ZDH14_MOUSE
ID ZDH14_MOUSE Reviewed; 489 AA.
AC Q8BQQ1; Q8BNR2; Q8CFN0;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Palmitoyltransferase ZDHHC14 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q8IZN3};
DE AltName: Full=DHHC domain-containing cysteine-rich protein 14 {ECO:0000250|UniProtKB:Q8IZN3};
DE Short=DHHC-14 {ECO:0000250|UniProtKB:Q8IZN3};
DE AltName: Full=NEW1 domain-containing protein {ECO:0000303|Ref.1};
DE Short=NEW1CP {ECO:0000303|Ref.1};
DE AltName: Full=Zinc finger DHHC domain-containing protein 14 {ECO:0000312|MGI:MGI:2653229};
GN Name=Zdhhc14 {ECO:0000312|MGI:MGI:2653229};
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=BALB/cJ; TISSUE=Adipose tissue;
RA Guo J.H., Chen L., Yu L.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, and Corpora quadrigemina;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Palmitoyltransferase that could catalyze the addition of
CC palmitate onto various protein substrates. May have a
CC palmitoyltransferase activity toward the beta-2 adrenergic
CC receptor/ADRB2 and thereby regulate G protein-coupled receptor
CC signaling. May play a role in cell differentiation and apoptosis.
CC {ECO:0000250|UniProtKB:Q8IZN3}.
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:Q8IZN3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q8IZN3};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8IZN3}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8IZN3};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BQQ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BQQ1-2; Sequence=VSP_016272;
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC ERF2/ZDHHC9 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC38040.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF542387; AAN47141.1; -; mRNA.
DR EMBL; AK046719; BAC32845.1; -; mRNA.
DR EMBL; AK080845; BAC38040.1; ALT_FRAME; mRNA.
DR EMBL; BC059814; AAH59814.1; -; mRNA.
DR CCDS; CCDS37422.1; -. [Q8BQQ1-1]
DR RefSeq; NP_666185.3; NM_146073.3. [Q8BQQ1-1]
DR AlphaFoldDB; Q8BQQ1; -.
DR SMR; Q8BQQ1; -.
DR STRING; 10090.ENSMUSP00000086589; -.
DR iPTMnet; Q8BQQ1; -.
DR PhosphoSitePlus; Q8BQQ1; -.
DR jPOST; Q8BQQ1; -.
DR MaxQB; Q8BQQ1; -.
DR PaxDb; Q8BQQ1; -.
DR PeptideAtlas; Q8BQQ1; -.
DR PRIDE; Q8BQQ1; -.
DR ProteomicsDB; 275134; -. [Q8BQQ1-1]
DR ProteomicsDB; 275135; -. [Q8BQQ1-2]
DR Antibodypedia; 33428; 61 antibodies from 19 providers.
DR DNASU; 224454; -.
DR Ensembl; ENSMUST00000089185; ENSMUSP00000086589; ENSMUSG00000034265. [Q8BQQ1-1]
DR GeneID; 224454; -.
DR KEGG; mmu:224454; -.
DR UCSC; uc008aff.1; mouse. [Q8BQQ1-1]
DR CTD; 79683; -.
DR MGI; MGI:2653229; Zdhhc14.
DR VEuPathDB; HostDB:ENSMUSG00000034265; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000156483; -.
DR HOGENOM; CLU_018741_0_0_1; -.
DR InParanoid; Q8BQQ1; -.
DR OMA; SVPKRKW; -.
DR OrthoDB; 1264614at2759; -.
DR PhylomeDB; Q8BQQ1; -.
DR TreeFam; TF312923; -.
DR BioGRID-ORCS; 224454; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Zdhhc14; mouse.
DR PRO; PR:Q8BQQ1; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8BQQ1; protein.
DR Bgee; ENSMUSG00000034265; Expressed in motor neuron and 242 other tissues.
DR Genevisible; Q8BQQ1; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016409; F:palmitoyltransferase activity; ISO:MGI.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; ISO:MGI.
DR GO; GO:0006612; P:protein targeting to membrane; 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 Acyltransferase; Alternative splicing; Endoplasmic reticulum;
KW Golgi apparatus; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..489
FT /note="Palmitoyltransferase ZDHHC14"
FT /id="PRO_0000212892"
FT TOPO_DOM 1..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..89
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..255
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 165..215
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 434..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 195
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..105
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_016272"
FT CONFLICT 274
FT /note="Y -> C (in Ref. 1; AAN47141)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 53659 MW; EFF96E948FA45A03 CRC64;
MPPGGGGPMK DCEYSQISTH SSSPMESPHK KKKIAARRKW EVFPGRNKFF CNGRIMMARQ
TGVFYLTLIL ILVTSGLFFA FDCRYLAEKI TPAIPVVGGI LFFFVMGTLL RTSFSDPGVL
PRATPDEAAD LERQIDIANG TSSGGYRPPP RTKEVVINGQ TVKLKYCFTC KIFRPPRASH
CSLCDNCVEQ FDHHCPWVGN CVGKRNYRFF YMFILSLSFL TVFIFAFVIT HVIHRSQQKG
FLDALKDSPA SVLEAVICFF SVWSIIGLSG FHTYLISSNQ TTNEDIKGSW SNKRGKENYN
PYSYGNIFTN CCVALCGPIS PSLIDRRGYV QPDTPQPAAP SNGITMYGAT QSQSDMCDQD
QCIQSTKFVL QAAATPLLQS EPSLTSEELH MPGKPGLGTP CASLTLGQPT PPSSMPNLAT
EATLSDIMPL KDEHGGHQFL TPDEAPSPPR MLGAGSPLAH SRTMHMLGLA SQDSLHEDSV
RGLVKLSSV
