ZDH16_MOUSE
ID ZDH16_MOUSE Reviewed; 361 AA.
AC Q9ESG8; Q3TI22; Q3UA59; Q91XC5;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Palmitoyltransferase ZDHHC16 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000269|PubMed:26644582};
DE AltName: Full=Abl-philin 2 {ECO:0000303|PubMed:12021275};
DE AltName: Full=Zinc finger DHHC domain-containing protein 16;
DE Short=DHHC-16;
GN Name=Zdhhc16 {ECO:0000312|MGI:MGI:1921418};
GN Synonyms=Aph2 {ECO:0000303|PubMed:12021275};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH ABL1,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RC STRAIN=BALB/cJ;
RX PubMed=12021275; DOI=10.1074/jbc.m202388200;
RA Li B., Cong F., Tan C.P., Wang S.X., Goff S.P.;
RT "Aph2, a protein with a zf-DHHC motif, interacts with c-Abl and has pro-
RT apoptotic activity.";
RL J. Biol. Chem. 277:28870-28876(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26644582; DOI=10.1073/pnas.1518368112;
RA Zhou T., Li J., Zhao P., Liu H., Jia D., Jia H., He L., Cang Y., Boast S.,
RA Chen Y.H., Thibault H., Scherrer-Crosbie M., Goff S.P., Li B.;
RT "Palmitoyl acyltransferase Aph2 in cardiac function and the development of
RT cardiomyopathy.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:15666-15671(2015).
RN [5]
RP FUNCTION.
RX PubMed=27159997; DOI=10.1186/s12867-016-0065-9;
RA Cao N., Li J.K., Rao Y.Q., Liu H., Wu J., Li B., Zhao P., Zeng L., Li J.;
RT "A potential role for protein palmitoylation and zDHHC16 in DNA damage
RT response.";
RL BMC Mol. Biol. 17:12-12(2016).
CC -!- FUNCTION: Palmitoyl acyltransferase that mediates palmitoylation of
CC proteins such as PLN and ZDHHC6 (PubMed:26644582). Required during
CC embryonic heart development and cardiac function, possibly by mediating
CC palmitoylation of PLN, thereby affecting PLN phosphorylation and
CC homooligomerization (PubMed:26644582). Also required for eye
CC development (PubMed:26644582). Palmitoylates ZDHHC6, affecting the
CC quaternary assembly of ZDHHC6, its localization, stability and function
CC (By similarity). May play a role in DNA damage response
CC (PubMed:27159997). May be involved in apoptosis regulation
CC (PubMed:12021275). Involved in the proliferation of neural stem cells
CC by regulating the FGF/ERK pathway (By similarity).
CC {ECO:0000250|UniProtKB:B8A4F0, ECO:0000250|UniProtKB:Q969W1,
CC ECO:0000269|PubMed:12021275, ECO:0000269|PubMed:26644582,
CC ECO:0000269|PubMed:27159997}.
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:26644582};
CC -!- SUBUNIT: Interacts with ABL1 (PubMed:12021275). Interacts with COPS5
CC (By similarity). {ECO:0000250|UniProtKB:Q969W1,
CC ECO:0000269|PubMed:12021275}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12021275}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:12021275}.
CC -!- DISRUPTION PHENOTYPE: Lethality one day after birth (PubMed:26644582).
CC Pups and embryos show eye malformation and heart defects
CC (PubMed:26644582). Mice display cardiomyopathy and cardiac defects
CC including bradycardia (PubMed:26644582). Heart defects are
CC characterized by thinner and enlarged ventricular walls, cardiomyocyte
CC disarray and abnormal nucleus morphology (PubMed:26644582).
CC {ECO:0000269|PubMed:26644582}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF176814; AAG09269.1; -; mRNA.
DR EMBL; AK151505; BAE30456.1; -; mRNA.
DR EMBL; AK168042; BAE40024.1; -; mRNA.
DR EMBL; BC010835; AAH10835.1; -; mRNA.
DR CCDS; CCDS29817.1; -.
DR RefSeq; NP_076229.2; NM_023740.2.
DR AlphaFoldDB; Q9ESG8; -.
DR SMR; Q9ESG8; -.
DR BioGRID; 216543; 1.
DR IntAct; Q9ESG8; 1.
DR STRING; 10090.ENSMUSP00000026154; -.
DR PhosphoSitePlus; Q9ESG8; -.
DR SwissPalm; Q9ESG8; -.
DR PaxDb; Q9ESG8; -.
DR PRIDE; Q9ESG8; -.
DR ProteomicsDB; 275137; -.
DR Antibodypedia; 30898; 133 antibodies from 20 providers.
DR Ensembl; ENSMUST00000026154; ENSMUSP00000026154; ENSMUSG00000025157.
DR GeneID; 74168; -.
DR KEGG; mmu:74168; -.
DR UCSC; uc008hmq.2; mouse.
DR CTD; 84287; -.
DR MGI; MGI:1921418; Zdhhc16.
DR VEuPathDB; HostDB:ENSMUSG00000025157; -.
DR eggNOG; KOG1313; Eukaryota.
DR GeneTree; ENSGT00940000155032; -.
DR HOGENOM; CLU_054274_0_0_1; -.
DR InParanoid; Q9ESG8; -.
DR OMA; CPVRINQ; -.
DR OrthoDB; 1491968at2759; -.
DR PhylomeDB; Q9ESG8; -.
DR TreeFam; TF320809; -.
DR BioGRID-ORCS; 74168; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Zdhhc16; mouse.
DR PRO; PR:Q9ESG8; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9ESG8; protein.
DR Bgee; ENSMUSG00000025157; Expressed in embryonic brain and 266 other tissues.
DR ExpressionAtlas; Q9ESG8; baseline and differential.
DR Genevisible; Q9ESG8; MM.
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; IMP:UniProtKB.
DR GO; GO:0001654; P:eye development; IMP:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP: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; Apoptosis; DNA damage; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..361
FT /note="Palmitoyltransferase ZDHHC16"
FT /id="PRO_0000212899"
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..250
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..361
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 CONFLICT 33
FT /note="R -> Q (in Ref. 2; BAE40024)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="A -> S (in Ref. 1; AAG09269)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="C -> R (in Ref. 3; AAH10835)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="S -> N (in Ref. 1; AAG09269)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 41794 MW; B9A4D4B4C4170FE9 CRC64;
MRGQRSLLLG PARLCLRLLL LLGYRRRCPP LLRGLVQRWR YGKVCLRSLL YNSFGGSDTA
VDAAFEPVYW LVDNVIRWFG VVFVVLVIVL TGSIVAIAYL CVLPLILRTY SVPRLCWHFF
YSHWNLILIV FHYYQAITTP PGYPPQGRND IATVSICKKC IYPKPARTHH CSICNRCVLK
MDHHCPWLNN CVGHYNHRYF FSFCFFMTLG CVYCSYGSWD LFREAYAAIE TYHQTPPPTF
SFRERITHKS LVYLWFLCSS VALALGALTM WHAVLISRGE TSIERHINKK ERRRLQAKGR
VFRNPYNYGC LDNWKVFLGV DTGRHWLTRV LLPSSHLPHG NGMSWDPPPW VTAHSASVMA
V
