ZDH19_MOUSE
ID ZDH19_MOUSE Reviewed; 347 AA.
AC Q810M5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Palmitoyltransferase ZDHHC19;
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q8WVZ1};
DE AltName: Full=Zinc finger DHHC domain-containing protein 19;
DE Short=DHHC-19;
GN Name=Zdhhc19; Synonyms=Gm616;
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].
RC TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 PROTEIN SEQUENCE OF 222-229, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
CC -!- FUNCTION: Palmitoyltransferase that mediates palmitoylation of RRAS,
CC leading to increased cell viability. {ECO:0000250|UniProtKB:Q8WVZ1}.
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:Q8WVZ1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q8WVZ1};
CC -!- INTERACTION:
CC Q810M5; P62993: GRB2; Xeno; NbExp=2; IntAct=EBI-22225085, EBI-401755;
CC Q810M5; P40763: STAT3; Xeno; NbExp=4; IntAct=EBI-22225085, EBI-518675;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8WVZ1}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q8WVZ1}.
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; BC049761; AAH49761.1; -; mRNA.
DR EMBL; AK133398; BAE21632.1; -; mRNA.
DR EMBL; AK132780; BAE21356.1; -; mRNA.
DR CCDS; CCDS28122.1; -.
DR RefSeq; NP_955013.1; NM_199309.2.
DR AlphaFoldDB; Q810M5; -.
DR SMR; Q810M5; -.
DR IntAct; Q810M5; 2.
DR STRING; 10090.ENSMUSP00000070727; -.
DR iPTMnet; Q810M5; -.
DR PhosphoSitePlus; Q810M5; -.
DR EPD; Q810M5; -.
DR PaxDb; Q810M5; -.
DR PRIDE; Q810M5; -.
DR ProteomicsDB; 302051; -.
DR Antibodypedia; 33933; 60 antibodies from 12 providers.
DR DNASU; 245308; -.
DR Ensembl; ENSMUST00000064192; ENSMUSP00000070727; ENSMUSG00000052363.
DR GeneID; 245308; -.
DR KEGG; mmu:245308; -.
DR UCSC; uc007yyy.1; mouse.
DR CTD; 131540; -.
DR MGI; MGI:2682948; Zdhhc19.
DR VEuPathDB; HostDB:ENSMUSG00000052363; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000161784; -.
DR HOGENOM; CLU_018741_4_0_1; -.
DR InParanoid; Q810M5; -.
DR OMA; NLHPPMS; -.
DR OrthoDB; 1264614at2759; -.
DR PhylomeDB; Q810M5; -.
DR TreeFam; TF354263; -.
DR BioGRID-ORCS; 245308; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Zdhhc19; mouse.
DR PRO; PR:Q810M5; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q810M5; protein.
DR Bgee; ENSMUSG00000052363; Expressed in seminiferous tubule of testis and 18 other tissues.
DR ExpressionAtlas; Q810M5; baseline and differential.
DR Genevisible; Q810M5; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097356; C:perinucleolar compartment; ISO:MGI.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; ISO:MGI.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:UniProtKB.
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; Cytoplasm; Direct protein sequencing; Golgi apparatus;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..347
FT /note="Palmitoyltransferase ZDHHC19"
FT /evidence="ECO:0000250|UniProtKB:Q8WVZ1"
FT /id="PRO_0000448574"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 112..162
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 275..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..304
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q8WVZ1,
FT ECO:0000255|PROSITE-ProRule:PRU00067"
SQ SEQUENCE 347 AA; 39009 MW; 35FB30F5DA6E608E CRC64;
MPFLKDAVTL VKEPQQLPSI PLSWFPSSVF AAFNVTLLLF LSGLFFGFPC RWLVQNGEWA
FPAITGPLFI LTFFSLVSLN FSDPGILHRG STKEDPMTVH VVRVNQRAFR LEWCPKCLFH
RPPRTYHCPW CNICVEDFDH HCKWVNNCIG HRNFRLFMLL VLSLCLYSGA LLVTCLTFLF
RTRHLPFSLD KGMAILVAVP AAGFLIPLFL LLLIQALSVS RAESSYESKC RYHPEYNPFD
QGFAKNWYLA MFAPLGPNYM SEVVCLQRPV GTAWIQEKTK PSPPRRPKHC RPGPPGPQHQ
PRRVPGKGPP GSGEAAALQE MRRLPASVEK SPGGPRQPTA EPAAGDP
