ID ZDHC9_HUMAN Reviewed; 364 AA.
AC Q9Y397; B4F6G2; D3DTF9; Q59EK4; Q5JSW5; Q8WWS7; Q9BPY4; Q9NSP0; Q9NVL0;
AC Q9NVR6;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 2.
DT 24-JUL-2024, entry version 185.
DE RecName: Full=Palmitoyltransferase ZDHHC9;
DE EC=2.3.1.225 {ECO:0000269|PubMed:16000296, ECO:0000269|PubMed:37802025, ECO:0000269|PubMed:38530158, ECO:0000269|PubMed:38599239};
DE AltName: Full=Zinc finger DHHC domain-containing protein 9;
DE Short=DHHC-9;
DE Short=DHHC9;
DE AltName: Full=Zinc finger protein 379;
DE AltName: Full=Zinc finger protein 380;
GN Name=ZDHHC9 {ECO:0000303|PubMed:37802025, ECO:0000312|HGNC:HGNC:18475};
GN Synonyms=CXorf11, ZDHHC10, ZNF379, ZNF380; ORFNames=CGI-89, UNQ261/PRO298;
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 [MRNA].
RX PubMed=16193335; DOI=10.1007/s00262-005-0074-x;
RA Zhou F.L., Zhang W.G., Chen G., Zhao W.H., Cao X.M., Chen Y.X., Tian W.,
RA Liu J., Liu S.H.;
RT "Serological identification and bioinformatics analysis of immunogenic
RT antigens in multiple myeloma.";
RL Cancer Immunol. Immunother. 55:910-917(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Muscle;
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 [10]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP INTERACTION WITH GOLGA7, ACTIVE SITE, AND MUTAGENESIS OF CYS-169.
RX PubMed=16000296; DOI=10.1074/jbc.m504113200;
RA Swarthout J.T., Lobo S., Farh L., Croke M.R., Greentree W.K.,
RA Deschenes R.J., Linder M.E.;
RT "DHHC9 and GCP16 constitute a human protein fatty acyltransferase with
RT specificity for H- and N-Ras.";
RL J. Biol. Chem. 280:31141-31148(2005).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27481942; DOI=10.1074/jbc.m116.725762;
RA Adachi N., Hess D.T., McLaughlin P., Stamler J.S.;
RT "S-Palmitoylation of a Novel Site in the beta2-Adrenergic Receptor
RT Associated with a Novel Intracellular Itinerary.";
RL J. Biol. Chem. 291:20232-20246(2016).
RN [12]
RP FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=34599882; DOI=10.1016/j.devcel.2021.09.016;
RA Mesquita F.S., Abrami L., Sergeeva O., Turelli P., Qing E., Kunz B.,
RA Raclot C., Paz Montoya J., Abriata L.A., Gallagher T., Dal Peraro M.,
RA Trono D., D'Angelo G., van der Goot F.G.;
RT "S-acylation controls SARS-CoV-2 membrane lipid organization and enhances
RT infectivity.";
RL Dev. Cell 56:1-18(2021).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF CYS-169.
RX PubMed=37802025; DOI=10.1016/j.molcel.2023.09.007;
RA Fan Y., Gao Y., Nie L., Hou T., Dan W., Wang Z., Liu T., Wei Y., Wang Y.,
RA Liu B., Que T., Lei Y., Zeng J., Ma J., Wei W., Li L.;
RT "Targeting LYPLAL1-mediated cGAS depalmitoylation enhances the response to
RT anti-tumor immunotherapy.";
RL Mol. Cell 83:3520-3532(2023).
RN [14]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=38599239; DOI=10.1038/s41586-024-07373-5;
RA Du G., Healy L.B., David L., Walker C., El-Baba T.J., Lutomski C.A.,
RA Goh B., Gu B., Pi X., Devant P., Fontana P., Dong Y., Ma X., Miao R.,
RA Balasubramanian A., Puthenveetil R., Banerjee A., Luo H.R., Kagan J.C.,
RA Oh S.F., Robinson C.V., Lieberman J., Wu H.;
RT "ROS-dependent S-palmitoylation activates cleaved and intact gasdermin D.";
RL Nature 0:0-0(2024).
RN [15]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=38530158; DOI=10.1126/sciimmunol.adn1452;
RA Balasubramanian A., Hsu A.Y., Ghimire L., Tahir M., Devant P., Fontana P.,
RA Du G., Liu X., Fabin D., Kambara H., Xie X., Liu F., Hasegawa T., Xu R.,
RA Yu H., Chen M., Kolakowski S., Trauger S., Larsen M.R., Wei W., Wu H.,
RA Kagan J.C., Lieberman J., Luo H.R.;
RT "The palmitoylation of gasdermin D directs its membrane translocation and
RT pore formation during pyroptosis.";
RL Sci. Immunol. 9:eadn1452-eadn1452(2024).
RN [16]
RP VARIANTS MRXSR TRP-148 AND SER-150.
RX PubMed=17436253; DOI=10.1086/513609;
RA Raymond F.L., Tarpey P.S., Edkins S., Tofts C., O'Meara S., Teague J.,
RA Butler A., Stevens C., Barthorpe S., Buck G., Cole J., Dicks E., Gray K.,
RA Halliday K., Hills K., Hinton J., Jones D., Menzies A., Perry J., Raine K.,
RA Shepherd R., Small A., Varian J., Widaa S., Mallya U., Moon J., Luo Y.,
RA Shaw M., Boyle J., Kerr B., Turner G., Quarrell O., Cole T., Easton D.F.,
RA Wooster R., Bobrow M., Schwartz C.E., Gecz J., Stratton M.R., Futreal P.A.;
RT "Mutations in ZDHHC9, which encodes a palmitoyltransferase of NRAS and
RT HRAS, cause X-linked mental retardation associated with a Marfanoid
RT habitus.";
RL Am. J. Hum. Genet. 80:982-987(2007).
RN [17]
RP VARIANTS MRXSR [LARGE SCALE ANALYSIS] TRP-148 AND SER-150.
RX PubMed=19377476; DOI=10.1038/ng.367;
RA Tarpey P.S., Smith R., Pleasance E., Whibley A., Edkins S., Hardy C.,
RA O'Meara S., Latimer C., Dicks E., Menzies A., Stephens P., Blow M.,
RA Greenman C., Xue Y., Tyler-Smith C., Thompson D., Gray K., Andrews J.,
RA Barthorpe S., Buck G., Cole J., Dunmore R., Jones D., Maddison M.,
RA Mironenko T., Turner R., Turrell K., Varian J., West S., Widaa S., Wray P.,
RA Teague J., Butler A., Jenkinson A., Jia M., Richardson D., Shepherd R.,
RA Wooster R., Tejada M.I., Martinez F., Carvill G., Goliath R.,
RA de Brouwer A.P., van Bokhoven H., Van Esch H., Chelly J., Raynaud M.,
RA Ropers H.H., Abidi F.E., Srivastava A.K., Cox J., Luo Y., Mallya U.,
RA Moon J., Parnau J., Mohammed S., Tolmie J.L., Shoubridge C., Corbett M.,
RA Gardner A., Haan E., Rujirabanjerd S., Shaw M., Vandeleur L., Fullston T.,
RA Easton D.F., Boyle J., Partington M., Hackett A., Field M., Skinner C.,
RA Stevenson R.E., Bobrow M., Turner G., Schwartz C.E., Gecz J., Raymond F.L.,
RA Futreal P.A., Stratton M.R.;
RT "A systematic, large-scale resequencing screen of X-chromosome coding exons
RT in mental retardation.";
RL Nat. Genet. 41:535-543(2009).
CC -!- FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate
CC onto various protein substrates, such as ADRB2, GSDMD, HRAS, NRAS and
CC CGAS (PubMed:16000296, PubMed:27481942, PubMed:37802025,
CC PubMed:38599239, PubMed:38530158). The ZDHHC9-GOLGA7 complex is a
CC palmitoyltransferase specific for HRAS and NRAS (PubMed:16000296). May
CC have a palmitoyltransferase activity toward the beta-2 adrenergic
CC receptor/ADRB2 and therefore regulate G protein-coupled receptor
CC signaling (PubMed:27481942). Acts as a regulator of innate immunity by
CC catalyzing palmitoylation of CGAS, thereby promoting CGAS
CC homodimerization and cyclic GMP-AMP synthase activity
CC (PubMed:37802025). Activates pyroptosis by catalyzing palmitoylation of
CC gasdermin-D (GSDMD), thereby promoting membrane translocation and pore
CC formation of GSDMD (PubMed:38599239, PubMed:38530158).
CC {ECO:0000269|PubMed:16000296, ECO:0000269|PubMed:27481942,
CC ECO:0000269|PubMed:37802025, ECO:0000269|PubMed:38530158,
CC ECO:0000269|PubMed:38599239}.
CC -!- FUNCTION: (Microbial infection) Through a sequential action with
CC ZDHHC20, rapidly and efficiently palmitoylates SARS coronavirus-2/SARS-
CC CoV-2 spike protein following its synthesis in the endoplasmic
CC reticulum (ER). In the infected cell, promotes spike biogenesis by
CC protecting it from premature ER degradation, increases half-life and
CC controls the lipid organization of its immediate membrane environment.
CC Once the virus has formed, spike palmitoylation controls fusion with
CC the target cell. {ECO:0000269|PubMed:34599882}.
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:16000296,
CC ECO:0000269|PubMed:34599882, ECO:0000269|PubMed:37802025,
CC ECO:0000269|PubMed:38530158, ECO:0000269|PubMed:38599239};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000269|PubMed:37802025, ECO:0000305|PubMed:16000296};
CC -!- SUBUNIT: Interacts with GOLGA7. {ECO:0000269|PubMed:16000296}.
CC -!- INTERACTION:
CC Q9Y397; O43889-2: CREB3; NbExp=3; IntAct=EBI-12690113, EBI-625022;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16000296, ECO:0000269|PubMed:34599882}; Multi-pass
CC membrane protein {ECO:0000255}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:16000296, ECO:0000269|PubMed:27481942}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, skeletal muscle, brain,
CC lung and liver. Absent in thymus, spleen and leukocytes.
CC {ECO:0000269|PubMed:16000296}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- DISEASE: Intellectual developmental disorder, X-linked, syndromic,
CC Raymond type (MRXSR) [MIM:300799]: A disorder characterized by
CC significantly below average general intellectual functioning associated
CC with impairments in adaptive behavior and manifested during the
CC developmental period. Some MRXSR patients show additional features,
CC including marfanoid habitus, epilepsy, facial dysmorphism, hypotonia,
CC and behavioral problems. {ECO:0000269|PubMed:17436253,
CC ECO:0000269|PubMed:19377476}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC ERF2/ZDHHC9 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34084.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91683.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD93044.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB82308.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY952881; ACF60379.1; -; mRNA.
DR EMBL; AF151847; AAD34084.1; ALT_INIT; mRNA.
DR EMBL; AY358558; AAQ88922.1; -; mRNA.
DR EMBL; AK001524; BAA91740.1; -; mRNA.
DR EMBL; AK001424; BAA91683.1; ALT_INIT; mRNA.
DR EMBL; AB209807; BAD93044.1; ALT_INIT; mRNA.
DR EMBL; AL161962; CAB82308.1; ALT_INIT; mRNA.
DR EMBL; AL034405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471107; EAX11823.1; -; Genomic_DNA.
DR EMBL; CH471107; EAX11824.1; -; Genomic_DNA.
DR EMBL; CH471107; EAX11825.1; -; Genomic_DNA.
DR EMBL; BC000035; AAH00035.1; -; mRNA.
DR EMBL; BC003128; AAH03128.1; -; mRNA.
DR EMBL; BC006200; AAH06200.1; -; mRNA.
DR EMBL; BC012826; AAH12826.1; -; mRNA.
DR CCDS; CCDS35395.1; -.
DR RefSeq; NP_001008223.1; NM_001008222.2.
DR RefSeq; NP_057116.2; NM_016032.3.
DR PDB; 8HF3; EM; 3.40 A; A=1-364.
DR PDBsum; 8HF3; -.
DR AlphaFoldDB; Q9Y397; -.
DR EMDB; EMD-34711; -.
DR SMR; Q9Y397; -.
DR BioGRID; 119302; 57.
DR IntAct; Q9Y397; 22.
DR STRING; 9606.ENSP00000349689; -.
DR TCDB; 8.A.114.1.5; the huntington-interacting protein 14 (hip14) family.
DR iPTMnet; Q9Y397; -.
DR PhosphoSitePlus; Q9Y397; -.
DR SwissPalm; Q9Y397; -.
DR BioMuta; ZDHHC9; -.
DR DMDM; 28202113; -.
DR jPOST; Q9Y397; -.
DR MassIVE; Q9Y397; -.
DR PaxDb; 9606-ENSP00000349689; -.
DR PeptideAtlas; Q9Y397; -.
DR ProteomicsDB; 85988; -.
DR Antibodypedia; 30107; 238 antibodies from 32 providers.
DR DNASU; 51114; -.
DR Ensembl; ENST00000357166.11; ENSP00000349689.6; ENSG00000188706.13.
DR Ensembl; ENST00000371064.7; ENSP00000360103.3; ENSG00000188706.13.
DR GeneID; 51114; -.
DR KEGG; hsa:51114; -.
DR MANE-Select; ENST00000357166.11; ENSP00000349689.6; NM_016032.4; NP_057116.2.
DR UCSC; uc004euv.4; human.
DR AGR; HGNC:18475; -.
DR CTD; 51114; -.
DR DisGeNET; 51114; -.
DR GeneCards; ZDHHC9; -.
DR HGNC; HGNC:18475; ZDHHC9.
DR HPA; ENSG00000188706; Low tissue specificity.
DR MalaCards; ZDHHC9; -.
DR MIM; 300646; gene.
DR MIM; 300799; phenotype.
DR neXtProt; NX_Q9Y397; -.
DR OpenTargets; ENSG00000188706; -.
DR Orphanet; 776; Lujan-Fryns syndrome.
DR PharmGKB; PA38340; -.
DR VEuPathDB; HostDB:ENSG00000188706; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000159999; -.
DR HOGENOM; CLU_018741_3_1_1; -.
DR InParanoid; Q9Y397; -.
DR OMA; YVTMFLI; -.
DR OrthoDB; 5480099at2759; -.
DR PhylomeDB; Q9Y397; -.
DR TreeFam; TF312923; -.
DR BRENDA; 2.3.1.225; 2681.
DR PathwayCommons; Q9Y397; -.
DR Reactome; R-HSA-9648002; RAS processing.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR SignaLink; Q9Y397; -.
DR SIGNOR; Q9Y397; -.
DR BioGRID-ORCS; 51114; 13 hits in 779 CRISPR screens.
DR ChiTaRS; ZDHHC9; human.
DR GeneWiki; ZDHHC9; -.
DR GenomeRNAi; 51114; -.
DR Pharos; Q9Y397; Tbio.
DR PRO; PR:Q9Y397; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9Y397; Protein.
DR Bgee; ENSG00000188706; Expressed in corpus callosum and 175 other cell types or tissues.
DR ExpressionAtlas; Q9Y397; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IC:UniProt.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0002178; C:palmitoyltransferase complex; IDA:UniProtKB.
DR GO; GO:0016409; F:palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0043849; F:Ras palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IDA:UniProtKB.
DR GO; GO:0044794; P:positive regulation by host of viral process; IDA:UniProtKB.
DR GO; GO:0141111; P:positive regulation of cGAS/STING signaling pathway; IDA:UniProt.
DR GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR PANTHER; PTHR22883:SF71; PALMITOYLTRANSFERASE ZDHHC9; 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 3D-structure; Acyltransferase; Disease variant; Endoplasmic reticulum;
KW Golgi apparatus; Host-virus interaction; Intellectual disability;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..364
FT /note="Palmitoyltransferase ZDHHC9"
FT /id="PRO_0000212880"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..63
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..228
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 139..189
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 303..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 169
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000305|PubMed:16000296,
FT ECO:0000305|PubMed:37802025"
FT VARIANT 148
FT /note="R -> W (in MRXSR; dbSNP:rs137852214)"
FT /evidence="ECO:0000269|PubMed:17436253,
FT ECO:0000269|PubMed:19377476"
FT /id="VAR_062674"
FT VARIANT 150
FT /note="P -> S (in MRXSR; dbSNP:rs137852215)"
FT /evidence="ECO:0000269|PubMed:17436253,
FT ECO:0000269|PubMed:19377476"
FT /id="VAR_062675"
FT MUTAGEN 169
FT /note="C->S: Abolishes palmitoyltransferase activity."
FT /evidence="ECO:0000269|PubMed:16000296,
FT ECO:0000269|PubMed:37802025"
FT CONFLICT 35
FT /note="K -> R (in Ref. 4; BAA91740)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="F -> L (in Ref. 4; BAA91740)"
FT /evidence="ECO:0000305"
FT CONFLICT 118..119
FT /note="QG -> GY (in Ref. 2; AAD34084)"
FT /evidence="ECO:0000305"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:8HF3"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:8HF3"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:8HF3"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:8HF3"
FT HELIX 36..55
FT /evidence="ECO:0007829|PDB:8HF3"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:8HF3"
FT HELIX 68..88
FT /evidence="ECO:0007829|PDB:8HF3"
FT HELIX 99..113
FT /evidence="ECO:0007829|PDB:8HF3"
FT STRAND 128..137
FT /evidence="ECO:0007829|PDB:8HF3"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:8HF3"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:8HF3"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:8HF3"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:8HF3"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:8HF3"
FT HELIX 182..210
FT /evidence="ECO:0007829|PDB:8HF3"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:8HF3"
FT HELIX 215..221
FT /evidence="ECO:0007829|PDB:8HF3"
FT HELIX 224..246
FT /evidence="ECO:0007829|PDB:8HF3"
FT TURN 247..253
FT /evidence="ECO:0007829|PDB:8HF3"
FT HELIX 256..261
FT /evidence="ECO:0007829|PDB:8HF3"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:8HF3"
FT HELIX 280..287
FT /evidence="ECO:0007829|PDB:8HF3"
SQ SEQUENCE 364 AA; 40916 MW; D1E97F3A93CC439F CRC64;
MSVMVVRKKV TRKWEKLPGR NTFCCDGRVM MARQKGIFYL TLFLILGTCT LFFAFECRYL
AVQLSPAIPV FAAMLFLFSM ATLLRTSFSD PGVIPRALPD EAAFIEMEIE ATNGAVPQGQ
RPPPRIKNFQ INNQIVKLKY CYTCKIFRPP RASHCSICDN CVERFDHHCP WVGNCVGKRN
YRYFYLFILS LSLLTIYVFA FNIVYVALKS LKIGFLETLK ETPGTVLEVL ICFFTLWSVV
GLTGFHTFLV ALNQTTNEDI KGSWTGKNRV QNPYSHGNIV KNCCEVLCGP LPPSVLDRRG
ILPLEESGSR PPSTQETSSS LLPQSPAPTE HLNSNEMPED SSTPEEMPPP EPPEPPQEAA
EAEK
//