ZH15B_DANRE
ID ZH15B_DANRE Reviewed; 332 AA.
AC F1QXD3;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Palmitoyltransferase ZDHHC15B {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000269|PubMed:29326245};
DE AltName: Full=Acyltransferase ZDHHC15B {ECO:0000250|UniProtKB:Q8BGJ0};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q8BGJ0};
DE AltName: Full=Zinc finger DHHC domain-containing protein 15B;
GN Name=zdhhc15b {ECO:0000312|ZFIN:ZDB-GENE-061110-106};
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 FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=26095893; DOI=10.1002/jcb.25256;
RA Wang F., Chen X., Shi W., Yao L., Gao M., Yang Y., Hao A.;
RT "Zdhhc15b Regulates Differentiation of Diencephalic Dopaminergic Neurons in
RT zebrafish.";
RL J. Cell. Biochem. 116:2980-2991(2015).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) IN COMPLEX WITH ZINC, FUNCTION,
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=29326245; DOI=10.1126/science.aao6326;
RA Rana M.S., Kumar P., Lee C.J., Verardi R., Rajashankar K.R., Banerjee A.;
RT "Fatty acyl recognition and transfer by an integral membrane S-
RT acyltransferase.";
RL Science 359:0-0(2018).
CC -!- FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate
CC onto various protein substrates (PubMed:29326245). Has no stringent
CC fatty acid selectivity and in addition to palmitate can also transfer
CC onto target proteins myristate from tetradecanoyl-CoA and stearate from
CC octadecanoyl-CoA (By similarity). May thereby regulate target proteins
CC association and localization to membranes (By similarity). In the
CC nervous system, probably catalyzes the palmitoylation of synaptic
CC proteins and is involved in the differentiation of dopaminergic neurons
CC and the development of the diencephalon (PubMed:26095893).
CC {ECO:0000250|UniProtKB:Q8BGJ0, ECO:0000250|UniProtKB:Q96MV8,
CC ECO:0000269|PubMed:26095893, ECO:0000269|PubMed:29326245}.
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:0000269|PubMed:29326245};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000305|PubMed:29326245};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + tetradecanoyl-CoA = CoA + S-
CC tetradecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59736, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:15433, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:143199;
CC Evidence={ECO:0000250|UniProtKB:Q8BGJ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737;
CC Evidence={ECO:0000250|UniProtKB:Q8BGJ0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + octadecanoyl-CoA = CoA + S-
CC octadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59740, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:15434, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:143200;
CC Evidence={ECO:0000250|UniProtKB:Q8BGJ0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741;
CC Evidence={ECO:0000250|UniProtKB:Q8BGJ0};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:29326245}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:29326245}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q2TGJ4}.
CC -!- DEVELOPMENTAL STAGE: Maternally supplied mRNAs are initially observed
CC (PubMed:26095893). Ubiquitous zygotic expression is visible at 3 hours
CC post-fertilization/hpf and strongly increases from 8 hpf to 48 hpf
CC (PubMed:26095893). From 10 hpf, the expression progressively
CC concentrates in the anterior neural plate (PubMed:26095893). From 18
CC hpf through 48 hpf, expression is abundant in the forebrain, especially
CC in the diencephalon (PubMed:26095893). {ECO:0000269|PubMed:26095893}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8BGJ0}.
CC -!- PTM: Autopalmitoylated (in vitro). {ECO:0000269|PubMed:29326245}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown has no effect on development
CC till 18 hpf (PubMed:26095893). At 24 hpf, the embryos exhibit abnormal
CC brain development with indistinguishable boundaries among different
CC regions in the forebrain and a slightly reduced size of diencephalon
CC (PubMed:26095893). A reduction in mature dopaminergic neurons is
CC observed associated within learning and memory deficits
CC (PubMed:26095893). {ECO:0000269|PubMed:26095893}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000255|RuleBase:RU079119}.
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DR EMBL; CR812849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 6BMS; X-ray; 2.44 A; A/D=1-332.
DR PDBsum; 6BMS; -.
DR AlphaFoldDB; F1QXD3; -.
DR SMR; F1QXD3; -.
DR STRING; 7955.ENSDARP00000097436; -.
DR PaxDb; F1QXD3; -.
DR Ensembl; ENSDART00000106658; ENSDARP00000097436; ENSDARG00000071872.
DR ZFIN; ZDB-GENE-061110-106; zdhhc15b.
DR eggNOG; KOG1315; Eukaryota.
DR GeneTree; ENSGT00940000158214; -.
DR HOGENOM; CLU_027721_1_1_1; -.
DR InParanoid; F1QXD3; -.
DR OMA; AICVLKM; -.
DR PhylomeDB; F1QXD3; -.
DR TreeFam; TF316044; -.
DR PRO; PR:F1QXD3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 14.
DR Bgee; ENSDARG00000071872; Expressed in mature ovarian follicle and 28 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0030173; C:integral component of Golgi membrane; IMP:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0019705; F:protein-cysteine S-myristoyltransferase activity; IEA:RHEA.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; IEA:RHEA.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0071542; P:dopaminergic neuron differentiation; IMP:ZFIN.
DR GO; GO:0030900; P:forebrain development; IMP:ZFIN.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IDA:UniProtKB.
DR GO; GO:0072657; P:protein localization to membrane; ISS:UniProtKB.
DR GO; GO:0045234; P:protein palmitoleylation; IDA:ZFIN.
DR GO; GO:0140450; P:protein targeting to Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR GO; GO:0016188; P:synaptic vesicle maturation; IBA:GO_Central.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Golgi apparatus; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Reference proteome; Synapse; Transferase;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..332
FT /note="Palmitoyltransferase ZDHHC15B"
FT /id="PRO_0000444031"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:29326245"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29326245"
FT TOPO_DOM 36..50
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:29326245"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29326245"
FT TOPO_DOM 72..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:29326245"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29326245"
FT TOPO_DOM 188..204
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:29326245"
FT TRANSMEM 205..228
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29326245"
FT TOPO_DOM 229..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:29326245"
FT DOMAIN 123..173
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 305..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 153
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29326245,
FT ECO:0007744|PDB:6BMS"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29326245,
FT ECO:0007744|PDB:6BMS"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q5W0Z9"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29326245,
FT ECO:0007744|PDB:6BMS"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29326245,
FT ECO:0007744|PDB:6BMS"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29326245,
FT ECO:0007744|PDB:6BMS"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29326245,
FT ECO:0007744|PDB:6BMS"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29326245,
FT ECO:0007744|PDB:6BMS"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29326245,
FT ECO:0007744|PDB:6BMS"
FT HELIX 9..14
FT /evidence="ECO:0007829|PDB:6BMS"
FT HELIX 17..34
FT /evidence="ECO:0007829|PDB:6BMS"
FT HELIX 36..40
FT /evidence="ECO:0007829|PDB:6BMS"
FT HELIX 45..71
FT /evidence="ECO:0007829|PDB:6BMS"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:6BMS"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:6BMS"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:6BMS"
FT TURN 126..129
FT /evidence="ECO:0007829|PDB:6BMS"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:6BMS"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:6BMS"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:6BMS"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:6BMS"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:6BMS"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:6BMS"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:6BMS"
FT HELIX 165..194
FT /evidence="ECO:0007829|PDB:6BMS"
FT HELIX 207..233
FT /evidence="ECO:0007829|PDB:6BMS"
FT HELIX 238..242
FT /evidence="ECO:0007829|PDB:6BMS"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:6BMS"
FT HELIX 260..268
FT /evidence="ECO:0007829|PDB:6BMS"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:6BMS"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:6BMS"
SQ SEQUENCE 332 AA; 38798 MW; 2E3621187B11540A CRC64;
MALSRALRCC QRIFSWIPVI IISSVVLWSY YAYVFELCFV TLSNNLERVT YLLIFHVCFI
MFCWTYWKAI FTPPSTPTKK FHLSYTDKER YEMEERPEVQ KQILVDIAKK LPIFTRAQSG
AIRFCDRCQV IKPDRCHHCS VCETCVLKMD HHCPWVNNCV GFSNYKFFLL FLSYSMIYCV
FIASTVFQYF LKFWVGDLPN GPAKFHVLFL LFVALMFFVS LMFLFGYHCW LVAKNRSTLE
AFSPPVFQNG PDRNGFNVGL SKNLRQVFGE HKKLWFIPVF TSQGDGHYFP LRTLRESENP
LLANEEKWVE DGGSDEESAD ENGSSLLIRT ES
