ZDHC8_MOUSE
ID ZDHC8_MOUSE Reviewed; 762 AA.
AC Q5Y5T5; Q7TNF7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Palmitoyltransferase ZDHHC8 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q9ULC8};
DE AltName: Full=Zinc finger DHHC domain-containing protein 8 {ECO:0000312|MGI:MGI:1338012};
DE Short=DHHC-8 {ECO:0000250|UniProtKB:Q9ULC8};
GN Name=Zdhhc8 {ECO:0000312|MGI:MGI:1338012};
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].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15603741; DOI=10.1016/j.neuron.2004.12.005;
RA Fukata M., Fukata Y., Adesnik H., Nicoll R.A., Bredt D.S.;
RT "Identification of PSD-95 palmitoylating enzymes.";
RL Neuron 44:987-996(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 527-762.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15184899; DOI=10.1038/ng1375;
RA Mukai J., Liu H., Burt R.A., Swor D.E., Lai W.-S., Karayiorgou M.,
RA Gogos J.A.;
RT "Evidence that the gene encoding ZDHHC8 contributes to the risk of
RT schizophrenia.";
RL Nat. Genet. 36:725-731(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=18775783; DOI=10.1016/j.mcn.2008.07.027;
RA Maynard T.M., Meechan D.W., Dudevoir M.L., Gopalakrishna D., Peters A.Z.,
RA Heindel C.C., Sugimoto T.J., Wu Y., Lieberman J.A., Lamantia A.S.;
RT "Mitochondrial localization and function of a subset of 22q11 deletion
RT syndrome candidate genes.";
RL Mol. Cell. Neurosci. 39:439-451(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-624, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Spleen;
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 [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-439, 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).
CC -!- FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate
CC onto various protein substrates and therefore functions in several
CC unrelated biological processes. Through the palmitoylation of ABCA1
CC regulates the localization of the transporter to the plasma membrane
CC and thereby regulates its function in cholesterol and phospholipid
CC efflux (By similarity). Could also pamitoylate the D(2) dopamine
CC receptor DRD2 and regulate its stability and localization to the plasma
CC membrane (By similarity). Could also play a role in glutamatergic
CC transmission (PubMed:15184899). {ECO:0000250|UniProtKB:Q9ULC8,
CC ECO:0000269|PubMed:15184899}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151;
CC EC=2.3.1.225; Evidence={ECO:0000250|UniProtKB:Q9ULC8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q9ULC8};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9ULC8}; Multi-pass membrane protein
CC {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:18775783};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in brain cortex and hippocampus.
CC {ECO:0000269|PubMed:15184899}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- DISRUPTION PHENOTYPE: Mice have normal brain morphology, but female
CC have strong locomotor deficits in open field, due to a greater fear of
CC new environments. {ECO:0000269|PubMed:15184899}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC ERF2/ZDHHC9 subfamily. {ECO:0000305}.
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DR EMBL; AY668947; AAU89701.1; -; mRNA.
DR EMBL; BC055694; AAH55694.1; -; mRNA.
DR CCDS; CCDS28017.1; -.
DR RefSeq; NP_742163.4; NM_172151.4.
DR AlphaFoldDB; Q5Y5T5; -.
DR SMR; Q5Y5T5; -.
DR STRING; 10090.ENSMUSP00000076224; -.
DR iPTMnet; Q5Y5T5; -.
DR PhosphoSitePlus; Q5Y5T5; -.
DR SwissPalm; Q5Y5T5; -.
DR jPOST; Q5Y5T5; -.
DR MaxQB; Q5Y5T5; -.
DR PaxDb; Q5Y5T5; -.
DR PRIDE; Q5Y5T5; -.
DR ProteomicsDB; 302124; -.
DR Antibodypedia; 328; 154 antibodies from 29 providers.
DR DNASU; 27801; -.
DR Ensembl; ENSMUST00000076957; ENSMUSP00000076224; ENSMUSG00000060166.
DR GeneID; 27801; -.
DR KEGG; mmu:27801; -.
DR UCSC; uc007ymx.1; mouse.
DR CTD; 29801; -.
DR MGI; MGI:1338012; Zdhhc8.
DR VEuPathDB; HostDB:ENSMUSG00000060166; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000158044; -.
DR HOGENOM; CLU_013779_1_0_1; -.
DR InParanoid; Q5Y5T5; -.
DR OMA; TAEQITM; -.
DR OrthoDB; 1264614at2759; -.
DR PhylomeDB; Q5Y5T5; -.
DR TreeFam; TF354263; -.
DR Reactome; R-MMU-8963896; HDL assembly.
DR BioGRID-ORCS; 27801; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Zdhhc8; mouse.
DR PRO; PR:Q5Y5T5; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q5Y5T5; protein.
DR Bgee; ENSMUSG00000060166; Expressed in primary visual cortex and 72 other tissues.
DR ExpressionAtlas; Q5Y5T5; baseline and differential.
DR Genevisible; Q5Y5T5; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0016409; F:palmitoyltransferase activity; ISO:MGI.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:UniProtKB.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; ISO:MGI.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR030291; ZDHHC8.
DR PANTHER; PTHR12349:SF1; PTHR12349:SF1; 1.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Golgi apparatus; Lipoprotein; Membrane; Methylation;
KW Mitochondrion; Palmitate; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..762
FT /note="Palmitoyltransferase ZDHHC8"
FT /id="PRO_0000212878"
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="Lumenal"
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..190
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..762
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 104..154
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 289..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..531
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 134
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 439
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULC8"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULC8"
FT MOD_RES 722
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULC8"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULC8"
SQ SEQUENCE 762 AA; 82031 MW; 28FC98CACA74B2E8 CRC64;
MPRSPGTRLK PAKYIPVATA AALLVGSSTL FFVFTCPWLT RAVSPAIPVY NGILFLFVLA
NFSMATFMDP GVFPRADEDE DKEDDFRAPL YKNVDVRGIQ VRMKWCATCH FYRPPRCSHC
SVCDNCVEDF DHHCPWVNNC IGRRNYRYFF LFLLSLSAHM VGVVAFGLLY VLNHSEGLGA
AHTTITMAVM CVAGLFFIPV IGLTGFHVVL VTRGRTTNEQ VTGKFRGGVN PFTRGCYGNV
EHVLCSPLAP RYVVEPPRMP LSVSLKPPFL RPELLERAVP LKVKLSDNGL KAGRSKSKGS
LDQLDEKPLD LGPPLPPKIE AGTFGRDLKT PRPGSAESAL SVQRTSPPTP AMYKFRPAFS
TGPKTPFCGP NEQVPGPDSL TLADDSTHSL DFVSEPSLDL PDHGPGGLRP PYPPSPPLNT
TDAFSGALRS LSLKAASRRG GDHMTLQPLR SEGGPPTPHR SLFAPHALPN RNGSLSYDSL
LNPGSPSGHA CPTHPSVGIA SYHSPYLHPG PSDPPRPPPR SFSPVLGPRP REPSPVRYDN
LSRTIMASIQ ERKDREERER LLRSQTDSLF GDSGVYDTPS SYSLQQASVL TEGPRGSVLR
YGSRDDLVAG PGFGGARNPA LQTSLSSLSS SMSRAPRTSS SSLQADQANN NAPGPRPGSG
SHRSPARQGL PSPPGTPRSP SYTGSKAVAF IHTDLPDRQP SLAMQRDHPQ LKTPPSKLNG
QSPGMARLGP AASPMGPNAS PARHTLVKKV SGVGGTTYEI SV
