ZDHC5_MOUSE
ID ZDHC5_MOUSE Reviewed; 715 AA.
AC Q8VDZ4; Q2TGE8; Q69ZB5; Q8R2X7;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Palmitoyltransferase ZDHHC5;
DE EC=2.3.1.225 {ECO:0000269|PubMed:22081607, ECO:0000269|PubMed:24562000, ECO:0000269|PubMed:30605677};
DE AltName: Full=Zinc finger DHHC domain-containing protein 5;
DE Short=DHHC-5;
GN Name=Zdhhc5; Synonyms=Kiaa1748;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RA Huang C.-H., Chen Y., Ye T.;
RT "A superfamily of membrane-associated DHHC type zinc finger proteins.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II, and FVB/10; TISSUE=Brain, and Mammary gland;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-299 AND SER-345, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-91, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-299; SER-380 AND
RP SER-621, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH DLG4, AND TISSUE
RP SPECIFICITY.
RX PubMed=20178993; DOI=10.1074/jbc.m109.079426;
RA Li Y., Hu J., Hoefer K., Wong A.M., Cooper J.D., Birnbaum S.G.,
RA Hammer R.E., Hofmann S.L.;
RT "DHHC5 interacts with PDZ domain 3 of post-synaptic density-95 (PSD-95)
RT protein and plays a role in learning and memory.";
RL J. Biol. Chem. 285:13022-13031(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-294; SER-296; SER-299;
RP THR-303; SER-345; THR-348; THR-350; SER-380; SER-429; SER-432; THR-436 AND
RP SER-621, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21820437; DOI=10.1016/j.febslet.2011.07.028;
RA Kokkola T., Kruse C., Roy-Pogodzik E.M., Pekkinen J., Bauch C., Honck H.H.,
RA Hennemann H., Kreienkamp H.J.;
RT "Somatostatin receptor 5 is palmitoylated by the interacting ZDHHC5
RT palmitoyltransferase.";
RL FEBS Lett. 585:2665-2670(2011).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, MUTAGENESIS OF CYS-134, AND ACTIVE
RP SITE.
RX PubMed=22081607; DOI=10.1074/jbc.m111.306183;
RA Li Y., Martin B.R., Cravatt B.F., Hofmann S.L.;
RT "DHHC5 protein palmitoylates flotillin-2 and is rapidly degraded on
RT induction of neuronal differentiation in cultured cells.";
RL J. Biol. Chem. 287:523-530(2012).
RN [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-697, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [13]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24562000; DOI=10.1038/nn.3657;
RA Brigidi G.S., Sun Y., Beccano-Kelly D., Pitman K., Mobasser M.,
RA Borgland S.L., Milnerwood A.J., Bamji S.X.;
RT "Palmitoylation of delta-catenin by DHHC5 mediates activity-induced synapse
RT plasticity.";
RL Nat. Neurosci. 17:522-532(2014).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=30605677; DOI=10.1016/j.celrep.2018.12.022;
RA Wang J., Hao J.W., Wang X., Guo H., Sun H.H., Lai X.Y., Liu L.Y., Zhu M.,
RA Wang H.Y., Li Y.F., Yu L.Y., Xie C., Wang H.R., Mo W., Zhou H.M., Chen S.,
RA Liang G., Zhao T.J.;
RT "DHHC4 and DHHC5 Facilitate Fatty Acid Uptake by Palmitoylating and
RT Targeting CD36 to the Plasma Membrane.";
RL Cell Rep. 26:209-221(2019).
RN [15]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=34724258; DOI=10.1002/glia.24113;
RA Ma Y., Liu H., Ou Z., Qi C., Xing R., Wang S., Han Y., Zhao T.J., Chen Y.;
RT "DHHC5 facilitates oligodendrocyte development by palmitoylating and
RT activating STAT3.";
RL Glia 70:379-392(2022).
CC -!- FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate
CC onto various protein substrates such as CTNND2, CD36, STAT3 and S1PR1
CC thus plays a role in various biological processes including cell
CC adhesion, fatty acid uptake, bacterial sensing or cardiac functions
CC (PubMed:21820437, PubMed:22081607). Plays an important role in the
CC regulation of synapse efficacy by mediating palmitoylation of delta-
CC catenin/CTNND2, thereby increasing synaptic delivery and surface
CC stabilization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic
CC acid receptors (AMPARs) (PubMed:24562000). Under basal conditions,
CC remains at the synaptic membrane through FYN-mediated phosphorylation
CC that prevents association with endocytic proteins. Neuronal activity
CC enhances the internalization and trafficking of DHHC5 from spines to
CC dendritic shafts where it palmitoylates delta-catenin/CTNND2. Regulates
CC cell adhesion at the plasma membrane by palmitoylating GOLGA7B and
CC DSG2. Plays a role in innate immune response by mediating the
CC palmitoylation of NOD1 and NOD2 and their proper recruitment to the
CC bacterial entry site and phagosomes. Participates also in fatty acid
CC uptake by palmitoylating CD36 and thereby targeting it to the plasma
CC membrane (PubMed:30605677). Upon binding of fatty acids to CD36, gets
CC phosphorylated by LYN leading to inactivation and subsequent CD36
CC caveolar endocytosis. Controls oligodendrocyte development by
CC catalyzing STAT3 palmitoylation (PubMed:34724258).
CC {ECO:0000250|UniProtKB:Q9C0B5, ECO:0000269|PubMed:21820437,
CC ECO:0000269|PubMed:22081607, ECO:0000269|PubMed:24562000,
CC ECO:0000269|PubMed:30605677, ECO:0000269|PubMed:34724258}.
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:22081607,
CC ECO:0000269|PubMed:24562000, ECO:0000269|PubMed:30605677};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000269|PubMed:22081607, ECO:0000269|PubMed:24562000,
CC ECO:0000269|PubMed:30605677};
CC -!- INTERACTION:
CC Q8VDZ4; Q9D428: GOLGA7B; NbExp=2; IntAct=EBI-7057556, EBI-25635843;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21820437,
CC ECO:0000269|PubMed:30605677}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VDZ4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VDZ4-2; Sequence=VSP_006936, VSP_006937;
CC -!- TISSUE SPECIFICITY: Highly enriched in brain, detectable in liver and
CC heart, and undetectable in most other tissues.
CC {ECO:0000269|PubMed:20178993}.
CC -!- INDUCTION: In neural stem cells, rapid up-regulation by EGF, combined
CC with FGF2 and heparin.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- PTM: Phosphorylation regulates association with endocytic proteins and
CC its subcellular localization. Phosphorylation by LYN during fatty acid
CC uptake leads to inactivation of the activity.
CC {ECO:0000250|UniProtKB:Q9C0B5}.
CC -!- PTM: Autopalmitoylated (By similarity). Palmitoylation of the C-
CC terminal tail regulates stimulation-dependent plasma membrane motility
CC (By similarity). {ECO:0000250|UniProtKB:Q2THW7,
CC ECO:0000250|UniProtKB:Q9C0B5}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant mice are born at half the
CC expected rate, and survivors show a marked deficit in contextual fear
CC conditioning, an indicator of defective hippocampal-dependent learning
CC (PubMed:20178993). Loss of ZDHHC5 in oligodendrocytes inhibits
CC myelination and reduces the expression levels of myelin-related and
CC anti-apoptosis genes (PubMed:34724258). {ECO:0000269|PubMed:20178993,
CC ECO:0000269|PubMed:34724258}.
CC -!- MISCELLANEOUS: In neural stem cells, rapidly degraded through the
CC proteasome pathway following growth factors withdrawal, a strategy used
CC to induce differentiation. {ECO:0000269|PubMed:22081607}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC ERF2/ZDHHC9 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32529.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY894891; AAX73370.1; -; mRNA.
DR EMBL; AK082513; BAC38513.1; -; mRNA.
DR EMBL; AK075641; BAC35875.1; -; mRNA.
DR EMBL; AK173251; BAD32529.1; ALT_INIT; mRNA.
DR EMBL; BC020051; AAH20051.1; -; mRNA.
DR EMBL; BC027047; AAH27047.1; -; mRNA.
DR EMBL; BC065155; AAH65155.1; -; mRNA.
DR CCDS; CCDS16190.1; -. [Q8VDZ4-1]
DR RefSeq; NP_659136.1; NM_144887.4. [Q8VDZ4-1]
DR AlphaFoldDB; Q8VDZ4; -.
DR BioGRID; 230716; 2.
DR IntAct; Q8VDZ4; 3.
DR MINT; Q8VDZ4; -.
DR STRING; 10090.ENSMUSP00000048198; -.
DR iPTMnet; Q8VDZ4; -.
DR PhosphoSitePlus; Q8VDZ4; -.
DR SwissPalm; Q8VDZ4; -.
DR EPD; Q8VDZ4; -.
DR jPOST; Q8VDZ4; -.
DR MaxQB; Q8VDZ4; -.
DR PaxDb; Q8VDZ4; -.
DR PeptideAtlas; Q8VDZ4; -.
DR PRIDE; Q8VDZ4; -.
DR ProteomicsDB; 275140; -. [Q8VDZ4-1]
DR ProteomicsDB; 275141; -. [Q8VDZ4-2]
DR Antibodypedia; 3027; 102 antibodies from 21 providers.
DR DNASU; 228136; -.
DR Ensembl; ENSMUST00000035840; ENSMUSP00000048198; ENSMUSG00000034075. [Q8VDZ4-1]
DR GeneID; 228136; -.
DR KEGG; mmu:228136; -.
DR UCSC; uc008kiz.2; mouse. [Q8VDZ4-1]
DR CTD; 25921; -.
DR MGI; MGI:1923573; Zdhhc5.
DR VEuPathDB; HostDB:ENSMUSG00000034075; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000156001; -.
DR HOGENOM; CLU_013779_0_0_1; -.
DR InParanoid; Q8VDZ4; -.
DR OMA; LAPRYMG; -.
DR OrthoDB; 1264614at2759; -.
DR PhylomeDB; Q8VDZ4; -.
DR TreeFam; TF354263; -.
DR BRENDA; 2.3.1.225; 3474.
DR BioGRID-ORCS; 228136; 11 hits in 75 CRISPR screens.
DR ChiTaRS; Zdhhc5; mouse.
DR PRO; PR:Q8VDZ4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8VDZ4; protein.
DR Bgee; ENSMUSG00000034075; Expressed in seminiferous tubule of testis and 258 other tissues.
DR Genevisible; Q8VDZ4; MM.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0016409; F:palmitoyltransferase activity; IDA:MGI.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0062208; P:positive regulation of pattern recognition receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:1905171; P:positive regulation of protein localization to phagocytic vesicle; IMP:UniProtKB.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; IDA:MGI.
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; Cell membrane; Immunity;
KW Innate immunity; Lipid transport; Lipoprotein; Membrane; Methylation;
KW Palmitate; Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..715
FT /note="Palmitoyltransferase ZDHHC5"
FT /id="PRO_0000212869"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..52
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..191
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..715
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 104..154
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 289..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..646
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 134
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000305|PubMed:22081607"
FT MOD_RES 91
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 294
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 303
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 348
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 350
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 411
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 436
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 617
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 659
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C0B5"
FT MOD_RES 697
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 641..652
FT /note="KAPSGVSETEEV -> NPHLVSQRQRK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_006936"
FT VAR_SEQ 653..715
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_006937"
FT MUTAGEN 134
FT /note="C->S: Loss of palmitoyltransferase activity."
FT /evidence="ECO:0000269|PubMed:22081607"
SQ SEQUENCE 715 AA; 77501 MW; 6FD8E83FA3D3F961 CRC64;
MPAESGKRFK PSKYVPVSAA AIFLVGATTL FFAFTCPGLS LNVSPAVPIY NAIMFLFVLA
NFSMATFMDP GIFPRAEEDE DKEDDFRAPL YKTVEIKGIQ VRMKWCATCR FYRPPRCSHC
SVCDNCVEEF DHHCPWVNNC IGRRNYRYFF LFLLSLTAHI MGVFGFGLLY VLYHIEELSG
VRTAVTMAVM CVAGLFFIPV AGLTGFHVVL VARGRTTNEQ VTGKFRGGVN PFTNGCCNNV
SRVLCSSPAP RYLGRPKKEK TIVIRPPFLR PEVSDGQITV KIMDNGIQGE LRRTKSKGSL
EITESQSADA EPPPPPKPDL SRYTGLRTHL SLATNEDSSL LGKDSPPTPT MYKYRPGYSS
SSTSAAMPHS SSAKLSRGDS LKEPTSIADS SRHPSYRSEP SLEPESFRSP TFGKSFHFDP
LSSGSRSSSL KSAQGTGFEL GQLQSIRSEG TTSTSYKSLA NQTRNGSLSY DSLLTPSDSP
DFESVQAGPE PDPPLGYTSP FLSARLAQQR EAERHPRLLP TGPPHREPSP VRYDNLSRHI
VASLQEREKL LRQSPPLAGR EEEPGLGDSG IQSTPGSGHA PRTSSSSDDS KRSPLSKTPL
GRPAVPRFGK PDGLRSRGLG SPEPGTTAPY LGRSISYSSQ KAPSGVSETE EVALQPLLTP
KDEVQLKTTY SKSNGQPKSI GSASPGPGQP PLSSPTRGGV KKVSGVGGTT YEISV
