DHC5B_DANRE
ID DHC5B_DANRE Reviewed; 658 AA.
AC E7FBS9;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Palmitoyltransferase ZDHHC5-B {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q8VDZ4};
DE AltName: Full=Zdhhc5-like {ECO:0000303|PubMed:27235108};
DE AltName: Full=Zinc finger DHHC domain-containing protein 5-B {ECO:0000305};
DE Short=DHHC-5B {ECO:0000305};
GN Name=zdhhc5b {ECO:0000312|ZFIN:ZDB-GENE-101117-1};
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 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; CR855307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_009289570.1; XM_009291295.2.
DR RefSeq; XP_009289571.1; XM_009291296.2.
DR AlphaFoldDB; E7FBS9; -.
DR SMR; E7FBS9; -.
DR STRING; 7955.ENSDARP00000104903; -.
DR PaxDb; E7FBS9; -.
DR Ensembl; ENSDART00000128508; ENSDARP00000104903; ENSDARG00000087417.
DR GeneID; 792560; -.
DR KEGG; dre:792560; -.
DR CTD; 792560; -.
DR ZFIN; ZDB-GENE-101117-1; zdhhc5b.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000156001; -.
DR HOGENOM; CLU_013779_2_0_1; -.
DR InParanoid; E7FBS9; -.
DR OMA; LAPRYMG; -.
DR OrthoDB; 1264614at2759; -.
DR PhylomeDB; E7FBS9; -.
DR TreeFam; TF354263; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 14.
DR Bgee; ENSDARG00000087417; Expressed in zone of skin and 24 other tissues.
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..658
FT /note="Palmitoyltransferase ZDHHC5-B"
FT /id="PRO_0000451034"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..56
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..202
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..658
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 115..165
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 306..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..592
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
SQ SEQUENCE 658 AA; 70489 MW; D20E046D1149B89E CRC64;
MPVGLSVGGA LGDPSPSRPF RPSRYVPVSA ATAFLVGATT LFLCFTCPWL SEKFSSFIPL
YNVVVFLFTL ANFCMATFMD PGVFPRAEED EDKEDDFRAP LYKTVEVRGI QVRMKWCSTC
RFYRPPRCSH CSVCDNCVEE FDHHCPWVNN CIGRRNYRYF FLFLLSLTVH IMDVFGFSLL
YILHHTKQLD LVQSGVTMAV MCVAGLFFVP VAGLTGFHVV LVARGRTTNE QVTGKFRGGV
NPFTHGCFKN IAHVLCSSQA PRYLGRLRKP QSVQVQPPFL RPPLSEAQLA AKVLDNGIQQ
SKSSLEIMES QSTDADPPPP PKPEHRYPGL PHTQNEECSL LTEAPPTPSL YKYRPAYSSP
GKNHTASTHS SKMSRGNSMT ESPSVPVTTG QPSYRSDPSL SSRGAAGCRG GAEGGRSGSG
GLGGASAFGG RSYPSFTDTL LQSAAASCSS SLRSAHTAHN ALGPLISEGT TSTSYKSLAN
QTRNGSLSYE SLLTPSESPE FESAAHELSP PRPHPPHSLS TAAGAAPILG YTSPFLSAQQ
REGSLQACPA PLRPSPNRAF LRPISSPPSR APPLSPRARS LGSPPPGPAP GHTPLGKSMS
YGGGAELQHR PSSSGGGTSM PNSTIKQNVA NHNTHSHKPA RGVKKVSGVG GTTYEISV
