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ZD16A_DANRE
ID   ZD16A_DANRE             Reviewed;         387 AA.
AC   B8A4F0; Q7SXG0;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Palmitoyltransferase ZDHHC16A {ECO:0000305};
DE            EC=2.3.1.225 {ECO:0000250|UniProtKB:Q969W1};
DE   AltName: Full=Zinc finger DHHC domain-containing protein 16A {ECO:0000305};
DE            Short=DHHC-16A {ECO:0000305};
GN   Name=zdhhc16a {ECO:0000312|ZFIN:ZDB-GENE-040426-1621};
GN   Synonyms=zdhhc16 {ECO:0000303|PubMed:26663717};
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].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=26663717; DOI=10.1002/dneu.22372;
RA   Shi W., Chen X., Wang F., Gao M., Yang Y., Du Z., Wang C., Yao Y., He K.,
RA   Hao A.;
RT   "ZDHHC16 modulates FGF/ERK dependent proliferation of neural
RT   stem/progenitor cells in the zebrafish telencephalon.";
RL   Dev. Neurobiol. 76:1014-1028(2016).
CC   -!- FUNCTION: Palmitoyl acyltransferase that mediates palmitoylation of
CC       proteins and is required during embryonic heart development. Involved
CC       in the proliferation of neural stem cells by regulating the FGF/ERK
CC       pathway (By similarity). Involved in the proliferation of neural stem
CC       cells by regulating the FGF/ERK pathway (PubMed:26663717).
CC       {ECO:0000250|UniProtKB:Q969W1, ECO:0000250|UniProtKB:Q9ESG8,
CC       ECO:0000269|PubMed:26663717}.
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:Q969W1};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q969W1}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9ESG8}.
CC   -!- TISSUE SPECIFICITY: Expressed in the central nervous system (CNS)
CC       (PubMed:26663717). Expressed in the developing forebrain, and
CC       especially in the telencephalon (PubMed:26663717).
CC       {ECO:0000269|PubMed:26663717}.
CC   -!- DEVELOPMENTAL STAGE: Maternally expressed in the at four-cell stage.
CC       Highly expressed in the developing anterior neural plate since tailbud
CC       stage. During the segmentation period, 24 hour post fertilization
CC       (hpf), expression is still enriched in cell clusters at prosencephalon
CC       and mesencephalon. {ECO:0000269|PubMed:26663717}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC       {ECO:0000250|UniProtKB:Q8IUH5}.
CC   -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
CC       malformation in telencephalon (PubMed:26663717). Impaired neural
CC       stem/progenitor cells (NSPCs) proliferation in the telencephalon
CC       (PubMed:26663717). {ECO:0000269|PubMed:26663717}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; BX072537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC055620; AAH55620.1; -; mRNA.
DR   RefSeq; NP_957336.1; NM_201042.1.
DR   RefSeq; XP_017214211.1; XM_017358722.1.
DR   AlphaFoldDB; B8A4F0; -.
DR   STRING; 7955.ENSDARP00000119367; -.
DR   PaxDb; B8A4F0; -.
DR   Ensembl; ENSDART00000134630; ENSDARP00000119367; ENSDARG00000007808.
DR   GeneID; 394017; -.
DR   KEGG; dre:394017; -.
DR   CTD; 394017; -.
DR   ZFIN; ZDB-GENE-040426-1621; zdhhc16a.
DR   eggNOG; KOG1313; Eukaryota.
DR   GeneTree; ENSGT00940000155032; -.
DR   HOGENOM; CLU_054274_0_0_1; -.
DR   InParanoid; B8A4F0; -.
DR   OMA; VEAVSMC; -.
DR   OrthoDB; 1491968at2759; -.
DR   PhylomeDB; B8A4F0; -.
DR   TreeFam; TF320809; -.
DR   PRO; PR:B8A4F0; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 13.
DR   Bgee; ENSDARG00000007808; Expressed in early embryo and 25 other tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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; IEA:UniProtKB-EC.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0021898; P:commitment of multipotent stem cells to neuronal lineage in forebrain; IMP:ZFIN.
DR   GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR   GO; GO:0021899; P:fibroblast growth factor receptor signaling pathway involved in forebrain neuron fate commitment; IMP:ZFIN.
DR   GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR   GO; GO:0018345; P:protein palmitoylation; ISS:UniProtKB.
DR   GO; GO:0021537; P:telencephalon development; IMP:UniProtKB.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   InterPro; IPR039859; ZDH16.
DR   PANTHER; PTHR12246; PTHR12246; 1.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Endoplasmic reticulum; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..387
FT                   /note="Palmitoyltransferase ZDHHC16A"
FT                   /id="PRO_0000442461"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          150..200
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   ACT_SITE        180
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   CONFLICT        41
FT                   /note="F -> S (in Ref. 2; AAH55620)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        203
FT                   /note="T -> A (in Ref. 2; AAH55620)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        371
FT                   /note="D -> G (in Ref. 2; AAH55620)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   387 AA;  44531 MW;  0454F0A56B929858 CRC64;
     MHPCSSVLHL LLRCMRGCCR HTRSRVPRRL RRHVSYIRLI FKSLYFNSLT NSDVVTDSIL
     EPVFWMVEVV TRWFGMVFVF LVVALTSSVV FIAYFCLLPL VLHTYSPGWM IWHICYGHWN
     LVMIVFHYYK ATKTPPGYPP KMKTDVPFVS VCKKCIIPKP ARSHHCGICK TCILKMDHHC
     PWLNNCVGHF NHRYFFSFCL FLTLGCMYCS VSGRHLFIDA YNTIDQLKHL EAEKQGVPVT
     GIGLLIGIVP SAGVAGKAVQ VAQEVSQPPY TYKDRMFHKS VIYMWVLTST VSVALGALTL
     WHALLITRGE TSIERHINGK EAKRLAKRGR VYRNPFSYGK LNNWKVFFGV EKRSHWLTRV
     LLPSGHAPYG DGLTWDIYPL KKDMMPV
 
 
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