ZDH11_HUMAN
ID ZDH11_HUMAN Reviewed; 412 AA.
AC Q9H8X9; Q6UWR9;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Palmitoyltransferase ZDHHC11 {ECO:0000250|UniProtKB:Q14AK4};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q14AK4};
DE AltName: Full=Zinc finger DHHC domain-containing protein 11 {ECO:0000303|PubMed:16647879};
DE Short=DHHC-11 {ECO:0000303|PubMed:16647879};
DE AltName: Full=Zinc finger protein 399 {ECO:0000312|HGNC:HGNC:19158};
GN Name=ZDHHC11 {ECO:0000312|HGNC:HGNC:19158};
GN Synonyms=ZNF399 {ECO:0000312|HGNC:HGNC:19158};
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 MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16647879; DOI=10.1016/j.bbalip.2006.03.010;
RA Ohno Y., Kihara A., Sano T., Igarashi Y.;
RT "Intracellular localization and tissue-specific distribution of human and
RT yeast DHHC cysteine-rich domain-containing proteins.";
RL Biochim. Biophys. Acta 1761:474-483(2006).
RN [6]
RP FUNCTION, INTERACTION WITH IRF3 AND STING1, REGION, AND MUTAGENESIS OF
RP 152-ASP-HIS-153 AND CYS-155.
RX PubMed=28331227; DOI=10.1038/leu.2017.94;
RA Dzikiewicz-Krawczyk A., Kok K., Slezak-Prochazka I., Robertus J.L.,
RA Bruining J., Tayari M.M., Rutgers B., de Jong D., Koerts J., Seitz A.,
RA Li J., Tillema B., Guikema J.E., Nolte I.M., Diepstra A., Visser L.,
RA Kluiver J., van den Berg A.;
RT "ZDHHC11 and ZDHHC11B are critical novel components of the oncogenic MYC-
RT miR-150-MYB network in Burkitt lymphoma.";
RL Leukemia 31:1470-1473(2017).
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 (By
CC similarity). Has a palmitoyltransferase activity toward NCDN and
CC regulates NCDN association with endosome membranes through this
CC palmitoylation (By similarity). May play a role in cell proliferation
CC (PubMed:28331227). {ECO:0000250|UniProtKB:Q14AK4,
CC ECO:0000269|PubMed:28331227}.
CC -!- FUNCTION: Has also a palmitoyltransferase activity-independent function
CC in DNA virus-triggered and CGAS-mediated innate immune response
CC (PubMed:28331227). 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:28331227).
CC {ECO:0000269|PubMed:28331227}.
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:Q14AK4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q14AK4};
CC -!- SUBUNIT: Interacts with IRF3 and STING1; in presence of DNA viruses
CC recruits IRF3 to STING1 promoting IRF3 phosphorylation and activation.
CC {ECO:0000269|PubMed:28331227}.
CC -!- INTERACTION:
CC Q9H8X9; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-17961574, EBI-8638294;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16647879}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H8X9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H8X9-2; Sequence=VSP_055997, VSP_055998, VSP_055999;
CC -!- TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:16647879}.
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; AY358673; AAQ89036.1; -; mRNA.
DR EMBL; AK023215; BAB14468.1; -; mRNA.
DR EMBL; AC010427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032000; AAH32000.1; -; mRNA.
DR CCDS; CCDS3857.1; -. [Q9H8X9-1]
DR RefSeq; NP_079062.1; NM_024786.2. [Q9H8X9-1]
DR AlphaFoldDB; Q9H8X9; -.
DR BioGRID; 122935; 22.
DR IntAct; Q9H8X9; 12.
DR MINT; Q9H8X9; -.
DR STRING; 9606.ENSP00000283441; -.
DR iPTMnet; Q9H8X9; -.
DR PhosphoSitePlus; Q9H8X9; -.
DR SwissPalm; Q9H8X9; -.
DR BioMuta; ZDHHC11; -.
DR DMDM; 28202107; -.
DR MassIVE; Q9H8X9; -.
DR PaxDb; Q9H8X9; -.
DR PeptideAtlas; Q9H8X9; -.
DR PRIDE; Q9H8X9; -.
DR ProteomicsDB; 81254; -. [Q9H8X9-1]
DR Antibodypedia; 22260; 39 antibodies from 14 providers.
DR DNASU; 79844; -.
DR Ensembl; ENST00000283441.13; ENSP00000283441.8; ENSG00000188818.13. [Q9H8X9-1]
DR Ensembl; ENST00000511539.1; ENSP00000427067.1; ENSG00000188818.13. [Q9H8X9-2]
DR GeneID; 79844; -.
DR KEGG; hsa:79844; -.
DR MANE-Select; ENST00000283441.13; ENSP00000283441.8; NM_024786.3; NP_079062.1.
DR UCSC; uc003jbk.5; human. [Q9H8X9-1]
DR CTD; 79844; -.
DR DisGeNET; 79844; -.
DR GeneCards; ZDHHC11; -.
DR HGNC; HGNC:19158; ZDHHC11.
DR HPA; ENSG00000188818; Tissue enhanced (brain).
DR neXtProt; NX_Q9H8X9; -.
DR OpenTargets; ENSG00000188818; -.
DR PharmGKB; PA38801; -.
DR VEuPathDB; HostDB:ENSG00000188818; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000161608; -.
DR HOGENOM; CLU_020283_1_1_1; -.
DR InParanoid; Q9H8X9; -.
DR OMA; RTKQPHV; -.
DR OrthoDB; 1216670at2759; -.
DR PhylomeDB; Q9H8X9; -.
DR TreeFam; TF317498; -.
DR PathwayCommons; Q9H8X9; -.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR SignaLink; Q9H8X9; -.
DR BioGRID-ORCS; 79844; 21 hits in 1062 CRISPR screens.
DR ChiTaRS; ZDHHC11; human.
DR GenomeRNAi; 79844; -.
DR Pharos; Q9H8X9; Tdark.
DR PRO; PR:Q9H8X9; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9H8X9; protein.
DR Bgee; ENSG00000188818; Expressed in right uterine tube and 182 other tissues.
DR ExpressionAtlas; Q9H8X9; baseline and differential.
DR Genevisible; Q9H8X9; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; ISS: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; ISS:UniProtKB.
DR GO; GO:0035591; F:signaling adaptor activity; IDA:UniProtKB.
DR GO; GO:0140374; P:antiviral innate immune response; IMP:UniProtKB.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS: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; Alternative splicing; Endoplasmic reticulum; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..412
FT /note="Palmitoyltransferase ZDHHC11"
FT /id="PRO_0000212883"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..69
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..230
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..412
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 125..175
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 198..412
FT /note="Mediates interaction with IRF3 and STING1"
FT /evidence="ECO:0000269|PubMed:28331227"
FT REGION 374..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 155
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q14AK4,
FT ECO:0000255|PROSITE-ProRule:PRU00067"
FT VAR_SEQ 1..213
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_055997"
FT VAR_SEQ 262..355
FT /note="KAKKMTTFEYLINNRKEESSKHQAVRKDPYVQMDKGVLQQGAGALGSSAQGV
FT KAKSSLLIHKHLCHFCTSVNQDGDSTAREGDEDPCPSALGAK -> SMSPTLSPRSPQG
FT WVVRAAHLTPLLEYVPNPEPPTPGARVFVPRVRMCSGSASPRSEIMDKKGKSQEEIKSM
FT RTQQAQQEAELTPRPAGVVPGA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_055998"
FT VAR_SEQ 356..412
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_055999"
FT VARIANT 325
FT /note="L -> S (in dbSNP:rs2878468)"
FT /id="VAR_052975"
FT VARIANT 341
FT /note="R -> Q (in dbSNP:rs1809008)"
FT /id="VAR_024704"
FT VARIANT 372
FT /note="R -> H (in dbSNP:rs3747738)"
FT /id="VAR_021998"
FT MUTAGEN 152..153
FT /note="DH->AA: No effect on the regulation of STING1-
FT mediated innate immune response."
FT /evidence="ECO:0000269|PubMed:28331227"
FT MUTAGEN 155
FT /note="C->S: No effect on the regulation of STING1-mediated
FT innate immune response."
FT /evidence="ECO:0000269|PubMed:28331227"
SQ SEQUENCE 412 AA; 45975 MW; 7A5B74FBC37B2F9E CRC64;
MDTRSGSQCS VTPEAILNNE KLVLPPRISR VNGWSLPLHY FQVVTWAVFV GLSSATFGIF
IPFLPHAWKY IAYVVTGGIF SFHLVVHLIA SCIDPADSNV RLMKNYSQPM PLFDRSKHAH
VIQNQFCHLC KVTVNKKTKH CISCNKCVSG FDHHCKWINN CVGSRNYWFF FSTVASATAG
MLCLIAILLY VLVQYLVNPG VLRTDPRYED VKNMNTWLLF LPLFPVQVQT LIVVIIGMLV
LLLDFLGLVH LGQLLIFHIY LKAKKMTTFE YLINNRKEES SKHQAVRKDP YVQMDKGVLQ
QGAGALGSSA QGVKAKSSLL IHKHLCHFCT SVNQDGDSTA REGDEDPCPS ALGAKARNSR
LICRRLCQFS TRVHPDGGSM AQEADDAPSI STLGLQQETT EPMKTDSAES ED
