ZDH12_HUMAN
ID ZDH12_HUMAN Reviewed; 267 AA.
AC Q96GR4; A6NH95; B2RE03; Q5T265; Q5T267; Q5T268; Q86VT5; Q96T09;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Palmitoyltransferase ZDHHC12 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q8VC90};
DE AltName: Full=DHHC domain-containing cysteine-rich protein 12 {ECO:0000303|PubMed:16647879};
DE Short=DHHC-12 {ECO:0000303|PubMed:16647879};
DE AltName: Full=Zinc finger DHHC domain-containing protein 12 {ECO:0000312|HGNC:HGNC:19159};
DE AltName: Full=Zinc finger protein 400;
GN Name=ZDHHC12 {ECO:0000312|HGNC:HGNC:19159}; Synonyms=ZNF400;
GN ORFNames=PSEC0008 {ECO:0000312|EMBL:BAC11553.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP LEU-172.
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT LEU-172.
RC TISSUE=Teratocarcinoma;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-172.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP LEU-172.
RC TISSUE=Mammary gland, and Uterus;
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 [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16647879; DOI=10.1016/j.bbalip.2006.03.010;
RA Ohno Y., Kihara A., Sano T., Igarashi Y.;
RT "Intracellular localization and tissue-specific distribution of human and
RT yeast DHHC cysteine-rich domain-containing proteins.";
RL Biochim. Biophys. Acta 1761:474-483(2006).
CC -!- FUNCTION: Palmitoyltransferase that could catalyze the addition of
CC palmitate onto various protein substrates. Has a palmitoyltransferase
CC activity toward gephyrin/GPHN, regulating its clustering at synapses
CC and its function in gamma-aminobutyric acid receptor clustering.
CC Thereby, indirectly regulates GABAergic synaptic transmission.
CC {ECO:0000250|UniProtKB:Q8VC90}.
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:Q8VC90};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q8VC90};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8VC90}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16647879}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96GR4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96GR4-2; Sequence=VSP_006945;
CC Name=3;
CC IsoId=Q96GR4-3; Sequence=VSP_016271;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16647879}.
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; AK027430; BAB55104.1; -; mRNA.
DR EMBL; AK075332; BAC11553.1; -; mRNA.
DR EMBL; AK315746; BAG38100.1; -; mRNA.
DR EMBL; AL441992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87826.1; -; Genomic_DNA.
DR EMBL; BC009280; AAH09280.1; -; mRNA.
DR EMBL; BC048251; AAH48251.1; -; mRNA.
DR CCDS; CCDS6909.1; -. [Q96GR4-1]
DR RefSeq; NP_001304944.1; NM_001318015.1. [Q96GR4-3]
DR RefSeq; NP_001304945.1; NM_001318016.1.
DR RefSeq; NP_001304949.1; NM_001318020.1.
DR RefSeq; NP_001304952.1; NM_001318023.1.
DR RefSeq; NP_116188.2; NM_032799.4. [Q96GR4-1]
DR AlphaFoldDB; Q96GR4; -.
DR SMR; Q96GR4; -.
DR BioGRID; 124326; 128.
DR IntAct; Q96GR4; 3.
DR MINT; Q96GR4; -.
DR STRING; 9606.ENSP00000361748; -.
DR iPTMnet; Q96GR4; -.
DR PhosphoSitePlus; Q96GR4; -.
DR SwissPalm; Q96GR4; -.
DR BioMuta; ZDHHC12; -.
DR DMDM; 126302619; -.
DR EPD; Q96GR4; -.
DR jPOST; Q96GR4; -.
DR MassIVE; Q96GR4; -.
DR PaxDb; Q96GR4; -.
DR PeptideAtlas; Q96GR4; -.
DR PRIDE; Q96GR4; -.
DR ProteomicsDB; 76657; -. [Q96GR4-1]
DR ProteomicsDB; 76658; -. [Q96GR4-2]
DR ProteomicsDB; 76659; -. [Q96GR4-3]
DR Antibodypedia; 67200; 70 antibodies from 14 providers.
DR DNASU; 84885; -.
DR Ensembl; ENST00000372663.9; ENSP00000361748.4; ENSG00000160446.19. [Q96GR4-1]
DR GeneID; 84885; -.
DR KEGG; hsa:84885; -.
DR MANE-Select; ENST00000372663.9; ENSP00000361748.4; NM_032799.5; NP_116188.3.
DR UCSC; uc004bvy.4; human. [Q96GR4-1]
DR CTD; 84885; -.
DR DisGeNET; 84885; -.
DR GeneCards; ZDHHC12; -.
DR HGNC; HGNC:19159; ZDHHC12.
DR HPA; ENSG00000160446; Low tissue specificity.
DR neXtProt; NX_Q96GR4; -.
DR OpenTargets; ENSG00000160446; -.
DR PharmGKB; PA38802; -.
DR VEuPathDB; HostDB:ENSG00000160446; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000156902; -.
DR HOGENOM; CLU_031257_2_0_1; -.
DR InParanoid; Q96GR4; -.
DR OMA; RRCRYCM; -.
DR OrthoDB; 1440636at2759; -.
DR PhylomeDB; Q96GR4; -.
DR TreeFam; TF329809; -.
DR PathwayCommons; Q96GR4; -.
DR SignaLink; Q96GR4; -.
DR BioGRID-ORCS; 84885; 14 hits in 1075 CRISPR screens.
DR ChiTaRS; ZDHHC12; human.
DR GenomeRNAi; 84885; -.
DR Pharos; Q96GR4; Tdark.
DR PRO; PR:Q96GR4; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q96GR4; protein.
DR Bgee; ENSG00000160446; Expressed in mucosa of transverse colon and 112 other tissues.
DR ExpressionAtlas; Q96GR4; baseline and differential.
DR Genevisible; Q96GR4; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0097116; P:gephyrin clustering involved in postsynaptic density assembly; ISS:UniProtKB.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:UniProtKB.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; ISS:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; IDA: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 2: Evidence at transcript 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_0000212884"
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:0000250|UniProtKB:Q8VC90"
FT VAR_SEQ 33
FT /note="T -> TDKSADELLATHSHSWNQHLQAFAQPGTHFPTSNCTPTPPTPVLPGP
FT ASLCSPASP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016271"
FT VAR_SEQ 189..240
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:16303743"
FT /id="VSP_006945"
FT VARIANT 69
FT /note="P -> S (in dbSNP:rs2298039)"
FT /id="VAR_023833"
FT VARIANT 172
FT /note="Q -> L (in dbSNP:rs2900268)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16303743,
FT ECO:0000269|Ref.4"
FT /id="VAR_023834"
SQ SEQUENCE 267 AA; 30813 MW; 7A98B39BDFE43940 CRC64;
MAPWALLSPG VLVRTGHTVL TWGITLVLFL HDTELRQWEE QGELLLPLTF LLLVLGSLLL
YLAVSLMDPG YVNVQPQPQE ELKEEQTAMV PPAIPLRRCR YCLVLQPLRA RHCRECRRCV
RRYDHHCPWM ENCVGERNHP LFVVYLALQL VVLLWGLYLA WSGLRFFQPW GQWLRSSGLL
FATFLLLSLF SLVASLLLVS HLYLVASNTT TWEFISSHRI AYLRQRPSNP FDRGLTRNLA
HFFCGWPSGS WETLWAEEEE EGSSPAV
