ZD16B_DANRE
ID ZD16B_DANRE Reviewed; 382 AA.
AC A0A0R4IF99; A0A0R4IX74; F1R4N0; R4GEX6;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Palmitoyltransferase ZDHHC16B {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q969W1};
DE AltName: Full=Zinc finger DHHC domain-containing protein 16B {ECO:0000305};
DE Short=DHHC-16B {ECO:0000305};
GN Name=zdhhc16b {ECO:0000312|ZFIN:ZDB-GENE-040426-1301};
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).
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). {ECO:0000250|UniProtKB:Q969W1,
CC ECO:0000250|UniProtKB:Q9ESG8}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=A0A0R4IF99-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0A0R4IF99-2; Sequence=VSP_059246, VSP_059249;
CC Name=3;
CC IsoId=A0A0R4IF99-3; Sequence=VSP_059245, VSP_059247, VSP_059249;
CC Name=4;
CC IsoId=A0A0R4IF99-4; Sequence=VSP_059248;
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; CU459184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001314728.1; NM_001327799.1. [A0A0R4IF99-4]
DR RefSeq; XP_009304660.1; XM_009306385.2. [A0A0R4IF99-1]
DR RefSeq; XP_009304661.1; XM_009306386.1.
DR AlphaFoldDB; A0A0R4IF99; -.
DR SMR; A0A0R4IF99; -.
DR STRING; 7955.ENSDARP00000127039; -.
DR PaxDb; A0A0R4IF99; -.
DR Ensembl; ENSDART00000152772; ENSDARP00000127039; ENSDARG00000015989. [A0A0R4IF99-4]
DR GeneID; 393316; -.
DR KEGG; dre:393316; -.
DR CTD; 393316; -.
DR ZFIN; ZDB-GENE-040426-1301; zdhhc16b.
DR eggNOG; KOG1313; Eukaryota.
DR GeneTree; ENSGT00940000155032; -.
DR OMA; CPVRINQ; -.
DR OrthoDB; 1491968at2759; -.
DR PRO; PR:A0A0R4IF99; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 12.
DR Bgee; ENSDARG00000015989; Expressed in early embryo and 26 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; 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 InterPro; IPR039859; ZDH16.
DR PANTHER; PTHR12246; PTHR12246; 1.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Alternative splicing; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..382
FT /note="Palmitoyltransferase ZDHHC16B"
FT /id="PRO_0000442462"
FT TOPO_DOM 1..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..107
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 108..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..275
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 153..203
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 183
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT VAR_SEQ 175..183
FT /note="CILKMDHHC -> YTTHTHTHT (in isoform 3)"
FT /id="VSP_059245"
FT VAR_SEQ 214..239
FT /note="ISAKDMFLDAYNAIESGRYKGGASQG -> INRNQRGETHQPQGETTTQTQG
FT ESTS (in isoform 2)"
FT /id="VSP_059246"
FT VAR_SEQ 214..239
FT /note="ISAKDMFLDAYNAIESGRYKGGASQG -> IRRNQRGETHQPQGETTTQTQG
FT ETFP (in isoform 3)"
FT /id="VSP_059247"
FT VAR_SEQ 229..255
FT /note="Missing (in isoform 4)"
FT /id="VSP_059248"
FT VAR_SEQ 240..382
FT /note="Missing (in isoform 2 and isoform 3)"
FT /id="VSP_059249"
SQ SEQUENCE 382 AA; 44693 MW; C2EC5B381E415D2E CRC64;
MRSWRWSVSR IMRLFLRWFR LCPRRGHRKR SRVRDLWNYG MVVLKSLYYN VQTNSDTVLD
CMFEPIYWLV DNMTRWFGVV FVCLVMALTS SVVVIVYLCV LPIIFSSYPV YWILWHLCYG
HWNLLMVVFH YYKATTTQPG FPPQEKTDIP TVTICKKCIV PKPARTHHCS ICNRCILKMD
HHCPWLNNCV GHFNHRYFFS FCLFMTMGCV YCSISAKDMF LDAYNAIESG RYKGGASQGE
AVPGAGLIYI SFQHQSSYQT PPPAFTHQER MVHKSLVYLW VLTSSVAVAL GALTLWHAIL
ITRGETSVER HINRKERRRL KLRGKLFRNP YHHGRINNWR IFFGVEKGSD WLWRVLLPST
HPPLGDGLTW DCPAYKSSTT AI