ZDHC7_HUMAN
ID ZDHC7_HUMAN Reviewed; 308 AA.
AC Q9NXF8; D3DUM1; Q8WV42; Q9NVD8;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Palmitoyltransferase ZDHHC7 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000269|PubMed:22031296, ECO:0000269|PubMed:25301068, ECO:0000269|PubMed:27380321, ECO:0000269|PubMed:28196865};
DE AltName: Full=Acyltransferase ZDHHC7 {ECO:0000250|UniProtKB:Q91WU6};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q91WU6};
DE AltName: Full=Zinc finger DHHC domain-containing protein 7 {ECO:0000312|HGNC:HGNC:18459};
DE Short=DHHC-7 {ECO:0000303|PubMed:22031296};
GN Name=ZDHHC7 {ECO:0000312|HGNC:HGNC:18459};
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] (ISOFORM 1).
RC TISSUE=Hepatoma, and 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 GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 97-308 (ISOFORM 1).
RC TISSUE=Duodenal mucosa, and Skin;
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 FUNCTION.
RX PubMed=19001095; DOI=10.1128/mcb.01144-08;
RA Tsutsumi R., Fukata Y., Noritake J., Iwanaga T., Perez F., Fukata M.;
RT "Identification of G protein alpha subunit-palmitoylating enzyme.";
RL Mol. Cell. Biol. 29:435-447(2009).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=22031296; DOI=10.1091/mbc.e11-07-0638;
RA Pedram A., Razandi M., Deschenes R.J., Levin E.R.;
RT "DHHC-7 and -21 are palmitoylacyltransferases for sex steroid receptors.";
RL Mol. Biol. Cell 23:188-199(2012).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25301068; DOI=10.1038/cdd.2014.153;
RA Rossin A., Durivault J., Chakhtoura-Feghali T., Lounnas N.,
RA Gagnoux-Palacios L., Hueber A.O.;
RT "Fas palmitoylation by the palmitoyl acyltransferase DHHC7 regulates Fas
RT stability.";
RL Cell Death Differ. 22:643-653(2015).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27380321; DOI=10.1038/nchembio.2119;
RA Chen B., Zheng B., DeRan M., Jarugumilli G.K., Fu J., Brooks Y.S., Wu X.;
RT "ZDHHC7-mediated S-palmitoylation of Scribble regulates cell polarity.";
RL Nat. Chem. Biol. 12:686-693(2016).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28196865; DOI=10.1074/jbc.m116.730523;
RA Aramsangtienchai P., Spiegelman N.A., Cao J., Lin H.;
RT "S-Palmitoylation of Junctional Adhesion Molecule C Regulates Its Tight
RT Junction Localization and Cell Migration.";
RL J. Biol. Chem. 292:5325-5334(2017).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-44.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Golgi-localized palmitoyltransferase that catalyzes the
CC addition of palmitate onto various protein substrates and therefore
CC functions in several unrelated biological processes (PubMed:22031296,
CC PubMed:27380321, PubMed:28196865). Has no stringent fatty acid
CC selectivity and in addition to palmitate can also transfer onto target
CC proteins myristate from tetradecanoyl-CoA and stearate from
CC octadecanoyl-CoA (By similarity). Palmitoylates sex steroid hormone
CC receptors, including ESR1, PGR and AR, thereby regulating their
CC targeting to the plasma membrane and their function in rapid
CC intracellular signaling upon binding of sex hormones (PubMed:22031296).
CC Palmitoylates GNAQ, a heterotrimeric G protein, regulating its dynamic
CC localization at the plasma membrane and is thereby involved in GNAQ-
CC dependent G protein-coupled receptor signaling pathways
CC (PubMed:19001095). Functions also in ligand-induced cell death by
CC regulating the FAS signaling pathway through the palmitoylation and
CC stabilization of the receptor at the plasma membrane (PubMed:25301068).
CC In epithelial cells, palmitoylates SCRIB and regulates its localization
CC to the plasma membrane, regulating indirectly cell polarity and
CC differentiation (PubMed:27380321). Also palmitoylates JAM3 and promotes
CC its expression at tight junctions and regulates its function in cell
CC migration (PubMed:28196865). Palmitoylates the glucose transporter
CC GLUT4/SLC2A4 and controls the insulin-dependent translocation of GLUT4
CC to the plasma membrane (By similarity). In brain, could also
CC palmitoylate SNAP25 and DLG4/PSD95 (By similarity). Could also
CC palmitoylate DNAJC5 and regulate its localization to the Golgi membrane
CC (By similarity). Could also palmitoylate NCDN (By similarity). May play
CC a role in follicle stimulation hormone (FSH) activation of testicular
CC Sertoli cells (By similarity). {ECO:0000250|UniProtKB:Q91WU6,
CC ECO:0000250|UniProtKB:Q923G5, ECO:0000269|PubMed:19001095,
CC ECO:0000269|PubMed:22031296, ECO:0000269|PubMed:25301068,
CC ECO:0000269|PubMed:27380321, ECO:0000269|PubMed:28196865}.
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:0000269|PubMed:22031296,
CC ECO:0000269|PubMed:25301068, ECO:0000269|PubMed:27380321,
CC ECO:0000269|PubMed:28196865};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000269|PubMed:25301068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + tetradecanoyl-CoA = CoA + S-
CC tetradecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59736, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:15433, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:143199;
CC Evidence={ECO:0000250|UniProtKB:Q91WU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737;
CC Evidence={ECO:0000250|UniProtKB:Q91WU6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + octadecanoyl-CoA = CoA + S-
CC octadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59740, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:15434, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:143200;
CC Evidence={ECO:0000250|UniProtKB:Q91WU6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741;
CC Evidence={ECO:0000250|UniProtKB:Q91WU6};
CC -!- SUBUNIT: Homooligomers. Heterooligomers with ZDHHC3.
CC {ECO:0000250|UniProtKB:Q91WU6}.
CC -!- INTERACTION:
CC Q9NXF8-2; P49447: CYB561; NbExp=3; IntAct=EBI-12948063, EBI-8646596;
CC Q9NXF8-2; O43561-2: LAT; NbExp=3; IntAct=EBI-12948063, EBI-8070286;
CC Q9NXF8-2; Q9Y548: YIPF1; NbExp=3; IntAct=EBI-12948063, EBI-7850136;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:22031296}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NXF8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NXF8-2; Sequence=VSP_006942;
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- PTM: Autopalmitoylated. {ECO:0000250|UniProtKB:Q91WU6}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17702.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91814.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK000286; BAA91055.1; -; mRNA.
DR EMBL; AK001654; BAA91814.1; ALT_INIT; mRNA.
DR EMBL; CH471114; EAW95464.1; -; Genomic_DNA.
DR EMBL; CH471114; EAW95465.1; -; Genomic_DNA.
DR EMBL; BC017702; AAH17702.1; ALT_INIT; mRNA.
DR EMBL; BC018772; AAH18772.1; -; mRNA.
DR CCDS; CCDS10950.1; -. [Q9NXF8-1]
DR CCDS; CCDS45538.1; -. [Q9NXF8-2]
DR RefSeq; NP_001139020.1; NM_001145548.1. [Q9NXF8-2]
DR RefSeq; NP_060210.2; NM_017740.2. [Q9NXF8-1]
DR AlphaFoldDB; Q9NXF8; -.
DR SMR; Q9NXF8; -.
DR BioGRID; 120764; 24.
DR IntAct; Q9NXF8; 9.
DR iPTMnet; Q9NXF8; -.
DR PhosphoSitePlus; Q9NXF8; -.
DR SwissPalm; Q9NXF8; -.
DR BioMuta; ZDHHC7; -.
DR DMDM; 116242853; -.
DR EPD; Q9NXF8; -.
DR jPOST; Q9NXF8; -.
DR MassIVE; Q9NXF8; -.
DR MaxQB; Q9NXF8; -.
DR PeptideAtlas; Q9NXF8; -.
DR PRIDE; Q9NXF8; -.
DR ProteomicsDB; 83089; -. [Q9NXF8-1]
DR ProteomicsDB; 83090; -. [Q9NXF8-2]
DR Antibodypedia; 30621; 147 antibodies from 26 providers.
DR DNASU; 55625; -.
DR Ensembl; ENST00000313732.9; ENSP00000315604.5; ENSG00000153786.13. [Q9NXF8-1]
DR Ensembl; ENST00000344861.9; ENSP00000341681.5; ENSG00000153786.13. [Q9NXF8-2]
DR Ensembl; ENST00000564466.5; ENSP00000456782.1; ENSG00000153786.13. [Q9NXF8-2]
DR GeneID; 55625; -.
DR KEGG; hsa:55625; -.
DR MANE-Select; ENST00000313732.9; ENSP00000315604.5; NM_017740.3; NP_060210.2.
DR UCSC; uc002fiq.3; human. [Q9NXF8-1]
DR CTD; 55625; -.
DR DisGeNET; 55625; -.
DR GeneCards; ZDHHC7; -.
DR HGNC; HGNC:18459; ZDHHC7.
DR HPA; ENSG00000153786; Low tissue specificity.
DR MIM; 614604; gene.
DR neXtProt; NX_Q9NXF8; -.
DR OpenTargets; ENSG00000153786; -.
DR PharmGKB; PA38335; -.
DR VEuPathDB; HostDB:ENSG00000153786; -.
DR GeneTree; ENSGT00940000156519; -.
DR HOGENOM; CLU_048061_1_1_1; -.
DR InParanoid; Q9NXF8; -.
DR OMA; WYSMING; -.
DR OrthoDB; 1491968at2759; -.
DR PhylomeDB; Q9NXF8; -.
DR TreeFam; TF319798; -.
DR PathwayCommons; Q9NXF8; -.
DR Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
DR SignaLink; Q9NXF8; -.
DR BioGRID-ORCS; 55625; 20 hits in 1076 CRISPR screens.
DR ChiTaRS; ZDHHC7; human.
DR GenomeRNAi; 55625; -.
DR Pharos; Q9NXF8; Tbio.
DR PRO; PR:Q9NXF8; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9NXF8; protein.
DR Bgee; ENSG00000153786; Expressed in secondary oocyte and 207 other tissues.
DR ExpressionAtlas; Q9NXF8; baseline and differential.
DR Genevisible; Q9NXF8; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0016409; F:palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0019705; F:protein-cysteine S-myristoyltransferase activity; IEA:RHEA.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; IEA:RHEA.
DR GO; GO:0044381; P:glucose import in response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0009895; P:negative regulation of catabolic process; IMP:UniProtKB.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IDA:UniProtKB.
DR GO; GO:0030859; P:polarized epithelial cell differentiation; IMP:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR GO; GO:1902044; P:regulation of Fas signaling pathway; IMP:UniProtKB.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0150106; P:regulation of protein localization to cell-cell junction; IMP:UniProtKB.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; IMP:UniProtKB.
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; Golgi apparatus; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..308
FT /note="Palmitoyltransferase ZDHHC7"
FT /id="PRO_0000212874"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..75
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..217
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 130..180
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 160
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT VAR_SEQ 105
FT /note="P -> PEKSSDCRPSACTVKTGLDPTLVGICGEGTESVQSLLL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_006942"
FT VARIANT 44
FT /note="D -> N (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036261"
FT VARIANT 201
FT /note="V -> I (in dbSNP:rs13334011)"
FT /id="VAR_028360"
FT CONFLICT 22
FT /note="N -> D (in Ref. 1; BAA91055)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 35140 MW; 0E4F2E69A62C90C3 CRC64;
MQPSGHRLRD VEHHPLLAEN DNYDSSSSSS SEADVADRVW FIRDGCGMIC AVMTWLLVAY
ADFVVTFVML LPSKDFWYSV VNGVIFNCLA VLALSSHLRT MLTDPGAVPK GNATKEYMES
LQLKPGEVIY KCPKCCCIKP ERAHHCSICK RCIRKMDHHC PWVNNCVGEK NQRFFVLFTM
YIALSSVHAL ILCGFQFISC VRGQWTECSD FSPPITVILL IFLCLEGLLF FTFTAVMFGT
QIHSICNDET EIERLKSEKP TWERRLRWEG MKSVFGGPPS LLWMNPFVGF RFRRLPTRPR
KGGPEFSV
