ID ZDH15_HUMAN Reviewed; 337 AA. AC Q96MV8; B3KVG7; Q3SY30; Q6UWH3; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 164. DE RecName: Full=Palmitoyltransferase ZDHHC15 {ECO:0000305}; DE EC=2.3.1.225 {ECO:0000269|PubMed:18817523}; DE AltName: Full=Acyltransferase ZDHHC15 {ECO:0000250|UniProtKB:Q8BGJ0}; DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q8BGJ0}; DE AltName: Full=Zinc finger DHHC domain-containing protein 15; DE Short=DHHC-15; GN Name=ZDHHC15 {ECO:0000312|HGNC:HGNC:20342}; ORFNames=UNQ1969/PRO4501; 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] (ISOFORMS 1 AND 3). RC TISSUE=Brain, and 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 [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 TISSUE SPECIFICITY, AND POSSIBLE INVOLVEMENT IN MRX91. RX PubMed=15915161; DOI=10.1038/sj.ejhg.5201445; RA Mansouri M.R., Marklund L., Gustavsson P., Davey E., Carlsson B., RA Larsson C., White I., Gustavson K.-H., Dahl N.; RT "Loss of ZDHHC15 expression in a woman with a balanced translocation RT t(X;15)(q13.3;cen) and severe mental retardation."; RL Eur. J. Hum. Genet. 13:970-977(2005). RN [6] RP SUBCELLULAR LOCATION. 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 [7] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=18817523; DOI=10.1111/j.1600-0854.2008.00814.x; RA McCormick P.J., Dumaresq-Doiron K., Pluviose A.S., Pichette V., Tosato G., RA Lefrancois S.; RT "Palmitoylation controls recycling in lysosomal sorting and trafficking."; RL Traffic 9:1984-1997(2008). RN [8] RP FUNCTION. RX PubMed=19956733; DOI=10.1371/journal.pgen.1000748; RA Mill P., Lee A.W., Fukata Y., Tsutsumi R., Fukata M., Keighren M., RA Porter R.M., McKie L., Smyth I., Jackson I.J.; RT "Palmitoylation regulates epidermal homeostasis and hair follicle RT differentiation."; RL PLoS Genet. 5:e1000748-e1000748(2009). RN [9] RP FUNCTION. RX PubMed=23034182; DOI=10.1091/mbc.e12-05-0336; RA Ohno Y., Kashio A., Ogata R., Ishitomi A., Yamazaki Y., Kihara A.; RT "Analysis of substrate specificity of human DHHC protein acyltransferases RT using a yeast expression system."; RL Mol. Biol. Cell 23:4543-4551(2012). CC -!- FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate CC onto various protein substrates (PubMed:18817523, PubMed:23034182). Has CC no stringent fatty acid selectivity and in addition to palmitate can CC also transfer onto target proteins myristate from tetradecanoyl-CoA and CC stearate from octadecanoyl-CoA (By similarity). Palmitoylates IGF2R and CC SORT1, promoting their partitioning to an endosomal membrane subdomain CC where they can interact with the retromer cargo-selective complex CC (PubMed:18817523). Thereby, regulates retrograde transport from CC endosomes to the Golgi apparatus of these lysosomal sorting receptors CC and plays a role in trafficking of lysosomal proteins CC (PubMed:18817523). In the nervous system, catalyzes the palmitoylation CC of DLG4/PSD95 and regulates its synaptic clustering and function in CC synaptogenesis (By similarity). Could be involved in the CC differentiation of dopaminergic neurons and the development of the CC diencephalon (By similarity). Could also catalyze the palmitoylation of CC GAP43 (By similarity). Could also palmitoylate DNAJC5 and regulate its CC localization to the Golgi membrane (By similarity). Could also CC palmitoylate FYN as shown in vitro (PubMed:19956733). CC {ECO:0000250|UniProtKB:F1QXD3, ECO:0000250|UniProtKB:Q8BGJ0, CC ECO:0000269|PubMed:18817523, ECO:0000269|PubMed:19956733, CC ECO:0000269|PubMed:23034182}. 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:18817523}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684; CC Evidence={ECO:0000269|PubMed:18817523}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-cysteinyl-[protein] + tetradecanoyl-CoA = CoA + S- CC tetradecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59736, Rhea:RHEA- CC COMP:10131, Rhea:RHEA-COMP:15433, ChEBI:CHEBI:29950, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:143199; CC Evidence={ECO:0000250|UniProtKB:Q8BGJ0}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737; CC Evidence={ECO:0000250|UniProtKB:Q8BGJ0}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-cysteinyl-[protein] + octadecanoyl-CoA = CoA + S- CC octadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59740, Rhea:RHEA- CC COMP:10131, Rhea:RHEA-COMP:15434, ChEBI:CHEBI:29950, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:143200; CC Evidence={ECO:0000250|UniProtKB:Q8BGJ0}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741; CC Evidence={ECO:0000250|UniProtKB:Q8BGJ0}; CC -!- INTERACTION: CC Q96MV8; P41586-2: ADCYAP1R1; NbExp=3; IntAct=EBI-12837904, EBI-17241711; CC Q96MV8; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-12837904, EBI-11343438; CC Q96MV8; Q12983: BNIP3; NbExp=3; IntAct=EBI-12837904, EBI-749464; CC Q96MV8; O14523: C2CD2L; NbExp=3; IntAct=EBI-12837904, EBI-12822627; CC Q96MV8; P11912: CD79A; NbExp=3; IntAct=EBI-12837904, EBI-7797864; CC Q96MV8; P08218: CELA2B; NbExp=3; IntAct=EBI-12837904, EBI-11478642; CC Q96MV8; Q5T4B2: CERCAM; NbExp=3; IntAct=EBI-12837904, EBI-12261896; CC Q96MV8; Q8IUN9: CLEC10A; NbExp=3; IntAct=EBI-12837904, EBI-2873246; CC Q96MV8; P58418: CLRN1; NbExp=3; IntAct=EBI-12837904, EBI-17274839; CC Q96MV8; Q96BA8: CREB3L1; NbExp=5; IntAct=EBI-12837904, EBI-6942903; CC Q96MV8; P00387: CYB5R3; NbExp=3; IntAct=EBI-12837904, EBI-1046040; CC Q96MV8; P78329: CYP4F2; NbExp=3; IntAct=EBI-12837904, EBI-1752413; CC Q96MV8; Q8N5I4: DHRSX; NbExp=3; IntAct=EBI-12837904, EBI-3923585; CC Q96MV8; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-12837904, EBI-781551; CC Q96MV8; Q96D05-2: FAM241B; NbExp=3; IntAct=EBI-12837904, EBI-12118888; CC Q96MV8; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-12837904, EBI-11991950; CC Q96MV8; Q2TAP0: GOLGA7B; NbExp=3; IntAct=EBI-12837904, EBI-13310443; CC Q96MV8; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-12837904, EBI-13345167; CC Q96MV8; Q68G75: LEMD1; NbExp=3; IntAct=EBI-12837904, EBI-12268900; CC Q96MV8; O95214: LEPROTL1; NbExp=3; IntAct=EBI-12837904, EBI-750776; CC Q96MV8; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-12837904, EBI-2820517; CC Q96MV8; Q8N8F7: LSMEM1; NbExp=3; IntAct=EBI-12837904, EBI-10200825; CC Q96MV8; Q8IX19: MCEMP1; NbExp=3; IntAct=EBI-12837904, EBI-2816356; CC Q96MV8; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-12837904, EBI-3923617; CC Q96MV8; Q8N912: NRAC; NbExp=3; IntAct=EBI-12837904, EBI-12051377; CC Q96MV8; Q9P0S3: ORMDL1; NbExp=3; IntAct=EBI-12837904, EBI-1054848; CC Q96MV8; Q53FV1: ORMDL2; NbExp=3; IntAct=EBI-12837904, EBI-11075081; CC Q96MV8; Q9Y5Y5: PEX16; NbExp=3; IntAct=EBI-12837904, EBI-981985; CC Q96MV8; Q9Y342: PLLP; NbExp=3; IntAct=EBI-12837904, EBI-3919291; CC Q96MV8; O60831: PRAF2; NbExp=3; IntAct=EBI-12837904, EBI-2506064; CC Q96MV8; P15151: PVR; NbExp=3; IntAct=EBI-12837904, EBI-3919694; CC Q96MV8; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-12837904, EBI-8636004; CC Q96MV8; Q9BWM7: SFXN3; NbExp=3; IntAct=EBI-12837904, EBI-1171999; CC Q96MV8; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-12837904, EBI-18159983; CC Q96MV8; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-12837904, EBI-12188413; CC Q96MV8; Q6UX34: SNORC; NbExp=3; IntAct=EBI-12837904, EBI-11957067; CC Q96MV8; Q13277: STX3; NbExp=3; IntAct=EBI-12837904, EBI-1394295; CC Q96MV8; Q0VAB0: TBXA2R; NbExp=3; IntAct=EBI-12837904, EBI-18271435; CC Q96MV8; Q9UIK5: TMEFF2; NbExp=3; IntAct=EBI-12837904, EBI-11423693; CC Q96MV8; Q9BXJ8: TMEM120A; NbExp=3; IntAct=EBI-12837904, EBI-727322; CC Q96MV8; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-12837904, EBI-10171534; CC Q96MV8; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-12837904, EBI-10694905; CC Q96MV8; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-12837904, EBI-2339195; CC Q96MV8; Q9H0R3: TMEM222; NbExp=3; IntAct=EBI-12837904, EBI-347385; CC Q96MV8; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-12837904, EBI-12038591; CC Q96MV8; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-12837904, EBI-18178701; CC Q96MV8; O14763: TNFRSF10B; NbExp=6; IntAct=EBI-12837904, EBI-518882; CC Q96MV8; A0AVG3: TSNARE1; NbExp=3; IntAct=EBI-12837904, EBI-12003468; CC Q96MV8; A0A384ME17: TUFM; NbExp=3; IntAct=EBI-12837904, EBI-12261790; CC Q96MV8; Q9Y385: UBE2J1; NbExp=3; IntAct=EBI-12837904, EBI-988826; CC Q96MV8; O95183: VAMP5; NbExp=3; IntAct=EBI-12837904, EBI-10191195; CC Q96MV8; O95292: VAPB; NbExp=3; IntAct=EBI-12837904, EBI-1188298; CC Q96MV8; Q9BSR8: YIPF4; NbExp=3; IntAct=EBI-12837904, EBI-751253; CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000269|PubMed:16647879}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:F1QXD3}. Postsynaptic density CC {ECO:0000250|UniProtKB:Q2TGJ4}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q96MV8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96MV8-2; Sequence=VSP_013206, VSP_013207, VSP_013208; CC Name=3; CC IsoId=Q96MV8-3; Sequence=VSP_013206; CC -!- TISSUE SPECIFICITY: Expressed in placenta, liver, lung, kidney, heart CC and brain. {ECO:0000269|PubMed:15915161}. CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity. CC {ECO:0000250|UniProtKB:Q8BGJ0}. CC -!- PTM: Autopalmitoylated (in vitro). {ECO:0000250|UniProtKB:F1QXD3}. CC -!- DISEASE: Intellectual developmental disorder, X-linked 91 (MRX91) CC [MIM:300577]: A disorder characterized by significantly below average CC general intellectual functioning associated with impairments in CC adaptive behavior and manifested during the developmental period. CC {ECO:0000269|PubMed:15915161}. Note=The disease may be caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY358786; AAQ89146.1; -; mRNA. DR EMBL; AK056374; BAB71168.1; -; mRNA. DR EMBL; AK122885; BAG53779.1; -; mRNA. DR EMBL; AC020717; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL137013; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL391055; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC103980; AAI03981.1; -; mRNA. DR EMBL; BC103981; AAI03982.1; -; mRNA. DR EMBL; BC103982; AAI03983.1; -; mRNA. DR CCDS; CCDS14430.1; -. [Q96MV8-1] DR CCDS; CCDS55454.1; -. [Q96MV8-3] DR RefSeq; NP_001139728.1; NM_001146256.1. [Q96MV8-3] DR RefSeq; NP_001139729.1; NM_001146257.1. [Q96MV8-2] DR RefSeq; NP_659406.1; NM_144969.2. [Q96MV8-1] DR RefSeq; XP_006724687.1; XM_006724624.3. [Q96MV8-1] DR AlphaFoldDB; Q96MV8; -. DR SMR; Q96MV8; -. DR BioGRID; 127719; 122. DR IntAct; Q96MV8; 54. DR MINT; Q96MV8; -. DR STRING; 9606.ENSP00000362465; -. DR iPTMnet; Q96MV8; -. DR PhosphoSitePlus; Q96MV8; -. DR BioMuta; ZDHHC15; -. DR DMDM; 37999855; -. DR MassIVE; Q96MV8; -. DR PaxDb; 9606-ENSP00000362465; -. DR PeptideAtlas; Q96MV8; -. DR ProteomicsDB; 77420; -. [Q96MV8-2] DR Antibodypedia; 13846; 119 antibodies from 21 providers. DR DNASU; 158866; -. DR Ensembl; ENST00000373367.8; ENSP00000362465.3; ENSG00000102383.14. [Q96MV8-1] DR Ensembl; ENST00000541184.1; ENSP00000445420.1; ENSG00000102383.14. [Q96MV8-3] DR GeneID; 158866; -. DR KEGG; hsa:158866; -. DR MANE-Select; ENST00000373367.8; ENSP00000362465.3; NM_144969.3; NP_659406.1. DR UCSC; uc004ecg.4; human. [Q96MV8-1] DR AGR; HGNC:20342; -. DR CTD; 158866; -. DR DisGeNET; 158866; -. DR GeneCards; ZDHHC15; -. DR HGNC; HGNC:20342; ZDHHC15. DR HPA; ENSG00000102383; Low tissue specificity. DR MalaCards; ZDHHC15; -. DR MIM; 300576; gene. DR MIM; 300577; phenotype. DR neXtProt; NX_Q96MV8; -. DR OpenTargets; ENSG00000102383; -. DR PharmGKB; PA134945089; -. DR VEuPathDB; HostDB:ENSG00000102383; -. DR eggNOG; KOG1315; Eukaryota. DR GeneTree; ENSGT00940000158214; -. DR HOGENOM; CLU_027721_1_1_1; -. DR InParanoid; Q96MV8; -. DR OMA; KLPIYTR; -. DR OrthoDB; 6683at2759; -. DR PhylomeDB; Q96MV8; -. DR TreeFam; TF316044; -. DR PathwayCommons; Q96MV8; -. DR SignaLink; Q96MV8; -. DR BioGRID-ORCS; 158866; 8 hits in 772 CRISPR screens. DR ChiTaRS; ZDHHC15; human. DR GenomeRNAi; 158866; -. DR Pharos; Q96MV8; Tbio. DR PRO; PR:Q96MV8; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q96MV8; Protein. DR Bgee; ENSG00000102383; Expressed in primordial germ cell in gonad and 112 other cell types or tissues. DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB. DR GO; GO:0098794; C:postsynapse; ISS:UniProtKB. DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell. DR GO; GO:0016409; F:palmitoyltransferase activity; IDA:UniProtKB. DR GO; GO:0019705; F:protein-cysteine S-myristoyltransferase activity; IEA:RHEA. DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IDA:UniProtKB. DR GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; IEA:RHEA. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IDA:UniProtKB. DR GO; GO:1900006; P:positive regulation of dendrite development; ISS:UniProtKB. DR GO; GO:0072657; P:protein localization to membrane; IMP:UniProtKB. DR GO; GO:0062237; P:protein localization to postsynapse; ISS:UniProtKB. DR GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB. DR GO; GO:0140450; P:protein targeting to Golgi apparatus; IMP:UniProtKB. DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central. DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB. DR GO; GO:0016188; P:synaptic vesicle maturation; IBA:GO_Central. DR InterPro; IPR001594; Palmitoyltrfase_DHHC. DR PANTHER; PTHR12246; PALMITOYLTRANSFERASE ZDHHC16; 1. DR PANTHER; PTHR12246:SF13; PALMITOYLTRANSFERASE ZDHHC16; 1. DR Pfam; PF01529; DHHC; 1. DR PROSITE; PS50216; DHHC; 1. DR Genevisible; Q96MV8; HS. PE 1: Evidence at protein level; KW Acyltransferase; Alternative splicing; Golgi apparatus; KW Intellectual disability; Lipoprotein; Membrane; Metal-binding; Palmitate; KW Reference proteome; Synapse; Transferase; Transmembrane; KW Transmembrane helix; Zinc. FT CHAIN 1..337 FT /note="Palmitoyltransferase ZDHHC15" FT /id="PRO_0000212893" FT TOPO_DOM 1..20 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:F1QXD3" FT TRANSMEM 21..41 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:F1QXD3" FT TOPO_DOM 42..56 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:F1QXD3" FT TRANSMEM 57..77 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:F1QXD3" FT TOPO_DOM 78..172 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:F1QXD3" FT TRANSMEM 173..193 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:F1QXD3" FT TOPO_DOM 194..210 FT /note="Lumenal" FT /evidence="ECO:0000250|UniProtKB:F1QXD3" FT TRANSMEM 211..234 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:F1QXD3" FT TOPO_DOM 235..337 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:F1QXD3" FT DOMAIN 129..179 FT /note="DHHC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067" FT REGION 306..337 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 159 FT /note="S-palmitoyl cysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067" FT BINDING 131 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:F1QXD3" FT BINDING 134 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:F1QXD3" FT BINDING 144 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:F1QXD3" FT BINDING 145 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:F1QXD3" FT BINDING 148 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:F1QXD3" FT BINDING 151 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:F1QXD3" FT BINDING 158 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:F1QXD3" FT BINDING 165 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:F1QXD3" FT VAR_SEQ 46..54 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:12975309, FT ECO:0000303|PubMed:14702039" FT /id="VSP_013206" FT VAR_SEQ 127..152 FT /note="AVRFCDRCHLIKPDRCHHCSVCAMCV -> GQFIQRQLERQLSKYLRKAKSY FT MFSN (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12975309" FT /id="VSP_013207" FT VAR_SEQ 153..337 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12975309" FT /id="VSP_013208" SQ SEQUENCE 337 AA; 39331 MW; 6D7F920921E5D124 CRC64; MRRGWKMALS GGLRCCRRVL SWVPVLVIVL VVLWSYYAYV FELCLVTVLS PAEKVIYLIL YHAIFVFFTW TYWKSIFTLP QQPNQKFHLS YTDKERYENE ERPEVQKQML VDMAKKLPVY TRTGSGAVRF CDRCHLIKPD RCHHCSVCAM CVLKMDHHCP WVNNCIGFSN YKFFLQFLAY SVLYCLYIAT TVFSYFIKYW RGELPSVRSK FHVLFLLFVA CMFFVSLVIL FGYHCWLVSR NKTTLEAFCT PVFTSGPEKN GFNLGFIKNI QQVFGDKKKF WLIPIGSSPG DGHSFPMRSM NESQNPLLAN EETWEDNEDD NQDYPEGSSS LAVETET //