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 24-JAN-2024, entry version 171. 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}; 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; 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; 27. DR IntAct; Q9NXF8; 9. DR STRING; 9606.ENSP00000456782; -. 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 ProteomicsDB; 83089; -. [Q9NXF8-1] DR ProteomicsDB; 83090; -. [Q9NXF8-2] DR Antibodypedia; 30621; 166 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 AGR; HGNC:18459; -. 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; 6683at2759; -. 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; 22 hits in 1156 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 209 other cell types or tissues. DR ExpressionAtlas; Q9NXF8; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. 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:0030521; P:androgen receptor signaling pathway; IMP:UniProt. 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:0050847; P:progesterone receptor signaling pathway; IMP:UniProt. DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProt. 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 GO; GO:0043401; P:steroid hormone mediated signaling pathway; IMP:UniProt. DR InterPro; IPR001594; Palmitoyltrfase_DHHC. DR PANTHER; PTHR22883:SF49; PALMITOYLTRANSFERASE ZDHHC7; 1. DR PANTHER; PTHR22883; ZINC FINGER DHHC DOMAIN CONTAINING PROTEIN; 1. DR Pfam; PF01529; DHHC; 1. DR PROSITE; PS50216; DHHC; 1. DR Genevisible; Q9NXF8; HS. 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 //