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Palmitoyltransferase ZDHHC16 (EC 2.3.1.225) (Abl-philin 2) (Zinc finger DHHC domain-containing protein 16) (DHHC-16)

 ZDH16_MOUSE             Reviewed;         361 AA.
Q9ESG8; Q3TI22; Q3UA59; Q91XC5;
24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
22-NOV-2005, sequence version 2.
23-MAY-2018, entry version 122.
RecName: Full=Palmitoyltransferase ZDHHC16 {ECO:0000305};
EC=2.3.1.225 {ECO:0000269|PubMed:26644582};
AltName: Full=Abl-philin 2 {ECO:0000303|PubMed:12021275};
AltName: Full=Zinc finger DHHC domain-containing protein 16;
Short=DHHC-16;
Name=Zdhhc16 {ECO:0000312|MGI:MGI:1921418};
Synonyms=Aph2 {ECO:0000303|PubMed:12021275};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH ABL1,
SUBCELLULAR LOCATION, AND FUNCTION.
STRAIN=BALB/cJ;
PubMed=12021275; DOI=10.1074/jbc.M202388200;
Li B., Cong F., Tan C.P., Wang S.X., Goff S.P.;
"Aph2, a protein with a zf-DHHC motif, interacts with c-Abl and has
pro-apoptotic activity.";
J. Biol. Chem. 277:28870-28876(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and DBA/2J; TISSUE=Bone marrow;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=26644582; DOI=10.1073/pnas.1518368112;
Zhou T., Li J., Zhao P., Liu H., Jia D., Jia H., He L., Cang Y.,
Boast S., Chen Y.H., Thibault H., Scherrer-Crosbie M., Goff S.P.,
Li B.;
"Palmitoyl acyltransferase Aph2 in cardiac function and the
development of cardiomyopathy.";
Proc. Natl. Acad. Sci. U.S.A. 112:15666-15671(2015).
[5]
FUNCTION.
PubMed=27159997; DOI=10.1186/s12867-016-0065-9;
Cao N., Li J.K., Rao Y.Q., Liu H., Wu J., Li B., Zhao P., Zeng L.,
Li J.;
"A potential role for protein palmitoylation and zDHHC16 in DNA damage
response.";
BMC Mol. Biol. 17:12-12(2016).
-!- FUNCTION: Palmitoyl acyltransferase that mediates palmitoylation
of proteins such as PLN and ZDHHC6 (PubMed:26644582). Required
during embryonic heart development and cardiac function, possibly
by mediating palmitoylation of PLN, thereby affecting PLN
phosphorylation and homooligomerization (PubMed:26644582). Also
required for eye development (PubMed:26644582). Palmitoylates
ZDHHC6, affecting the quaternary assembly of ZDHHC6, its
localization, stability and function (By similarity). May play a
role in DNA damage response (PubMed:27159997). May be involved in
apoptosis regulation (PubMed:12021275). Involved in the
proliferation of neural stem cells by regulating the FGF/ERK
pathway (By similarity). {ECO:0000250|UniProtKB:B8A4F0,
ECO:0000250|UniProtKB:Q969W1, ECO:0000269|PubMed:12021275,
ECO:0000269|PubMed:26644582, ECO:0000269|PubMed:27159997}.
-!- CATALYTIC ACTIVITY: Palmitoyl-CoA + [protein]-L-cysteine =
[protein]-S-palmitoyl-L-cysteine + CoA.
{ECO:0000269|PubMed:26644582}.
-!- SUBUNIT: Interacts with ABL1 (PubMed:12021275). Interacts with
COPS5 (By similarity). {ECO:0000250|UniProtKB:Q969W1,
ECO:0000269|PubMed:12021275}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:12021275}; Multi-pass membrane protein
{ECO:0000255}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:12021275}.
-!- DISRUPTION PHENOTYPE: Lethality one day after birth
(PubMed:26644582). Pups and embryos show eye malformation and
heart defects (PubMed:26644582). Mice display cardiomyopathy and
cardiac defects including bradycardia (PubMed:26644582). Heart
defects are characterized by thinner and enlarged ventricular
walls, cardiomyocyte disarray and abnormal nucleus morphology
(PubMed:26644582). {ECO:0000269|PubMed:26644582}.
-!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF176814; AAG09269.1; -; mRNA.
EMBL; AK151505; BAE30456.1; -; mRNA.
EMBL; AK168042; BAE40024.1; -; mRNA.
EMBL; BC010835; AAH10835.1; -; mRNA.
CCDS; CCDS29817.1; -.
RefSeq; NP_076229.2; NM_023740.2.
UniGene; Mm.20387; -.
BioGrid; 216543; 1.
STRING; 10090.ENSMUSP00000026154; -.
PhosphoSitePlus; Q9ESG8; -.
SwissPalm; Q9ESG8; -.
PaxDb; Q9ESG8; -.
PRIDE; Q9ESG8; -.
Ensembl; ENSMUST00000026154; ENSMUSP00000026154; ENSMUSG00000025157.
GeneID; 74168; -.
KEGG; mmu:74168; -.
UCSC; uc008hmq.2; mouse.
CTD; 84287; -.
MGI; MGI:1921418; Zdhhc16.
eggNOG; KOG1313; Eukaryota.
eggNOG; COG5273; LUCA.
GeneTree; ENSGT00900000140969; -.
HOGENOM; HOG000234766; -.
HOVERGEN; HBG054667; -.
InParanoid; Q9ESG8; -.
KO; K18932; -.
OMA; KNWKLFL; -.
OrthoDB; EOG091G0FLT; -.
PhylomeDB; Q9ESG8; -.
TreeFam; TF320809; -.
PRO; PR:Q9ESG8; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000025157; -.
CleanEx; MM_ZDHHC16; -.
Genevisible; Q9ESG8; MM.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016409; F:palmitoyltransferase activity; IDA:UniProtKB.
GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0001654; P:eye development; IMP:UniProtKB.
GO; GO:0007507; P:heart development; IMP:UniProtKB.
GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB.
GO; GO:0021537; P:telencephalon development; ISS:UniProtKB.
InterPro; IPR001594; Palmitoyltrfase_DHHC.
Pfam; PF01529; DHHC; 1.
PROSITE; PS50216; DHHC; 1.
1: Evidence at protein level;
Acyltransferase; Apoptosis; Complete proteome; DNA damage;
Endoplasmic reticulum; Membrane; Reference proteome; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 361 Palmitoyltransferase ZDHHC16.
/FTId=PRO_0000212899.
TOPO_DOM 1 77 Cytoplasmic. {ECO:0000255}.
TRANSMEM 78 98 Helical. {ECO:0000255}.
TOPO_DOM 99 116 Lumenal. {ECO:0000255}.
TRANSMEM 117 137 Helical. {ECO:0000255}.
TOPO_DOM 138 198 Cytoplasmic. {ECO:0000255}.
TRANSMEM 199 219 Helical. {ECO:0000255}.
TOPO_DOM 220 250 Lumenal. {ECO:0000255}.
TRANSMEM 251 271 Helical. {ECO:0000255}.
TOPO_DOM 272 361 Cytoplasmic. {ECO:0000255}.
DOMAIN 155 205 DHHC. {ECO:0000255|PROSITE-
ProRule:PRU00067}.
ACT_SITE 185 185 S-palmitoyl cysteine intermediate.
{ECO:0000250|UniProtKB:Q8IUH5}.
CONFLICT 33 33 R -> Q (in Ref. 2; BAE40024).
{ECO:0000305}.
CONFLICT 63 63 A -> S (in Ref. 1; AAG09269).
{ECO:0000305}.
CONFLICT 171 171 C -> R (in Ref. 3; AAH10835).
{ECO:0000305}.
CONFLICT 335 335 S -> N (in Ref. 1; AAG09269).
{ECO:0000305}.
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


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