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ZD18A_DANRE
ID   ZD18A_DANRE             Reviewed;         467 AA.
AC   E7FH11; F1Q6I2; Q08C71;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2018, sequence version 3.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Palmitoyltransferase ZDHHC18-A {ECO:0000305};
DE            EC=2.3.1.225 {ECO:0000250|UniProtKB:Q9NUE0};
DE   AltName: Full=Zinc finger DHHC domain-containing protein 18-A {ECO:0000303|PubMed:27235108, ECO:0000312|ZFIN:ZDB-GENE-060929-424};
GN   Name=zdhhc18a {ECO:0000303|PubMed:27235108,
GN   ECO:0000312|ZFIN:ZDB-GENE-060929-424};
GN   Synonyms=pigv {ECO:0000312|ZFIN:ZDB-GENE-060929-424};
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].
RC   STRAIN=AB; TISSUE=Embryo {ECO:0000312|EMBL:AAI24361.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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 could catalyze the addition of
CC       palmitate onto various protein substrates.
CC       {ECO:0000250|UniProtKB:Q9NUE0}.
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:Q9NUE0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC         Evidence={ECO:0000250|UniProtKB:Q9NUE0};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q9NUE0}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DEVELOPMENTAL STAGE: Probably maternally supplied, the zygotic
CC       expression becomes significative at 4 hpf.
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; BX649265; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC124360; AAI24361.1; -; mRNA.
DR   RefSeq; NP_001071031.1; NM_001077563.1.
DR   AlphaFoldDB; E7FH11; -.
DR   SMR; E7FH11; -.
DR   Ensembl; ENSDART00000101885; ENSDARP00000092660; ENSDARG00000069807.
DR   Ensembl; ENSDART00000130540; ENSDARP00000112051; ENSDARG00000069807.
DR   GeneID; 564062; -.
DR   KEGG; dre:564062; -.
DR   CTD; 564062; -.
DR   ZFIN; ZDB-GENE-060929-424; zdhhc18a.
DR   GeneTree; ENSGT00940000156585; -.
DR   HOGENOM; CLU_018741_0_0_1; -.
DR   InParanoid; E7FH11; -.
DR   OrthoDB; 1264614at2759; -.
DR   TreeFam; TF312923; -.
DR   TreeFam; TF314515; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 16.
DR   Bgee; ENSDARG00000069807; Expressed in cleaving embryo and 24 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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:0016409; F:palmitoyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR   GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IBA:GO_Central.
DR   GO; GO:0006612; P:protein targeting to membrane; 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; Golgi apparatus; Lipoprotein; Membrane; Palmitate;
KW   Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..467
FT                   /note="Palmitoyltransferase ZDHHC18-A"
FT                   /id="PRO_0000451102"
FT   TOPO_DOM        1..59
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        81..88
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        110..204
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        226..247
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        269..467
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          161..211
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   ACT_SITE        191
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   CONFLICT        167
FT                   /note="K -> R (in Ref. 2; AAI24361)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        339
FT                   /note="D -> V (in Ref. 2; AAI24361)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   467 AA;  51688 MW;  5C69D7ADB3E2E575 CRC64;
     MKNCEYQQID PRALRTPSSR TSSTLPCGRK GSQRLRRKWE VFPGKNRFYC DGRIMLARQC
     GVLPLTIGLI FITSVLFFTF DCPFLVDHLT VFIPVIGGVL FIFVVISLLQ TSFTDPGILP
     RALPDEAADI EKQIDNSGSS TYRPPPRTKE ILINDQVVKL KYCFTCKMFR PPRTSHCSLC
     DNCVERFDHH CPWVGNCVGK RNYRFFYAFI VSLSFLTSFI FGCVITHLTL RSQGGNGFIQ
     AIQDSPASVV ELVICFFSIW SILGLSGFHT YLVASNLTTN EDIKGSWSSK RGEESGNPYT
     YNNIFTNCCV VLCGPMPPSL IDRRGFVPPE DAPQTVTSDA ELPAFMAKND TNMCAQGTKE
     LLESMANSTV IQSTCAPGKP KTAPVTQESL LNTVSITVSP PSKPPSNGCS GRQARRPIDV
     PCSQRGLKRA ALHTHKPMLR LPSPLYSLSD SPLILSDAPD MGFIPLN
 
 
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