKE THKELESCPR
KVRSIQEMEF YMRTFSHVRP EPSGQARTAA LNANPSQFLA TQGQVEPPLP SSSDTLALPP
RIQPQKKRKR RVYRLPRSGV LDRELPLPRL RETGTPSRRS SSSSDSTSAS PVHAGGSAGA
YYSASAESME EIPVAQTRLG SAALGAPGAR GRESGLALQA RSPAVFVSPS SGEPGTPGGG
DGLP
