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ZDH20_HUMAN
ID   ZDH20_HUMAN             Reviewed;         365 AA.
AC   Q5W0Z9; A8MTV9; C9JG20; I6L9D4; Q2TB82; Q6NVU8;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Palmitoyltransferase ZDHHC20 {ECO:0000305|PubMed:27153536};
DE            EC=2.3.1.225 {ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:29326245};
DE   AltName: Full=Acyltransferase ZDHHC20 {ECO:0000305|PubMed:29326245};
DE            EC=2.3.1.- {ECO:0000305|PubMed:29326245};
DE   AltName: Full=DHHC domain-containing cysteine-rich protein 20 {ECO:0000303|PubMed:27153536};
DE            Short=DHHC20 {ECO:0000303|PubMed:27153536};
DE   AltName: Full=Zinc finger DHHC domain-containing protein 20 {ECO:0000312|HGNC:HGNC:20749};
GN   Name=ZDHHC20 {ECO:0000312|HGNC:HGNC:20749};
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 GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC   TISSUE=Ovary, and Testis;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305 AND SER-330, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX   PubMed=27153536; DOI=10.1016/j.molcel.2016.04.003;
RA   Runkle K.B., Kharbanda A., Stypulkowski E., Cao X.J., Wang W., Garcia B.A.,
RA   Witze E.S.;
RT   "Inhibition of DHHC20-Mediated EGFR Palmitoylation Creates a Dependence on
RT   EGFR Signaling.";
RL   Mol. Cell 62:385-396(2016).
RN   [9]
RP   FUNCTION (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND CATALYTIC
RP   ACTIVITY.
RX   PubMed=34599882; DOI=10.1016/j.devcel.2021.09.016;
RA   Mesquita F.S., Abrami L., Sergeeva O., Turelli P., Qing E., Kunz B.,
RA   Raclot C., Paz Montoya J., Abriata L.A., Gallagher T., Dal Peraro M.,
RA   Trono D., D'Angelo G., van der Goot F.G.;
RT   "S-acylation controls SARS-CoV-2 membrane lipid organization and enhances
RT   infectivity.";
RL   Dev. Cell 56:1-18(2021).
RN   [10]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=33219126; DOI=10.1074/jbc.ra120.015701;
RA   Malgapo M.I.P., Safadi J.M., Linder M.E.;
RT   "Metallo-beta-Lactamase Domain-Containing Protein 2 (MBLAC2) is S-
RT   palmitoylated and exhibits acyl-CoA hydrolase activity.";
RL   J. Biol. Chem. 296:100106-100118(2021).
RN   [11] {ECO:0007744|PDB:6BML, ECO:0007744|PDB:6BMM, ECO:0007744|PDB:6BMN}
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 5-299 IN COMPLEX WITH PALMITATE;
RP   SUBSTRATE ANALOG AND ZINC, FUNCTION, CATALYTIC ACTIVITY, DOMAIN,
RP   MUTAGENESIS OF ILE-22; SER-29; ASP-153; HIS-154; CYS-156; TRP-158; PHE-171;
RP   PHE-174; TYR-181; LEU-227; 240-THR-THR-241; GLU-243; ASN-266; TRP-267 AND
RP   PHE-271, ACTIVE SITE, SUBCELLULAR LOCATION, TOPOLOGY, AND PALMITOYLATION.
RX   PubMed=29326245; DOI=10.1126/science.aao6326;
RA   Rana M.S., Kumar P., Lee C.J., Verardi R., Rajashankar K.R., Banerjee A.;
RT   "Fatty acyl recognition and transfer by an integral membrane S-
RT   acyltransferase.";
RL   Science 359:0-0(2018).
CC   -!- FUNCTION: Palmitoyltransferase that could catalyze the addition of
CC       palmitate onto various protein substrates (PubMed:27153536,
CC       PubMed:29326245, PubMed:33219126). Catalyzes palmitoylation of Cys
CC       residues in the cytoplasmic C-terminus of EGFR, and modulates the
CC       duration of EGFR signaling by modulating palmitoylation-dependent EGFR
CC       internalization and degradation (PubMed:27153536). Has a preference for
CC       acyl-CoA with C16 fatty acid chains (PubMed:29326245). Can also utilize
CC       acyl-CoA with C14 and C18 fatty acid chains (PubMed:29326245).
CC       {ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:29326245,
CC       ECO:0000269|PubMed:33219126}.
CC   -!- FUNCTION: (Microbial infection) Dominant palmitoyltransferase
CC       responsible for lipidation of SARS coronavirus-2/SARS-CoV-2 spike
CC       protein. Through a sequential action with ZDHHC9, rapidly and
CC       efficiently palmitoylates spike protein following its synthesis in the
CC       endoplasmic reticulum (ER). In the infected cell, promotes spike
CC       biogenesis by protecting it from premature ER degradation, increases
CC       half-life and controls the lipid organization of its immediate membrane
CC       environment. Once the virus has formed, spike palmitoylation controls
CC       fusion with the target cell. {ECO:0000269|PubMed:34599882}.
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:29326245,
CC         ECO:0000269|PubMed:33219126, ECO:0000269|PubMed:34599882};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC         Evidence={ECO:0000305|PubMed:29326245};
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:0000269|PubMed:29326245};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737;
CC         Evidence={ECO:0000305|PubMed:29326245};
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:0000269|PubMed:29326245};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741;
CC         Evidence={ECO:0000305|PubMed:29326245};
CC   -!- INTERACTION:
CC       Q5W0Z9-4; P07339: CTSD; NbExp=3; IntAct=EBI-25840130, EBI-2115097;
CC       Q5W0Z9-4; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-25840130, EBI-396669;
CC       Q5W0Z9-4; O76024: WFS1; NbExp=3; IntAct=EBI-25840130, EBI-720609;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:29326245}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:29326245}. Cell membrane
CC       {ECO:0000269|PubMed:27153536}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:29326245}. Cytoplasm, perinuclear region
CC       {ECO:0000269|PubMed:27153536}. Endoplasmic reticulum membrane
CC       {ECO:0000305|PubMed:34599882}; Multi-pass membrane protein
CC       {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment
CC       membrane {ECO:0000305|PubMed:34599882}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q5W0Z9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5W0Z9-2; Sequence=VSP_016276, VSP_016277;
CC       Name=3;
CC         IsoId=Q5W0Z9-3; Sequence=VSP_040481, VSP_040482;
CC       Name=4;
CC         IsoId=Q5W0Z9-4; Sequence=VSP_056002;
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC       {ECO:0000269|PubMed:29326245}.
CC   -!- PTM: Autopalmitoylated (in vitro). {ECO:0000269|PubMed:29326245}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AL136219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471075; EAX08309.1; -; Genomic_DNA.
DR   EMBL; BC034944; AAH34944.1; -; mRNA.
DR   EMBL; BC050367; AAH50367.2; -; mRNA.
DR   EMBL; BC067898; AAH67898.1; -; mRNA.
DR   EMBL; BC110517; AAI10518.1; -; mRNA.
DR   CCDS; CCDS45017.1; -. [Q5W0Z9-3]
DR   CCDS; CCDS81758.1; -. [Q5W0Z9-1]
DR   RefSeq; NP_001273567.1; NM_001286638.1.
DR   RefSeq; NP_001316988.1; NM_001330059.1. [Q5W0Z9-1]
DR   RefSeq; NP_694983.2; NM_153251.3. [Q5W0Z9-3]
DR   PDB; 6BML; X-ray; 2.95 A; A/B=5-299.
DR   PDB; 6BMM; X-ray; 2.35 A; A/B=7-299.
DR   PDB; 6BMN; X-ray; 2.25 A; A/B=5-299.
DR   PDB; 7KHM; X-ray; 2.88 A; A/B=2-316.
DR   PDBsum; 6BML; -.
DR   PDBsum; 6BMM; -.
DR   PDBsum; 6BMN; -.
DR   PDBsum; 7KHM; -.
DR   AlphaFoldDB; Q5W0Z9; -.
DR   SMR; Q5W0Z9; -.
DR   BioGRID; 128991; 37.
DR   IntAct; Q5W0Z9; 11.
DR   MINT; Q5W0Z9; -.
DR   STRING; 9606.ENSP00000371905; -.
DR   TCDB; 8.A.114.1.6; the huntington-interacting protein 14 (hip14) family.
DR   iPTMnet; Q5W0Z9; -.
DR   PhosphoSitePlus; Q5W0Z9; -.
DR   SwissPalm; Q5W0Z9; -.
DR   BioMuta; ZDHHC20; -.
DR   DMDM; 74748004; -.
DR   EPD; Q5W0Z9; -.
DR   jPOST; Q5W0Z9; -.
DR   MassIVE; Q5W0Z9; -.
DR   MaxQB; Q5W0Z9; -.
DR   PaxDb; Q5W0Z9; -.
DR   PeptideAtlas; Q5W0Z9; -.
DR   PRIDE; Q5W0Z9; -.
DR   ProteomicsDB; 61482; -.
DR   ProteomicsDB; 65788; -. [Q5W0Z9-1]
DR   ProteomicsDB; 65789; -. [Q5W0Z9-2]
DR   ProteomicsDB; 65790; -. [Q5W0Z9-3]
DR   Antibodypedia; 4929; 196 antibodies from 24 providers.
DR   DNASU; 253832; -.
DR   Ensembl; ENST00000320220.13; ENSP00000313583.9; ENSG00000180776.16. [Q5W0Z9-4]
DR   Ensembl; ENST00000382466.7; ENSP00000371905.3; ENSG00000180776.16. [Q5W0Z9-3]
DR   Ensembl; ENST00000400590.8; ENSP00000383433.3; ENSG00000180776.16. [Q5W0Z9-1]
DR   Ensembl; ENST00000415724.2; ENSP00000401232.1; ENSG00000180776.16. [Q5W0Z9-1]
DR   GeneID; 253832; -.
DR   KEGG; hsa:253832; -.
DR   MANE-Select; ENST00000400590.8; ENSP00000383433.3; NM_001330059.2; NP_001316988.1.
DR   UCSC; uc001uoa.4; human. [Q5W0Z9-1]
DR   CTD; 253832; -.
DR   DisGeNET; 253832; -.
DR   GeneCards; ZDHHC20; -.
DR   HGNC; HGNC:20749; ZDHHC20.
DR   HPA; ENSG00000180776; Tissue enhanced (brain).
DR   MIM; 617972; gene.
DR   neXtProt; NX_Q5W0Z9; -.
DR   OpenTargets; ENSG00000180776; -.
DR   PharmGKB; PA134880838; -.
DR   VEuPathDB; HostDB:ENSG00000180776; -.
DR   eggNOG; KOG1315; Eukaryota.
DR   GeneTree; ENSGT00940000153716; -.
DR   InParanoid; Q5W0Z9; -.
DR   OMA; QPDSNKC; -.
DR   OrthoDB; 1491968at2759; -.
DR   PhylomeDB; Q5W0Z9; -.
DR   TreeFam; TF316044; -.
DR   PathwayCommons; Q5W0Z9; -.
DR   Reactome; R-HSA-9694548; Maturation of spike protein.
DR   SignaLink; Q5W0Z9; -.
DR   BioGRID-ORCS; 253832; 19 hits in 1077 CRISPR screens.
DR   ChiTaRS; ZDHHC20; human.
DR   GenomeRNAi; 253832; -.
DR   Pharos; Q5W0Z9; Tbio.
DR   PRO; PR:Q5W0Z9; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; Q5W0Z9; protein.
DR   Bgee; ENSG00000180776; Expressed in upper arm skin and 189 other tissues.
DR   ExpressionAtlas; Q5W0Z9; baseline and differential.
DR   Genevisible; Q5W0Z9; HS.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0030173; C:integral component of Golgi membrane; IMP:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IDA: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   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Alternative splicing; Cell membrane;
KW   Cytoplasm; Endoplasmic reticulum; Golgi apparatus; Host-virus interaction;
KW   Lipoprotein; Membrane; Metal-binding; Palmitate; Phosphoprotein;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..365
FT                   /note="Palmitoyltransferase ZDHHC20"
FT                   /id="PRO_0000212906"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   TOPO_DOM        36..53
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   TOPO_DOM        75..169
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   TOPO_DOM        191..207
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   TRANSMEM        208..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   TOPO_DOM        232..365
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   DOMAIN          126..176
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   ACT_SITE        156
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   BINDING         128
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:29326245,
FT                   ECO:0007744|PDB:6BMN"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:29326245,
FT                   ECO:0007744|PDB:6BMN"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:29326245"
FT   BINDING         140..143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:29326245"
FT   BINDING         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:29326245,
FT                   ECO:0007744|PDB:6BMN"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:29326245,
FT                   ECO:0007744|PDB:6BMN"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:29326245,
FT                   ECO:0007744|PDB:6BMN"
FT   BINDING         148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:29326245,
FT                   ECO:0007744|PDB:6BMN"
FT   BINDING         155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:29326245,
FT                   ECO:0007744|PDB:6BMN"
FT   BINDING         162
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:29326245,
FT                   ECO:0007744|PDB:6BMN"
FT   SITE            29
FT                   /note="Important for selectivity toward medium-length fatty
FT                   acids"
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   SITE            181
FT                   /note="Important for selectivity toward medium-length fatty
FT                   acids"
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   MOD_RES         305
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         330
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         339
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17525332"
FT   VAR_SEQ         124..130
FT                   /note="TIRYCEK -> SLMQSTK (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_016276"
FT   VAR_SEQ         131..365
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_016277"
FT   VAR_SEQ         315..365
FT                   /note="SSGSNQPFPIKPLSESKNRLLDSESQWLENGAEEGIVKSGTNNHVTVAIEN
FT                   -> RSKLQR (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056002"
FT   VAR_SEQ         315
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_040481"
FT   VAR_SEQ         355..365
FT                   /note="TNNHVTVAIEN -> V (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_040482"
FT   MUTAGEN         22
FT                   /note="I->W: Strongly reduced catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   MUTAGEN         29
FT                   /note="S->F: Strongly reduced catalytic activity. Enhances
FT                   activity with acyl-CoA with C12 and C14 fatty acid chains."
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   MUTAGEN         153
FT                   /note="D->A: Loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   MUTAGEN         154
FT                   /note="H->A: Loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   MUTAGEN         156
FT                   /note="C->S: Loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   MUTAGEN         158
FT                   /note="W->A: Strongly reduced catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   MUTAGEN         171
FT                   /note="F->A: Loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   MUTAGEN         174
FT                   /note="F->A: Strongly reduced catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   MUTAGEN         181
FT                   /note="Y->A: Moderately reduced catalytic activity.
FT                   Enhances activity with acyl-CoA with C18 and C20 fatty acid
FT                   chains."
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   MUTAGEN         227
FT                   /note="L->W: Loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   MUTAGEN         240..241
FT                   /note="TT->AA: Loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   MUTAGEN         243
FT                   /note="E->A: Mildly reduced catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   MUTAGEN         266
FT                   /note="N->A: Strongly reduced catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   MUTAGEN         267
FT                   /note="Missing: Loss of catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   MUTAGEN         271
FT                   /note="F->A: Mildly reduced catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:29326245"
FT   HELIX           7..14
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   HELIX           17..34
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   HELIX           35..42
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   TURN            43..46
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   HELIX           48..74
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   HELIX           82..84
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   HELIX           90..96
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   HELIX           100..111
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   TURN            112..115
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   TURN            129..132
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   STRAND          140..142
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   TURN            143..146
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   STRAND          147..149
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   STRAND          154..156
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   HELIX           157..159
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   STRAND          161..164
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   TURN            165..167
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   HELIX           168..197
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   HELIX           204..237
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   HELIX           241..245
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   TURN            256..259
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   HELIX           263..271
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   HELIX           275..277
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   STRAND          280..282
FT                   /evidence="ECO:0007829|PDB:6BMN"
FT   STRAND          295..297
FT                   /evidence="ECO:0007829|PDB:6BMN"
SQ   SEQUENCE   365 AA;  42278 MW;  179D8882138E4F53 CRC64;
     MAPWTLWRCC QRVVGWVPVL FITFVVVWSY YAYVVELCVF TIFGNEENGK TVVYLVAFHL
     FFVMFVWSYW MTIFTSPASP SKEFYLSNSE KERYEKEFSQ ERQQEILRRA ARALPIYTTS
     ASKTIRYCEK CQLIKPDRAH HCSACDSCIL KMDHHCPWVN NCVGFSNYKF FLLFLLYSLL
     YCLFVAATVL EYFIKFWTNE LTDTRAKFHV LFLFFVSAMF FISVLSLFSY HCWLVGKNRT
     TIESFRAPTF SYGPDGNGFS LGCSKNWRQV FGDEKKYWLL PIFSSLGDGC SFPTRLVGMD
     PEQASVTNQN EYARSSGSNQ PFPIKPLSES KNRLLDSESQ WLENGAEEGI VKSGTNNHVT
     VAIEN
 
 
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