ZDHC8_DROME
ID ZDHC8_DROME Reviewed; 934 AA.
AC Q9W345; A8JUM2; A8JUM5; M9NGX0; X2JE99; X2JJ56;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 4.
DT 03-AUG-2022, entry version 167.
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:0000250|UniProtKB:Q9ULC8};
DE AltName: Full=Zinc finger DHHC-type containing 8 {ECO:0000303|PubMed:30735487, ECO:0000312|FlyBase:FBgn0085478};
GN Name=Zdhhc8 {ECO:0000303|PubMed:30735487, ECO:0000312|FlyBase:FBgn0085478};
GN Synonyms=anon-Pen16 {ECO:0000312|EMBL:AAF46491.4},
GN Dm_X:47283 {ECO:0000312|EMBL:AAF46491.4},
GN p16 {ECO:0000312|EMBL:AAF46491.4};
GN ORFNames=CG34449 {ECO:0000312|FlyBase:FBgn0085478};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=30735487; DOI=10.1371/journal.pone.0198149;
RA Strassburger K., Kang E., Teleman A.A.;
RT "Drosophila ZDHHC8 palmitoylates scribble and Ras64B and controls growth
RT and viability.";
RL PLoS ONE 14:e0198149-e0198149(2019).
CC -!- FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate
CC onto various protein substrates and therefore functions in several
CC unrelated biological processes (By similarity). Regulates tissue growth
CC possibly by regulating Ras64B protein stability (PubMed:30735487). May
CC regulate CG34450 mRNA levels (PubMed:30735487).
CC {ECO:0000250|UniProtKB:Q5Y5T5, ECO:0000250|UniProtKB:Q9ULC8,
CC ECO:0000269|PubMed:30735487}.
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:0000269|PubMed:30735487}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:30735487}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=A {ECO:0000312|FlyBase:FBgn0085478};
CC IsoId=Q9W345-1; Sequence=Displayed;
CC Name=B {ECO:0000312|FlyBase:FBgn0085478};
CC IsoId=Q9W345-2; Sequence=VSP_061159;
CC Name=C {ECO:0000312|FlyBase:FBgn0085478};
CC IsoId=Q9W345-6; Sequence=VSP_061159, VSP_061161, VSP_061162;
CC Name=D {ECO:0000312|FlyBase:FBgn0085478};
CC IsoId=Q9W345-5; Sequence=VSP_061161, VSP_061162;
CC Name=F {ECO:0000312|FlyBase:FBgn0085478};
CC IsoId=Q9W345-4; Sequence=VSP_061160;
CC Name=G {ECO:0000312|FlyBase:FBgn0085478};
CC IsoId=Q9W345-3; Sequence=VSP_061158, VSP_061159;
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- DISRUPTION PHENOTYPE: Lethal at larval stage (PubMed:30735487). RNAi-
CC mediated knockdown results in extra vein material (PubMed:30735487).
CC RNAi-mediated knockdown in the wing results in tissue overgrowth due to
CC enhanced cell proliferation (PubMed:30735487).
CC {ECO:0000269|PubMed:30735487}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC ERF2/ZDHHC9 subfamily. {ECO:0000305}.
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DR EMBL; AE014298; AAF46491.4; -; Genomic_DNA.
DR EMBL; AE014298; AFH07306.1; -; Genomic_DNA.
DR EMBL; AE014298; ABW09368.1; -; Genomic_DNA.
DR EMBL; AE014298; ABW09369.1; -; Genomic_DNA.
DR EMBL; AE014298; AHN59522.1; -; Genomic_DNA.
DR EMBL; AE014298; AHN59523.1; -; Genomic_DNA.
DR RefSeq; NP_727339.3; NM_167189.6.
DR SMR; Q9W345; -.
DR IntAct; Q9W345; 8.
DR PRIDE; Q9W345; -.
DR EnsemblMetazoa; FBtr0112753; FBpp0111665; FBgn0085478. [Q9W345-1]
DR EnsemblMetazoa; FBtr0112754; FBpp0111666; FBgn0085478. [Q9W345-2]
DR EnsemblMetazoa; FBtr0112755; FBpp0111667; FBgn0085478. [Q9W345-6]
DR EnsemblMetazoa; FBtr0308591; FBpp0300815; FBgn0085478. [Q9W345-5]
DR EnsemblMetazoa; FBtr0343028; FBpp0309780; FBgn0085478. [Q9W345-4]
DR EnsemblMetazoa; FBtr0343029; FBpp0309781; FBgn0085478. [Q9W345-3]
DR GeneID; 31887; -.
DR KEGG; dme:Dmel_CG34449; -.
DR UCSC; CG34449-RA; d. melanogaster. [Q9W345-1]
DR CTD; 29801; -.
DR FlyBase; FBgn0085478; Zdhhc8.
DR VEuPathDB; VectorBase:FBgn0085478; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000175425; -.
DR HOGENOM; CLU_010307_0_0_1; -.
DR InParanoid; Q9W345; -.
DR OMA; YPWVPAY; -.
DR OrthoDB; 1264614at2759; -.
DR PhylomeDB; Q9W345; -.
DR BioGRID-ORCS; 31887; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 31887; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0085478; Expressed in brain and 23 other tissues.
DR ExpressionAtlas; Q9W345; baseline and differential.
DR Genevisible; Q9W345; DM.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016409; F:palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:RHEA.
DR GO; GO:0018345; P:protein palmitoylation; IBA:GO_Central.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Alternative splicing; Cell membrane; Golgi apparatus;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..934
FT /note="Palmitoyltransferase ZDHHC8"
FT /evidence="ECO:0000305"
FT /id="PRO_0000453525"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..47
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..177
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..934
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 99..149
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 336..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 129
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT VAR_SEQ 71..75
FT /note="Missing (in isoform G)"
FT /evidence="ECO:0000305"
FT /id="VSP_061158"
FT VAR_SEQ 328..350
FT /note="Missing (in isoform B, isoform G and isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_061159"
FT VAR_SEQ 430..511
FT /note="Missing (in isoform F)"
FT /evidence="ECO:0000305"
FT /id="VSP_061160"
FT VAR_SEQ 512..523
FT /note="RSNPGTPTQPRR -> SQYSNSENSTNS (in isoform D and
FT isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_061161"
FT VAR_SEQ 524..934
FT /note="Missing (in isoform D and isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_061162"
SQ SEQUENCE 934 AA; 99717 MW; 8772DDF71B7EE7E3 CRC64;
MPKCDVKTRY IPATFAWIVL LLTTFLFFFY PCQFYVKSHP WVLAYQGVIT FFVLANFTLA
TFMDPGIIPK ASPDEDCEEE LRAPLYKNAE INGITVKMKW CVTCKFYRPP RCSHCSVCNH
CIETFDHHCP WVNNCIGRRN YRFFFFFLVS LSIHMLSIFS LCLVYVLKIM PNIKDTAPIV
AIILMGLVTI LAIPIFGLTG FHMVLVSRGR TTNEQVTGKF KGGYNPFSRG CWHNCCYTQF
GPQYPSLLNP KKYASRRSQV QNQAISTICN DRSGQQTGAG SGAGGNGTAA VSGGGGGVGS
GGGMRGTAVQ YSPRSFYDAS REKRGIQVKT YMAEGNGYNQ RSGSTTLYSK LSPGRECSDT
DLEPPPASQS QDCEPTPPLQ RHNSSSFYLP QVSDSGGLNG SVSTGGGGGG DSPRHMRLYH
PRHSPHARPR GLDPQRGYTS DALSPDHPVG YGVGVNGSQQ QQQQALAAAA AAAAVAAQNQ
RSATTTATPT MQQRIKPLGV ATPLVMASPV RRSNPGTPTQ PRRPDFIGLN AQAVAQQQQQ
QQQAAAAAAA AYYEYTSGLP PQHPQAPSIQ QQQQQLLLQQ QRVLMQHQQQ QQALQQQQQQ
QQQAAVHAAH PQHAALAQAA YGGSPQRRFL SEGELVRQGA GGGVAGGELS YARSNNTVDN
IRELAGSPQR GVYMWKDTSP GFTNNAGQQQ QQQQQAQQVV SSGIGSSAGT LSSSGAAAGV
MPHAQYMTAG GGAHPLIMTH SRLQDYTIQQ QQQQQQQQAA AAAAASYHRS NPTSPTTMPQ
VSGAGQSYIL RYGGGGAVGA AGSSGSLASV TASNPATGGG GYQPALRGGV AVFPPNPMGN
QGGGNLQTQP SPQIKRKQTP TRPMSFVRAL EMADSMEMQS LEQQQNGGIP GSGSVGNNQQ
AGGGGGGHLM QSNASNSGTP DRASIYDMNY EISV
