ZDH17_RAT
ID ZDH17_RAT Reviewed; 622 AA.
AC E9PTT0; Q2TGJ2;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Palmitoyltransferase ZDHHC17 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q80TN5};
DE AltName: Full=Acyltransferase ZDHHC17 {ECO:0000250|UniProtKB:Q80TN5};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q80TN5};
DE AltName: Full=Zinc finger DHHC domain-containing protein 17 {ECO:0000312|RGD:1595790};
GN Name=Zdhhc17 {ECO:0000312|RGD:1595790};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Huang C.-H., Chen Y., Ye T.;
RT "A superfamily of membrane-associated DHHC type zinc finger proteins.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP INTERACTION WITH DNAJC5 AND SNAP25.
RX PubMed=25253725; DOI=10.1091/mbc.e14-06-1169;
RA Lemonidis K., Gorleku O.A., Sanchez-Perez M.C., Grefen C.,
RA Chamberlain L.H.;
RT "The Golgi S-acylation machinery comprises zDHHC enzymes with major
RT differences in substrate affinity and S-acylation activity.";
RL Mol. Biol. Cell 25:3870-3883(2014).
RN [4]
RP INTERACTION WITH SNAP25.
RX PubMed=26198635; DOI=10.1074/jbc.m115.657668;
RA Lemonidis K., Sanchez-Perez M.C., Chamberlain L.H.;
RT "Identification of a novel sequence motif recognized by the ankyrin repeat
RT domain of zDHHC17/13 S-acyltransferases.";
RL J. Biol. Chem. 290:21939-21950(2015).
CC -!- FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate
CC onto various protein substrates and is involved in a variety of
CC cellular processes. Has no stringent fatty acid selectivity and in
CC addition to palmitate can also transfer onto target proteins myristate
CC from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (By
CC similarity). Palmitoyltransferase specific for a subset of neuronal
CC proteins, including SNAP25, DLG4/PSD95, GAD2, SYT1 and HTT (By
CC similarity). Also palmitoylates neuronal protein GPM6A as well as
CC SPRED1 and SPRED3 (By similarity). Could also play a role in
CC axonogenesis through the regulation of NTRK1 and the downstream
CC ERK1/ERK2 signaling cascade (By similarity). May be involved in the
CC sorting or targeting of critical proteins involved in the initiating
CC events of endocytosis at the plasma membrane (By similarity). May play
CC a role in Mg(2+) transport (By similarity). Could also palmitoylate
CC DNAJC5 and regulate its localization to the Golgi membrane (By
CC similarity). Palmitoylates CASP6, thereby preventing its dimerization
CC and subsequent activation (By similarity).
CC {ECO:0000250|UniProtKB:Q80TN5, ECO:0000250|UniProtKB:Q8IUH5}.
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:Q8IUH5};
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:Q80TN5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737;
CC Evidence={ECO:0000250|UniProtKB:Q80TN5};
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:Q80TN5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741;
CC Evidence={ECO:0000250|UniProtKB:Q80TN5};
CC -!- SUBUNIT: Interacts (via ANK repeats) with numerous proteins (via the
CC consensus sequence motif [VIAP]-[VIT]-x-x-Q-P). Interacts (via ANK
CC repeats) with CLIP3. Interacts (via ANK repeats) with HTT (By
CC similarity). Interacts (via ANK repeats) with DNAJC5 (via C-terminus)
CC (PubMed:25253725). Interacts (via ANK repeats) with MAP6. Interacts
CC (via ANK repeats) with SNAP23 (By similarity). Interacts (via ANK
CC repeats) with SNAP25(PubMed:25253725, PubMed:26198635). Interacts (via
CC ANK repeats) with EVL (By similarity). Interacts with SPRED1 and SPRED3
CC (By similarity). Interacts with GPM6A and OPTN (By similarity). May
CC interact (via ANK repeats) with SPRED2 (By similarity). May interact
CC with NTRK1; may regulate its localization and function (By similarity).
CC {ECO:0000250|UniProtKB:Q80TN5, ECO:0000250|UniProtKB:Q8IUH5,
CC ECO:0000269|PubMed:25253725, ECO:0000269|PubMed:26198635}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8IUH5}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q8IUH5}; Multi-pass membrane protein
CC {ECO:0000255}. Presynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q8IUH5}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Low extracellular Mg(2+) induces increase in Golgi
CC and in post-Golgi membrane vesicles. {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- PTM: Autopalmitoylated. Autopalmitoylation has a regulatory role in
CC ZDHHC17-mediated Mg(2+) transport. {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC AKR/ZDHHC17 subfamily. {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; AY886533; AAX73395.1; -; mRNA.
DR EMBL; AABR06049566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06049567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06049568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001034429.1; NM_001039340.1.
DR AlphaFoldDB; E9PTT0; -.
DR SMR; E9PTT0; -.
DR STRING; 10116.ENSRNOP00000005078; -.
DR jPOST; E9PTT0; -.
DR PaxDb; E9PTT0; -.
DR PeptideAtlas; E9PTT0; -.
DR PRIDE; E9PTT0; -.
DR GeneID; 366889; -.
DR KEGG; rno:366889; -.
DR CTD; 23390; -.
DR RGD; 1595790; Zdhhc17.
DR VEuPathDB; HostDB:ENSRNOG00000003803; -.
DR eggNOG; KOG0509; Eukaryota.
DR HOGENOM; CLU_012510_3_1_1; -.
DR InParanoid; E9PTT0; -.
DR OMA; PWMAGIF; -.
DR OrthoDB; 445686at2759; -.
DR TreeFam; TF317342; -.
DR PRO; PR:E9PTT0; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000003803; Expressed in cerebellum and 18 other tissues.
DR GO; GO:0016235; C:aggresome; IEA:Ensembl.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISO:RGD.
DR GO; GO:0030660; C:Golgi-associated vesicle membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0016409; F:palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0019705; F:protein-cysteine S-myristoyltransferase activity; IEA:RHEA.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; IEA:RHEA.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR GO; GO:0042953; P:lipoprotein transport; ISO:RGD.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISO:RGD.
DR GO; GO:0018345; P:protein palmitoylation; ISS:UniProtKB.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0051386; P:regulation of neurotrophin TRK receptor signaling pathway; ISS:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR030289; ZDHHC17.
DR PANTHER; PTHR24161:SF18; PTHR24161:SF18; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF01529; DHHC; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50216; DHHC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; ANK repeat; Cell membrane; Cell projection;
KW Cytoplasmic vesicle; Golgi apparatus; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Repeat; Synapse; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..622
FT /note="Palmitoyltransferase ZDHHC17"
FT /id="PRO_0000433513"
FT TOPO_DOM 1..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..347
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..470
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..506
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 507..526
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 527..529
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 530..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 41..76
FT /note="ANK 1"
FT /evidence="ECO:0000250|UniProtKB:Q8IUH5"
FT REPEAT 79..108
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 113..142
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 146..175
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 179..209
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 214..243
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT REPEAT 247..276
FT /note="ANK 7"
FT /evidence="ECO:0000255"
FT DOMAIN 427..477
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 1..295
FT /note="Necessary and sufficient for interaction with DNAJC5
FT and SNAP25"
FT /evidence="ECO:0000250|UniProtKB:Q80TN5"
FT ACT_SITE 457
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q8IUH5"
FT CONFLICT 465
FT /note="G -> C (in Ref. 1; AAX73395)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 71319 MW; 845F70BCA572BE49 CRC64;
MADGPDEYDT ETGCVPLLHP EEIKPQSHYN HGYGEPLGRK THVDDYSTWD IVKATQYGIY
ERCRELVEAG YDVRQPDKEN VTLLHWAAIN NRIDLVKYYI SKGAIVDQLG GDLNSTPLHW
ATRQGHLSMV VQLMKYGADP SLIDGEGCSC IHLAAQFGHT SIVAYLIAKG QDVDMMDQNG
MTPLMWAAYR THSVDPTRLL LTFNVSVNLG DKYHKNTALH WAVLAGNTTV ISLLLEAGGN
VDAQNVKGES ALDLAKQRKN VWMINHLQEA RQAKGYDNPS FLRKLKADKE FRQKVMLGTP
FLVIWLVGFI ADLNIDSWLI KGLMYGGVWA TVQFLSKSFF DHSMHSALPL GIYLATKFWM
YVTWFFWFWN DLSFLSIHLP FLANSVALFY NFGKSWKSDP GIIKATEEQK KKTIVELAET
GSLDLSIFCS TCLIRKPVRS KHCGVCNRCI AKFDHHCPWV GNCVGAGNHR YFMGYLFFLL
FMICWMIYGC VSYWGLHCET TYTKDGFWTY ITQIATCSPW MFWMFLNSVF HFMWVAVLLM
CQMYQITCLG ITTNERMNAR RYKHFKVTTT SIESPFNHGC VRNIIDFFEF RCCGLFRPVI
VDWTRQYTIE YDQISGSGYQ LV
