ZDH15_HUMAN
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 03-AUG-2022, entry version 155.
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; A0A1P0AYU5: SFXN3; NbExp=3; IntAct=EBI-12837904, EBI-14193895;
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}.
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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; 51.
DR IntAct; Q96MV8; 53.
DR STRING; 9606.ENSP00000362465; -.
DR iPTMnet; Q96MV8; -.
DR PhosphoSitePlus; Q96MV8; -.
DR BioMuta; ZDHHC15; -.
DR DMDM; 37999855; -.
DR MassIVE; Q96MV8; -.
DR PaxDb; Q96MV8; -.
DR PeptideAtlas; Q96MV8; -.
DR PRIDE; Q96MV8; -.
DR ProteomicsDB; 77419; -. [Q96MV8-1]
DR ProteomicsDB; 77420; -. [Q96MV8-2]
DR ProteomicsDB; 77421; -. [Q96MV8-3]
DR Antibodypedia; 13846; 98 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 CTD; 158866; -.
DR DisGeNET; 158866; -.
DR GeneCards; ZDHHC15; -.
DR HGNC; HGNC:20342; ZDHHC15.
DR HPA; ENSG00000102383; Low tissue specificity.
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; AICVLKM; -.
DR PhylomeDB; Q96MV8; -.
DR TreeFam; TF316044; -.
DR PathwayCommons; Q96MV8; -.
DR SignaLink; Q96MV8; -.
DR BioGRID-ORCS; 158866; 6 hits in 698 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 ventricular zone and 111 other tissues.
DR Genevisible; Q96MV8; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0030173; C:integral component of 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 Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
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
