ZDHC9_DANRE
ID ZDHC9_DANRE Reviewed; 386 AA.
AC F1R013; A7YT88;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Palmitoyltransferase ZDHHC9 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q9Y397};
DE AltName: Full=DHHC domain-containing protein 9 {ECO:0000303|PubMed:26056731};
DE AltName: Full=Zinc finger DHHC domain-containing protein 9 {ECO:0000303|PubMed:27235108};
DE Short=DHHC-9;
GN Name=zdhhc9 {ECO:0000303|PubMed:27235108,
GN ECO:0000312|ZFIN:ZDB-GENE-071004-8};
GN Synonyms=dhcc9 {ECO:0000303|PubMed:26056731};
GN ORFNames=zgc:136936 {ECO:0000312|EMBL:AAI15337.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-386.
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=26056731; DOI=10.1016/j.ntt.2015.06.001;
RA Wang C., Chen X., Shi W., Wang F., Du Z., Li X., Yao Y., Liu T., Shao T.,
RA Li G., Hao A.;
RT "2-Bromopalmitate impairs neural stem/progenitor cell proliferation,
RT promotes cell apoptosis and induces malformation in zebrafish embryonic
RT brain.";
RL Neurotoxicol. Teratol. 50:53-63(2015).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=27235108; DOI=10.1016/j.bbrc.2016.05.074;
RA Du Z., Chen X., Li X., He K., Ji S., Shi W., Hao A.;
RT "Protein palmitoylation activate zygotic gene expression during the
RT maternal-to-zygotic transition.";
RL Biochem. Biophys. Res. Commun. 475:194-201(2016).
CC -!- FUNCTION: Palmitoyltransferase that could catalyze the addition of
CC palmitate onto various protein substrates.
CC {ECO:0000250|UniProtKB:Q9Y397}.
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:Q9Y397};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q9Y397};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Y397}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Y397};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Probably maternally supplied, the zygotic
CC expression becomes significative at the 512-cell stage and increases
CC until 10 hpf and then decreases but is still detected at 24 hpf.
CC {ECO:0000269|PubMed:26056731, ECO:0000269|PubMed:27235108}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC ERF2/ZDHHC9 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI15337.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BX004980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC115336; AAI15337.1; ALT_INIT; mRNA.
DR RefSeq; NP_001103496.1; NM_001110026.1.
DR AlphaFoldDB; F1R013; -.
DR SMR; F1R013; -.
DR STRING; 7955.ENSDARP00000079770; -.
DR PaxDb; F1R013; -.
DR Ensembl; ENSDART00000085335; ENSDARP00000079770; ENSDARG00000060515.
DR GeneID; 560095; -.
DR KEGG; dre:560095; -.
DR CTD; 51114; -.
DR ZFIN; ZDB-GENE-071004-8; zdhhc9.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000159999; -.
DR HOGENOM; CLU_018741_3_1_1; -.
DR InParanoid; F1R013; -.
DR OMA; PLVYQRW; -.
DR OrthoDB; 1264614at2759; -.
DR TreeFam; TF312923; -.
DR Reactome; R-DRE-9648002; RAS processing.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 14.
DR Bgee; ENSDARG00000060515; Expressed in intestine and 25 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
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:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR030292; ZDHHC9.
DR PANTHER; PTHR22883:SF71; PTHR22883:SF71; 1.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Endoplasmic reticulum; Golgi apparatus; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..386
FT /note="Palmitoyltransferase ZDHHC9"
FT /id="PRO_0000451040"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..63
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..224
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 139..189
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 306..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 169
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT CONFLICT 320
FT /note="V -> L (in Ref. 2; AAI15337)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="C -> G (in Ref. 2; AAI15337)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 386 AA; 42793 MW; DD4EED0617A6288C CRC64;
MSAVMITRKI TRKWEKLPGK NTFCCDGRVM MARQKGVFYL TLFLIVGTCS LFFAFECPYL
AVHLSPAIPV FAVLLFVFVM AMLLRTSFSD PGVLPRALPE EANFIEMEIE AANGNVLAGQ
RPPPRIKNVQ INNQIVKLKY CYTCKIFRPP RASHCSICDN CVDRFDHHCP WVGNCVGKRN
YRYFYLFTLS LSLLTIYIFA FDIVHVVLRS VDSGFVNTLK ETPGTVLEVL VCFFTLWSVV
GLTGFHTYLI SLNQTTNEDI KGSWSGKNRV QNPYSHKNII KNCCEVLCGP TYPSVLDRRG
LMLEDSCSSA PSNGATTVPV NKSSNPATQT TKSSAPLIPN EHTPDEAKPS ICSGTQKSSS
SPKEEKPSSP ISPNAVAPAV IKESTH
