DHC5A_DANRE
ID DHC5A_DANRE Reviewed; 744 AA.
AC Q2THW0;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Palmitoyltransferase ZDHHC5-A {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q8VDZ4};
DE AltName: Full=Zinc finger DHHC domain-containing protein 5-A {ECO:0000305};
DE Short=DHHC-5A {ECO:0000305};
GN Name=zdhhc5a {ECO:0000312|ZFIN:ZDB-GENE-090312-92};
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 [MRNA].
RA Chen Y., Huang C.-H.;
RT "A superfamily of membrane-associated DHHC type zinc finger proteins.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 catalyzes the addition of palmitate
CC onto various protein substrates and is involved in a variety of
CC cellular processes. {ECO:0000250|UniProtKB:Q8VDZ4}.
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:Q8VDZ4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q8VDZ4};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8VDZ4};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Probably maternally supplied, the zygotic
CC expression is detected early during development at the 512-cell stage.
CC {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}.
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DR EMBL; AY871210; AAX68543.1; -; mRNA.
DR EMBL; BX511158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX908740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001034729.1; NM_001039640.1.
DR RefSeq; XP_005160302.1; XM_005160245.3.
DR AlphaFoldDB; Q2THW0; -.
DR SMR; Q2THW0; -.
DR STRING; 7955.ENSDARP00000123884; -.
DR PaxDb; Q2THW0; -.
DR Ensembl; ENSDART00000003497; ENSDARP00000009029; ENSDARG00000016263.
DR Ensembl; ENSDART00000147702; ENSDARP00000123884; ENSDARG00000016263.
DR GeneID; 571795; -.
DR KEGG; dre:571795; -.
DR CTD; 571795; -.
DR ZFIN; ZDB-GENE-090312-92; zdhhc5a.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000156001; -.
DR HOGENOM; CLU_013779_2_0_1; -.
DR InParanoid; Q2THW0; -.
DR OMA; SGGRPCT; -.
DR OrthoDB; 1264614at2759; -.
DR PhylomeDB; Q2THW0; -.
DR TreeFam; TF354263; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 1.
DR Bgee; ENSDARG00000016263; Expressed in cleaving embryo and 26 other tissues.
DR ExpressionAtlas; Q2THW0; baseline and differential.
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:UniProtKB-EC.
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 2: Evidence at transcript level;
KW Acyltransferase; Cell membrane; Lipoprotein; Membrane; Methylation;
KW Palmitate; Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..744
FT /note="Palmitoyltransferase ZDHHC5-A"
FT /id="PRO_0000451033"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..61
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..208
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..744
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 121..171
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..602
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
SQ SEQUENCE 744 AA; 80501 MW; 288957115D2B1B2D CRC64;
MPSGSMSGGV SGPTSPPHPT VPSRPLRPSR YVPVSAATAF LVGSTTLFFC FTCPWLSEQF
SVAVPIYNGV MFMFVLANFC MATFMDPGIF PRAEEDEDKE DDFRAPLYKT VEIRGIQVRM
KWCSTCRFYR PPRCSHCSVC DNCVEDFDHH CPWVNNCIGR RNYRYFFLFL LSLTAHIMGV
FGFGLLFILY HTQQLDRVHS AVTMAVMCVA GLFFIPVAGL TGFHVVLVAR GRTTNEQVTG
KFRGGVNPFT NGCLRNVSHV LCSSQAPRYL GRKRKAQTVS VQPPFLRPQL TEAQLAAKVL
DNGIQGDLHR SKSSLEMMES QSADAEPPPP PKPELRYPGL SRGPAGHSEE SSLLNKAPPT
PTMFKYRPTY SSPGKNHTAL THAYANQSSQ QPGYRSEPSL DGREGGGAER SGAERTGGGP
GGPPGSGIPG YSLGGRSYPS FSDPTVLAER ASRSSSVRST HNAPPSEATT STSYKSLANQ
TPPQAARNGS LSYDSLLTPS ESPDFESAAP EMSPGRPRTP VVGYSSPFLS AQIAHQREAE
LHQPVASSSA LMASPQHAVF LRGSGSPPVP PERERERLLH DSQAQHHHHH HHHHHHHRPP
RFSRPPLLSD SGPPQPSYPY RTRSTDTTHP PRSPHPPPLG KSLSYSSAAA AEMQYRLVRK
ASASVAGGGI QAPKDEIQMK SYSRTNGQPK PSSTPSSPTH PISVSTRPGQ AHSSAGSSQS
PAHKPGGGVK KVTGVGGTTY EISV
