ZDH12_MOUSE
ID ZDH12_MOUSE Reviewed; 267 AA.
AC Q8VC90; Q9CZ24; Q9D0T6;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Palmitoyltransferase ZDHHC12 {ECO:0000305|PubMed:25025157};
DE EC=2.3.1.225 {ECO:0000305|PubMed:25025157};
DE AltName: Full=DHHC domain-containing cysteine-rich protein 12 {ECO:0000250|UniProtKB:Q96GR4};
DE Short=DHHC-12 {ECO:0000250|UniProtKB:Q96GR4};
DE AltName: Full=Zinc finger DHHC domain-containing protein 12 {ECO:0000312|MGI:MGI:1913470};
GN Name=Zdhhc12 {ECO:0000312|MGI:MGI:1913470};
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Ovary;
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] (ISOFORM 1).
RC TISSUE=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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-127,
RP AND ACTIVE SITE.
RX PubMed=25025157; DOI=10.1371/journal.pbio.1001908;
RA Dejanovic B., Semtner M., Ebert S., Lamkemeyer T., Neuser F., Luescher B.,
RA Meier J.C., Schwarz G.;
RT "Palmitoylation of gephyrin controls receptor clustering and plasticity of
RT GABAergic synapses.";
RL PLoS Biol. 12:e1001908-e1001908(2014).
CC -!- FUNCTION: Palmitoyltransferase that could catalyze the addition of
CC palmitate onto various protein substrates (PubMed:25025157). Has a
CC palmitoyltransferase activity toward gephyrin/GPHN, regulating its
CC clustering at synapses and its function in gamma-aminobutyric acid
CC receptor clustering (PubMed:25025157). Thereby, indirectly regulates
CC GABAergic synaptic transmission (PubMed:25025157).
CC {ECO:0000269|PubMed:25025157}.
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:0000305|PubMed:25025157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000305|PubMed:25025157};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:25025157}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96GR4}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VC90-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VC90-2; Sequence=VSP_006946;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK013074; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK087676; BAC39965.1; -; mRNA.
DR EMBL; AK013074; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC021432; AAH21432.1; -; mRNA.
DR CCDS; CCDS15868.1; -. [Q8VC90-1]
DR CCDS; CCDS15869.1; -. [Q8VC90-2]
DR RefSeq; NP_001032851.1; NM_001037762.1. [Q8VC90-1]
DR RefSeq; NP_079704.2; NM_025428.2. [Q8VC90-2]
DR AlphaFoldDB; Q8VC90; -.
DR SMR; Q8VC90; -.
DR STRING; 10090.ENSMUSP00000080521; -.
DR PhosphoSitePlus; Q8VC90; -.
DR SwissPalm; Q8VC90; -.
DR EPD; Q8VC90; -.
DR PeptideAtlas; Q8VC90; -.
DR PRIDE; Q8VC90; -.
DR ProteomicsDB; 298511; -. [Q8VC90-1]
DR ProteomicsDB; 298512; -. [Q8VC90-2]
DR Antibodypedia; 67200; 70 antibodies from 14 providers.
DR DNASU; 66220; -.
DR Ensembl; ENSMUST00000081838; ENSMUSP00000080521; ENSMUSG00000015335. [Q8VC90-2]
DR Ensembl; ENSMUST00000102865; ENSMUSP00000099929; ENSMUSG00000015335. [Q8VC90-1]
DR GeneID; 66220; -.
DR KEGG; mmu:66220; -.
DR UCSC; uc008jbd.1; mouse. [Q8VC90-2]
DR UCSC; uc008jbe.1; mouse. [Q8VC90-1]
DR CTD; 84885; -.
DR MGI; MGI:1913470; Zdhhc12.
DR VEuPathDB; HostDB:ENSMUSG00000015335; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000156902; -.
DR HOGENOM; CLU_031257_2_0_1; -.
DR InParanoid; Q8VC90; -.
DR OMA; RRCRYCM; -.
DR OrthoDB; 1440636at2759; -.
DR PhylomeDB; Q8VC90; -.
DR TreeFam; TF329809; -.
DR BioGRID-ORCS; 66220; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q8VC90; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8VC90; protein.
DR Bgee; ENSMUSG00000015335; Expressed in yolk sac and 196 other tissues.
DR Genevisible; Q8VC90; 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; IDA:UniProtKB.
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; IMP:UniProtKB.
DR GO; GO:0097116; P:gephyrin clustering involved in postsynaptic density assembly; IMP:UniProtKB.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IMP:UniProtKB.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IMP: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; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..267
FT /note="Palmitoyltransferase ZDHHC12"
FT /id="PRO_0000212885"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..43
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..178
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 97..147
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 127
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000305|PubMed:25025157"
FT VAR_SEQ 34
FT /note="E -> GEPDTAPPRAHPITQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_006946"
FT MUTAGEN 127
FT /note="C->S: Loss of protein-cysteine S-
FT palmitoyltransferase activity."
FT /evidence="ECO:0000305|PubMed:25025157"
FT CONFLICT 20
FT /note="L -> P (in Ref. 1; AK013074)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="L -> F (in Ref. 1; BAC39965)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 30708 MW; BFBE43C83061FA44 CRC64;
MALWPPLNSG MLVRTGHTVL TWGITLVLFL HDTELRQWEE QGELLLPLTF LLLVLSSLLL
YLAVSLMDPG YVTTQPQPQG EPKEEQAAMV PQAVPLRRCR HCLVLQPLRA RHCRDCRRCV
RRYDHHCPWM ENCVGERNHP LFVAYLALQL VVLLWGLCLA WSGLQFFQPW GLWLRSTGLL
FTTFLLLSFF ALVVALLLAS HLYLVARNTT TWEFISSHRI AYLRQRTSNP FDRGPTRNLA
HFFCGWPSGP WETLSAEEEE EGSSQVV
