ZDH11_MOUSE
ID ZDH11_MOUSE Reviewed; 347 AA.
AC Q14AK4; Q5Y5T4;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Palmitoyltransferase ZDHHC11 {ECO:0000305|PubMed:23687301};
DE EC=2.3.1.225 {ECO:0000269|PubMed:23687301};
DE AltName: Full=DHHC-containing protein 10 {ECO:0000303|PubMed:23687301};
DE Short=DHHC10(z11) {ECO:0000303|PubMed:23687301};
DE AltName: Full=Zinc finger DHHC domain-containing protein 11;
DE Short=DHHC-11;
GN Name=Zdhhc11 {ECO:0000312|MGI:MGI:1918414};
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].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RA Fukata M., Fukata Y., Bredt D.S.;
RT "DHHC-containing proteins.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-158.
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=29429998; DOI=10.1038/cmi.2017.146;
RA Liu Y., Zhou Q., Zhong L., Lin H., Hu M.M., Zhou Y., Shu H.B., Li S.;
RT "ZDHHC11 modulates innate immune response to DNA virus by mediating MITA-
RT IRF3 association.";
RL Cell. Mol. Immunol. 15:907-916(2018).
CC -!- FUNCTION: Endoplasmic reticulum-localized palmitoyltransferase that
CC could catalyze the addition of palmitate onto various protein
CC substrates and be involved in a variety of cellular processes
CC (PubMed:23687301). Has a palmitoyltransferase activity toward NCDN and
CC regulates NCDN association with endosome membranes through this
CC palmitoylation (PubMed:23687301). May play a role in cell proliferation
CC (By similarity). {ECO:0000250|UniProtKB:Q9H8X9,
CC 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:29429998). Functions as an adapter that recruits IRF3 to STING1
CC to promote the activation of that key transcriptional regulator of type
CC I interferon (IFN)-dependent immune response (PubMed:29429998).
CC {ECO:0000269|PubMed:29429998}.
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 IRF3 and STING1; in presence of DNA viruses
CC recruits IRF3 to STING1 promoting IRF3 phosphorylation and activation.
CC {ECO:0000250|UniProtKB:Q9H8X9}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:23687301};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- DISRUPTION PHENOTYPE: Homozygous knockout mice are viable and do not
CC show overt phenotype (PubMed:29429998). Composition and number of major
CC immune cells is normal but mice are more susceptible to DNA-virus
CC infection and death than their wild-type counterpart (PubMed:29429998).
CC {ECO:0000269|PubMed:29429998}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AY668948; AAU89702.1; -; mRNA.
DR EMBL; CT010471; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC116803; AAI16804.2; -; mRNA.
DR EMBL; BC116807; AAI16808.2; -; mRNA.
DR CCDS; CCDS36729.1; -.
DR RefSeq; NP_081980.1; NM_027704.2.
DR AlphaFoldDB; Q14AK4; -.
DR STRING; 10090.ENSMUSP00000089075; -.
DR PhosphoSitePlus; Q14AK4; -.
DR PaxDb; Q14AK4; -.
DR PRIDE; Q14AK4; -.
DR ProteomicsDB; 275133; -.
DR Ensembl; ENSMUST00000091493; ENSMUSP00000089075; ENSMUSG00000069189.
DR GeneID; 71164; -.
DR KEGG; mmu:71164; -.
DR UCSC; uc007ren.1; mouse.
DR CTD; 79844; -.
DR MGI; MGI:1918414; Zdhhc11.
DR VEuPathDB; HostDB:ENSMUSG00000069189; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000161608; -.
DR HOGENOM; CLU_020283_1_1_1; -.
DR InParanoid; Q14AK4; -.
DR OMA; RTKQPHV; -.
DR OrthoDB; 1216670at2759; -.
DR PhylomeDB; Q14AK4; -.
DR TreeFam; TF317498; -.
DR BioGRID-ORCS; 71164; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Zdhhc11; mouse.
DR PRO; PR:Q14AK4; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q14AK4; protein.
DR Bgee; ENSMUSG00000069189; Expressed in spermatid and 4 other tissues.
DR ExpressionAtlas; Q14AK4; baseline and differential.
DR Genevisible; Q14AK4; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0035591; F:signaling adaptor activity; ISO:MGI.
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: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; Endosome; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..347
FT /note="Palmitoyltransferase ZDHHC11"
FT /id="PRO_0000413764"
FT TOPO_DOM 1..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..75
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..234
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 128..178
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 291..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067,
FT ECO:0000305|PubMed:23687301"
FT MUTAGEN 158
FT /note="C->S: Loss of protein-cysteine S-
FT palmitoyltransferase activity."
FT /evidence="ECO:0000305|PubMed:23687301"
SQ SEQUENCE 347 AA; 39660 MW; 1D2C92540424C697 CRC64;
MKEMNICGIN KNWVLPEAQE NNVKKFLPRP LSRVNGWSPP LHSFQAISWI TYLAMSIVTF
GIFIPFLPYS WKYAANIVMG GVFIFHLIVH LIAITIDPAD TNVRLKKDYT QPVPAFDRSK
HTHVIQNQYC HLCEVTASKK AKHCSACNKC VSGFDHHCKW LNNCVGRRNY WFFFWSVASA
AVGILGVMII LCYICIQYFV NPDELRTDPL YKEIISENTW LLFLSLWPVP VKTPIVLSIA
VMALLLAIAS FVMLGHLLIF HLYLITKNMS TFDYLMKTRF KKNLHPAEEK ELPLQKKGDL
PQEKSDNWAW PKSPPRVGSQ KFPVSTLSPK SSVCFVASPP KICHSED
