ZDH16_HUMAN
ID ZDH16_HUMAN Reviewed; 377 AA.
AC Q969W1; D3DR52; D3DR53; D3DR54; Q5JTG7; Q5JTH0; Q8N4Z6; Q8WY84; Q9BSV3;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Palmitoyltransferase ZDHHC16 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000269|PubMed:28826475};
DE AltName: Full=Abl-philin 2 {ECO:0000303|PubMed:17123647};
DE AltName: Full=Zinc finger DHHC domain-containing protein 16;
DE Short=DHHC-16;
GN Name=ZDHHC16 {ECO:0000312|HGNC:HGNC:20714};
GN Synonyms=APH2 {ECO:0000303|PubMed:17123647}; ORFNames=UNQ2570/PRO6258;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, ALTERNATIVE
RP SPLICING, TISSUE SPECIFICITY, AND INTERACTION WITH COPS5.
RC TISSUE=Placenta;
RX PubMed=17123647; DOI=10.1016/j.bbaexp.2006.10.002;
RA Zhang F., Di Y., Li J., Shi Y., Zhang L., Wang C., He X., Liu Y., Wan D.,
RA Huo K., Gu J.;
RT "Molecular cloning and characterization of human Aph2 gene, involved in AP-
RT 1 regulation by interaction with JAB1.";
RL Biochim. Biophys. Acta 1759:514-525(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Sarafidou T., Moschonas N.K.;
RT "A novel gene containing the cysteine-rich zf-DHHC motif is localised at
RT human chromosomal region 10q23.3-q24.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=B-cell, Brain, Ovary, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28826475; DOI=10.7554/elife.27826;
RA Abrami L., Dallavilla T., Sandoz P.A., Demir M., Kunz B., Savoglidis G.,
RA Hatzimanikatis V., van der Goot F.G.;
RT "Identification and dynamics of the human ZDHHC16-ZDHHC6 palmitoylation
RT cascade.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: Palmitoyl acyltransferase that mediates palmitoylation of
CC proteins such as PLN and ZDHHC6 (PubMed:28826475). Required during
CC embryonic heart development and cardiac function, possibly by mediating
CC palmitoylation of PLN, thereby affecting PLN phosphorylation and
CC homooligomerization (By similarity). Also required for eye development
CC (By similarity). Palmitoylates ZDHHC6, affecting the quaternary
CC assembly of ZDHHC6, its localization, stability and function
CC (PubMed:28826475). May play a role in DNA damage response (By
CC similarity). May be involved in apoptosis regulation (By similarity).
CC Involved in the proliferation of neural stem cells by regulating the
CC FGF/ERK pathway (By similarity). {ECO:0000250|UniProtKB:B8A4F0,
CC ECO:0000250|UniProtKB:Q9ESG8, ECO:0000269|PubMed:28826475}.
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:28826475};
CC -!- SUBUNIT: Interacts with ABL1 (By similarity). Interacts with COPS5/JAB1
CC (PubMed:17123647). {ECO:0000250|UniProtKB:Q9ESG8,
CC ECO:0000269|PubMed:17123647}.
CC -!- INTERACTION:
CC Q969W1; Q6PL24: TMED8; NbExp=3; IntAct=EBI-11572692, EBI-11603430;
CC Q969W1; O95070: YIF1A; NbExp=3; IntAct=EBI-11572692, EBI-2799703;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:17123647}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9ESG8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q969W1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q969W1-2; Sequence=VSP_008716;
CC Name=3;
CC IsoId=Q969W1-3; Sequence=VSP_016275;
CC Name=4;
CC IsoId=Q969W1-4; Sequence=VSP_016274, VSP_008716;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:17123647}.
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; AF258563; AAG23766.1; -; mRNA.
DR EMBL; AJ294945; CAC82556.1; -; mRNA.
DR EMBL; AY359080; AAQ89439.1; -; mRNA.
DR EMBL; AL355490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49929.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49930.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49931.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49932.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49933.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49934.1; -; Genomic_DNA.
DR EMBL; BC004535; AAH04535.1; -; mRNA.
DR EMBL; BC008074; AAH08074.1; -; mRNA.
DR EMBL; BC011749; AAH11749.1; -; mRNA.
DR EMBL; BC012830; AAH12830.1; -; mRNA.
DR EMBL; BC033157; AAH33157.1; -; mRNA.
DR CCDS; CCDS7460.1; -. [Q969W1-1]
DR CCDS; CCDS7461.1; -. [Q969W1-2]
DR CCDS; CCDS7462.1; -. [Q969W1-3]
DR CCDS; CCDS7463.1; -. [Q969W1-4]
DR RefSeq; NP_001274732.1; NM_001287803.1.
DR RefSeq; NP_001274733.1; NM_001287804.1.
DR RefSeq; NP_115703.2; NM_032327.3. [Q969W1-1]
DR RefSeq; NP_932160.1; NM_198043.2. [Q969W1-2]
DR RefSeq; NP_932161.1; NM_198044.2. [Q969W1-3]
DR RefSeq; NP_932162.1; NM_198045.2. [Q969W1-4]
DR RefSeq; NP_932163.1; NM_198046.2. [Q969W1-1]
DR RefSeq; XP_016872255.1; XM_017016766.1. [Q969W1-2]
DR RefSeq; XP_016872257.1; XM_017016768.1. [Q969W1-3]
DR AlphaFoldDB; Q969W1; -.
DR SMR; Q969W1; -.
DR BioGRID; 124014; 9.
DR IntAct; Q969W1; 3.
DR STRING; 9606.ENSP00000377357; -.
DR GlyGen; Q969W1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q969W1; -.
DR PhosphoSitePlus; Q969W1; -.
DR SwissPalm; Q969W1; -.
DR BioMuta; ZDHHC16; -.
DR DMDM; 37999852; -.
DR MassIVE; Q969W1; -.
DR MaxQB; Q969W1; -.
DR PaxDb; Q969W1; -.
DR PeptideAtlas; Q969W1; -.
DR PRIDE; Q969W1; -.
DR ProteomicsDB; 75856; -. [Q969W1-1]
DR ProteomicsDB; 75857; -. [Q969W1-2]
DR ProteomicsDB; 75858; -. [Q969W1-3]
DR ProteomicsDB; 75859; -. [Q969W1-4]
DR Antibodypedia; 30898; 133 antibodies from 20 providers.
DR DNASU; 84287; -.
DR Ensembl; ENST00000345745.9; ENSP00000304487.8; ENSG00000171307.19. [Q969W1-4]
DR Ensembl; ENST00000352634.8; ENSP00000345383.4; ENSG00000171307.19. [Q969W1-2]
DR Ensembl; ENST00000353979.7; ENSP00000323360.3; ENSG00000171307.19. [Q969W1-3]
DR Ensembl; ENST00000370842.6; ENSP00000359879.1; ENSG00000171307.19. [Q969W1-2]
DR Ensembl; ENST00000370854.7; ENSP00000359891.3; ENSG00000171307.19. [Q969W1-1]
DR Ensembl; ENST00000393760.6; ENSP00000377357.1; ENSG00000171307.19. [Q969W1-1]
DR GeneID; 84287; -.
DR KEGG; hsa:84287; -.
DR MANE-Select; ENST00000393760.6; ENSP00000377357.1; NM_198046.3; NP_932163.1.
DR UCSC; uc001knj.5; human. [Q969W1-1]
DR CTD; 84287; -.
DR DisGeNET; 84287; -.
DR GeneCards; ZDHHC16; -.
DR HGNC; HGNC:20714; ZDHHC16.
DR HPA; ENSG00000171307; Low tissue specificity.
DR MIM; 616750; gene.
DR neXtProt; NX_Q969W1; -.
DR OpenTargets; ENSG00000171307; -.
DR PharmGKB; PA134985701; -.
DR VEuPathDB; HostDB:ENSG00000171307; -.
DR eggNOG; KOG1313; Eukaryota.
DR GeneTree; ENSGT00940000155032; -.
DR HOGENOM; CLU_054274_0_1_1; -.
DR InParanoid; Q969W1; -.
DR OMA; CPVRINQ; -.
DR OrthoDB; 1491968at2759; -.
DR PhylomeDB; Q969W1; -.
DR TreeFam; TF320809; -.
DR BRENDA; 2.3.1.225; 2681.
DR PathwayCommons; Q969W1; -.
DR SignaLink; Q969W1; -.
DR BioGRID-ORCS; 84287; 16 hits in 1081 CRISPR screens.
DR ChiTaRS; ZDHHC16; human.
DR GenomeRNAi; 84287; -.
DR Pharos; Q969W1; Tbio.
DR PRO; PR:Q969W1; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q969W1; protein.
DR Bgee; ENSG00000171307; Expressed in pancreatic ductal cell and 177 other tissues.
DR ExpressionAtlas; Q969W1; baseline and differential.
DR Genevisible; Q969W1; HS.
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; IDA:UniProtKB.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB.
DR GO; GO:0021537; P:telencephalon development; ISS: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 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Apoptosis; DNA damage;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..377
FT /note="Palmitoyltransferase ZDHHC16"
FT /id="PRO_0000212897"
FT TOPO_DOM 1..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..116
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..266
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 155..205
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 185
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q8IUH5"
FT VAR_SEQ 82..146
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016274"
FT VAR_SEQ 176..214
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016275"
FT VAR_SEQ 231..246
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12975309,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_008716"
SQ SEQUENCE 377 AA; 43633 MW; 68AC733DE498A81E CRC64;
MRGQRSLLLG PARLCLRLLL LLGYRRRCPP LLRGLVQRWR YGKVCLRSLL YNSFGGSDTA
VDAAFEPVYW LVDNVIRWFG VVFVVLVIVL TGSIVAIAYL CVLPLILRTY SVPRLCWHFF
YSHWNLILIV FHYYQAITTP PGYPPQGRND IATVSICKKC IYPKPARTHH CSICNRCVLK
MDHHCPWLNN CVGHYNHRYF FSFCFFMTLG CVYCSYGSWD LFREAYAAIE KMKQLDKNKL
QAVANQTYHQ TPPPTFSFRE RMTHKSLVYL WFLCSSVALA LGALTVWHAV LISRGETSIE
RHINKKERRR LQAKGRVFRN PYNYGCLDNW KVFLGVDTGR HWLTRVLLPS SHLPHGNGMS
WEPPPWVTAH SASVMAV
