ZDHC9_MOUSE
ID ZDHC9_MOUSE Reviewed; 364 AA.
AC P59268; Q5BL19;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Palmitoyltransferase ZDHHC9;
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q9Y397};
DE AltName: Full=Zinc finger DHHC domain-containing protein 9;
DE Short=DHHC-9;
DE Short=DHHC9;
GN Name=Zdhhc9;
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 STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary gland;
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).
CC -!- FUNCTION: Palmitoyltransferase that could catalyze the addition of
CC palmitate onto various protein substrates. The ZDHHC9-GOLGA7 complex is
CC a palmitoyltransferase specific for HRAS and NRAS. May have a
CC palmitoyltransferase activity toward the beta-2 adrenergic
CC receptor/ADRB2 and therefore regulate G protein-coupled receptor
CC signaling. {ECO:0000250|UniProtKB:Q9Y397}.
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:Q9Y397};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q9Y397};
CC -!- SUBUNIT: Interacts with GOLGA7. {ECO:0000250|UniProtKB:Q9Y397}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Y397}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Y397};
CC Multi-pass membrane protein {ECO:0000255}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK032233; BAC27774.1; -; mRNA.
DR EMBL; BC042618; AAH42618.1; -; mRNA.
DR EMBL; BC090832; AAH90832.1; -; mRNA.
DR CCDS; CCDS40960.1; -.
DR RefSeq; NP_766053.1; NM_172465.4.
DR RefSeq; XP_006541517.1; XM_006541454.3.
DR AlphaFoldDB; P59268; -.
DR SMR; P59268; -.
DR STRING; 10090.ENSMUSP00000044734; -.
DR iPTMnet; P59268; -.
DR PhosphoSitePlus; P59268; -.
DR SwissPalm; P59268; -.
DR MaxQB; P59268; -.
DR PaxDb; P59268; -.
DR PRIDE; P59268; -.
DR ProteomicsDB; 275347; -.
DR Antibodypedia; 30107; 212 antibodies from 32 providers.
DR DNASU; 208884; -.
DR Ensembl; ENSMUST00000037960; ENSMUSP00000044734; ENSMUSG00000036985.
DR Ensembl; ENSMUST00000088935; ENSMUSP00000086325; ENSMUSG00000036985.
DR GeneID; 208884; -.
DR KEGG; mmu:208884; -.
DR UCSC; uc009tbx.2; mouse.
DR CTD; 51114; -.
DR MGI; MGI:2444393; Zdhhc9.
DR VEuPathDB; HostDB:ENSMUSG00000036985; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000159999; -.
DR HOGENOM; CLU_018741_3_1_1; -.
DR InParanoid; P59268; -.
DR OMA; PLVYQRW; -.
DR OrthoDB; 1264614at2759; -.
DR PhylomeDB; P59268; -.
DR TreeFam; TF312923; -.
DR Reactome; R-MMU-9648002; RAS processing.
DR BioGRID-ORCS; 208884; 2 hits in 77 CRISPR screens.
DR PRO; PR:P59268; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P59268; protein.
DR Bgee; ENSMUSG00000036985; Expressed in esophagus and 240 other tissues.
DR Genevisible; P59268; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:CAFA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031228; C:intrinsic component of Golgi membrane; ISS:CAFA.
DR GO; GO:0002178; C:palmitoyltransferase complex; ISS:CAFA.
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:0043849; F:Ras palmitoyltransferase activity; ISS:CAFA.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:CAFA.
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 InterPro; IPR030292; ZDHHC9.
DR PANTHER; PTHR22883:SF71; PTHR22883:SF71; 1.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Endoplasmic reticulum; Golgi apparatus; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..364
FT /note="Palmitoyltransferase ZDHHC9"
FT /id="PRO_0000212881"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..63
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..228
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 139..189
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 303..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 169
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y397"
SQ SEQUENCE 364 AA; 40940 MW; D035759B8844B67A CRC64;
MSVMVVRKKV TRKWEKLPGR NTFCCDGRVM MARQKGIFYL TLFLILGTCT LFFAFECRYL
AVQLSPAIPV FAAMLFLFSM ATLLRTSFSD PGVIPRALPD EAAFIEMEIE ATNGAVPQGQ
RPPPRIKNFQ INNQIVKLKY CYTCKIFRPP RASHCSICDN CVERFDHHCP WVGNCVGKRN
YRYFYLFILS LSLLTIYVFA FNIVYVALKS LKIGFLETLK ETPGTVLEVL ICFFTLWSVV
GLTGFHTFLV ALNQTTNEDI KGSWTGKNRV QNPYSHGNIV KNCCEVLCGP LPPSVLDRRG
ILPLEESGSR PPSTQETSSS LLPQSPASTE HMNSNEMAED TSIPEEMPPP EPPEPPQEAS
EAEK
