ZDH13_MOUSE
ID ZDH13_MOUSE Reviewed; 622 AA.
AC Q9CWU2; Q3UK32; Q3UKV1;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Palmitoyltransferase ZDHHC13 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000269|PubMed:19299482, ECO:0000269|PubMed:20548961};
DE AltName: Full=Huntingtin-interacting protein 14-related protein {ECO:0000303|PubMed:18794299};
DE Short=HIP14-related protein {ECO:0000303|PubMed:18794299};
DE AltName: Full=Zinc finger DHHC domain-containing protein 13 {ECO:0000312|MGI:MGI:1919227};
DE Short=DHHC-13 {ECO:0000303|PubMed:19299482};
GN Name=Zdhhc13 {ECO:0000312|MGI:MGI:1919227}; Synonyms=Hip14l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
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 [3]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18794299; DOI=10.1074/jbc.m801469200;
RA Goytain A., Hines R.M., Quamme G.A.;
RT "Huntingtin-interacting proteins, HIP14 and HIP14L, mediate dual functions,
RT palmitoyl acyltransferase and Mg2+ transport.";
RL J. Biol. Chem. 283:33365-33374(2008).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=19299482; DOI=10.1096/fj.08-127399;
RA Huang K., Sanders S., Singaraja R., Orban P., Cijsouw T., Arstikaitis P.,
RA Yanai A., Hayden M.R., El-Husseini A.;
RT "Neuronal palmitoyl acyl transferases exhibit distinct substrate
RT specificity.";
RL FASEB J. 23:2605-2615(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=20548961; DOI=10.1371/journal.pgen.1000985;
RA Saleem A.N., Chen Y.H., Baek H.J., Hsiao Y.W., Huang H.W., Kao H.J.,
RA Liu K.M., Shen L.F., Song I.W., Tu C.P., Wu J.Y., Kikuchi T., Justice M.J.,
RA Yen J.J., Chen Y.T.;
RT "Mice with alopecia, osteoporosis, and systemic amyloidosis due to mutation
RT in Zdhhc13, a gene coding for palmitoyl acyltransferase.";
RL PLoS Genet. 6:e1000985-e1000985(2010).
RN [7]
RP INTERACTION WITH DNAJC5 AND SNAP25, AND SUBCELLULAR LOCATION.
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 [8]
RP INTERACTION WITH CLIP3; DNAJC5; HTT; MAP6; SNAP23 AND 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).
RN [9]
RP INTERACTION WITH SPRED2.
RX PubMed=28882895; DOI=10.1074/jbc.m117.799650;
RA Lemonidis K., MacLeod R., Baillie G.S., Chamberlain L.H.;
RT "Peptide array based screening reveals a large number of proteins
RT interacting with the ankyrin repeat domain of the zDHHC17 S-
RT acyltransferase.";
RL J. Biol. Chem. 292:17190-17202(2017).
CC -!- FUNCTION: Palmitoyltransferase that could catalyze the addition of
CC palmitate onto various protein substrates (PubMed:18794299,
CC PubMed:19299482). Palmitoyltransferase for HTT and GAD2
CC (PubMed:19299482, PubMed:20548961). May play a role in Mg(2+) transport
CC (PubMed:18794299). {ECO:0000269|PubMed:18794299,
CC ECO:0000269|PubMed:19299482}.
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:19299482,
CC ECO:0000269|PubMed:20548961};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000305|PubMed:19299482};
CC -!- SUBUNIT: Interacts (via ANK repeats) with CLIP3 (PubMed:26198635).
CC Interacts (via ANK repeats) with DNAJC5 (via C-terminus)
CC (PubMed:25253725, PubMed:26198635). Interacts (via ANK repeats) with
CC HTT (PubMed:26198635). Interacts (via ANK repeats) with MAP6
CC (PubMed:26198635). Interacts (via ANK repeats) with SNAP23
CC (PubMed:26198635). Interacts (via ANK repeats) with SNAP25
CC (PubMed:25253725, PubMed:26198635). May interact (via ANK repeats) with
CC SPRED2 (PubMed:28882895). {ECO:0000269|PubMed:25253725,
CC ECO:0000269|PubMed:26198635, ECO:0000269|PubMed:28882895}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:18794299, ECO:0000269|PubMed:19299482,
CC ECO:0000269|PubMed:25253725}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:18794299}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Low extracellular Mg(2+) induces increase in Golgi
CC and in post-Golgi vesicles. {ECO:0000269|PubMed:18794299}.
CC -!- TISSUE SPECIFICITY: Expressed in most adult tissues, but at low levels
CC in the liver, skin, and lung. {ECO:0000269|PubMed:20548961}.
CC -!- DEVELOPMENTAL STAGE: Expressed most highly in the liver, lung, and
CC brain at posnatal day 2 (P2). In contrast, expressed most highly in
CC skin at P8 in the epithelium surrounding the hair follicles.
CC {ECO:0000269|PubMed:20548961}.
CC -!- INDUCTION: Up-regulated by low extracellular Mg(2+).
CC {ECO:0000269|PubMed:18794299}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- DISRUPTION PHENOTYPE: Knockdown of the expression in mice through ENU-
CC induced stop codon in the gene or targeted knockout of the gene result
CC is similar phenotypes (PubMed:20548961). Mutant mice are normal at
CC birth, but by postnatal day 7 appear smaller (PubMed:20548961). They
CC display generalized hypotrichosis and hair loss with altered skin that
CC is loose with wrinkling and folding (PubMed:20548961). Kyphosis and
CC osteoporosisis are also observed (PubMed:20548961). Finally, a
CC generalized amyloid deposition results in early death
CC (PubMed:20548961). {ECO:0000269|PubMed:20548961}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC AKR/ZDHHC17 subfamily. {ECO:0000305}.
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DR EMBL; AK010382; BAB26899.2; -; mRNA.
DR EMBL; AK145855; BAE26700.1; -; mRNA.
DR EMBL; AK146196; BAE26970.1; -; mRNA.
DR EMBL; BC046599; AAH46599.1; -; mRNA.
DR CCDS; CCDS52259.1; -.
DR RefSeq; NP_082307.1; NM_028031.3.
DR AlphaFoldDB; Q9CWU2; -.
DR SMR; Q9CWU2; -.
DR BioGRID; 232597; 4.
DR IntAct; Q9CWU2; 3.
DR STRING; 10090.ENSMUSP00000112498; -.
DR iPTMnet; Q9CWU2; -.
DR PhosphoSitePlus; Q9CWU2; -.
DR SwissPalm; Q9CWU2; -.
DR EPD; Q9CWU2; -.
DR MaxQB; Q9CWU2; -.
DR PaxDb; Q9CWU2; -.
DR PeptideAtlas; Q9CWU2; -.
DR PRIDE; Q9CWU2; -.
DR ProteomicsDB; 298513; -.
DR Antibodypedia; 6224; 173 antibodies from 35 providers.
DR DNASU; 243983; -.
DR Ensembl; ENSMUST00000118927; ENSMUSP00000112498; ENSMUSG00000030471.
DR GeneID; 243983; -.
DR KEGG; mmu:243983; -.
DR UCSC; uc009haw.1; mouse.
DR CTD; 54503; -.
DR MGI; MGI:1919227; Zdhhc13.
DR VEuPathDB; HostDB:ENSMUSG00000030471; -.
DR eggNOG; KOG0509; Eukaryota.
DR GeneTree; ENSGT00530000063074; -.
DR HOGENOM; CLU_012510_3_1_1; -.
DR InParanoid; Q9CWU2; -.
DR OMA; DVPDCNG; -.
DR OrthoDB; 445686at2759; -.
DR PhylomeDB; Q9CWU2; -.
DR TreeFam; TF317342; -.
DR BioGRID-ORCS; 243983; 3 hits in 73 CRISPR screens.
DR PRO; PR:Q9CWU2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9CWU2; protein.
DR Bgee; ENSMUSG00000030471; Expressed in placenta labyrinth and 239 other tissues.
DR ExpressionAtlas; Q9CWU2; baseline and differential.
DR Genevisible; Q9CWU2; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR GO; GO:0030660; C:Golgi-associated vesicle membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0016409; F:palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0018345; P:protein palmitoylation; IBA:GO_Central.
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; IPR030290; ZDHHC13.
DR PANTHER; PTHR24161:SF16; PTHR24161:SF16; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF01529; DHHC; 1.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50216; DHHC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; ANK repeat; Cytoplasmic vesicle;
KW Golgi apparatus; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Repeat; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..622
FT /note="Palmitoyltransferase ZDHHC13"
FT /id="PRO_0000212889"
FT TOPO_DOM 1..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..320
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..371
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..518
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 43..78
FT /note="ANK 1"
FT /evidence="ECO:0000250|UniProtKB:Q8IUH5"
FT REPEAT 81..110
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 115..144
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 148..177
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 181..211
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 216..245
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT REPEAT 249..277
FT /note="ANK 7"
FT /evidence="ECO:0000255"
FT DOMAIN 426..476
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 456
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8IUH4"
FT CONFLICT 110
FT /note="Q -> L (in Ref. 1; BAE26700)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 70890 MW; C34EB8AB76899E72 CRC64;
MEGPGLGSQC RNHSHGSHVP GFGRHGICVH ENKELAKAKE ILPLIEDSSN CDIVKATQYG
IFERCKELVE AGYDVRQPDR ENVSLLHWAA INNRLELVKF YISKGAVIDQ LGGDLNSTPL
HWAIRQGHLP MVILLLQHGA DPTLIDGEGF SSIHLAVLFQ HMPIIAYLIS KGQSVNMTDV
NGQTPLMLSA YKVIGPEPTG FLLKFNPSLS VVDKTHQNTP LHWAVAAGNV SAVDKLLEAG
SSLDIRNAKG ETPLDMALQS KNQLISHMLR TEAKMRANKQ FRLWRWLHKC ELFLLLILSM
ITLWAVGYIL DFNSDSWLLK GCLLVALFFL TSLFPRFLVG YKNLVYLPTV FLLSSIFWIF
MTWFILFFPD TAGSPLYFAF IFSIMAFLYF FYKTWATDPG FTKASEEERK VNIVTLAETG
SLDFRTFCTS CLIRKPLRSL HCHVCNSCVA RFDQHCFWTG RCIGFGNHHH YIFFLLSLSM
VCDWIIYGSF VYWSNHCATT FKEDGLWTYL NQIVACSPWV LYIFMLAAFH FSWSTFLLIN
QLFQIAFLGL TSHERISLLK QSRHMKQTLS LRKTPYNLGF TQNLADFFQC GCFGLVKPCI
IDWTSQYTMV FHPAKEKVLR SV
