ZDH13_HUMAN
ID ZDH13_HUMAN Reviewed; 622 AA.
AC Q8IUH4; Q7Z2D3; Q86VK2; Q9NV30; Q9NV99;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Palmitoyltransferase ZDHHC13 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q9CWU2};
DE AltName: Full=Huntingtin-interacting protein 14-related protein {ECO:0000303|PubMed:12393793};
DE Short=HIP14-related protein {ECO:0000303|PubMed:12393793};
DE AltName: Full=Huntingtin-interacting protein HIP3RP {ECO:0000312|EMBL:BAC22090.1};
DE AltName: Full=Putative MAPK-activating protein PM03 {ECO:0000312|EMBL:BAC77380.1};
DE AltName: Full=Putative NF-kappa-B-activating protein 209 {ECO:0000312|EMBL:BAC77367.1};
DE AltName: Full=Zinc finger DHHC domain-containing protein 13 {ECO:0000312|HGNC:HGNC:18413};
DE Short=DHHC-13 {ECO:0000250|UniProtKB:Q9CWU2};
GN Name=ZDHHC13 {ECO:0000312|HGNC:HGNC:18413};
GN Synonyms=HIP14L {ECO:0000303|PubMed:12393793},
GN HIP3RP {ECO:0000312|EMBL:BAC22090.1};
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 [MRNA] (ISOFORM 1), AND VARIANT ARG-99.
RX PubMed=12393793; DOI=10.1093/hmg/11.23.2815;
RA Singaraja R.R., Hadano S., Metzler M., Givan S., Wellington C.L., Warby S.,
RA Yanai A., Gutekunst C.-A., Leavitt B.R., Yi H., Fichter K., Gan L.,
RA McGutcheon K., Chopra V., Michel J., Hersch S.M., Ikeda J.E., Hayden M.R.;
RT "HIP14, a novel ankyrin domain-containing protein, links huntingtin to
RT intracellular trafficking and endocytosis.";
RL Hum. Mol. Genet. 11:2815-2828(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung fibroblast;
RX PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O., Nagano Y.,
RA Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H., Sugano S.;
RT "Large-scale identification and characterization of human genes that
RT activate NF-kappaB and MAPK signaling pathways.";
RL Oncogene 22:3307-3318(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ARG-99.
RC TISSUE=Placenta, 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP ARG-99.
RC TISSUE=Eye, 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP INTERACTION WITH CLIP3; HTT AND MAP6.
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 could catalyze the addition of
CC palmitate onto various protein substrates (By similarity).
CC Palmitoyltransferase for HTT and GAD2. May play a role in Mg(2+)
CC transport. {ECO:0000250|UniProtKB:Q9CWU2}.
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:Q9CWU2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q9CWU2};
CC -!- SUBUNIT: Interacts (via ANK repeats) with CLIP3 (PubMed:26198635).
CC Interacts (via ANK repeats) with DNAJC5 (via C-terminus) (By
CC similarity). Interacts (via ANK repeats) with HTT (PubMed:26198635).
CC Interacts (via ANK repeats) with MAP6 (PubMed:26198635). Interacts (via
CC ANK repeats) with SNAP23. Interacts (via ANK repeats) with SNAP25. May
CC interact (via ANK repeats) with SPRED2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9CWU2, ECO:0000269|PubMed:26198635}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9CWU2}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q9CWU2}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Low extracellular Mg(2+) induces increase in Golgi
CC and in post-Golgi vesicles. {ECO:0000250|UniProtKB:Q9CWU2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IUH4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IUH4-2; Sequence=VSP_010029;
CC Name=3;
CC IsoId=Q8IUH4-3; Sequence=VSP_010028;
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC AKR/ZDHHC17 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91856.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB024495; BAC22090.1; -; mRNA.
DR EMBL; AB097014; BAC77367.1; -; mRNA.
DR EMBL; AB097027; BAC77380.1; -; mRNA.
DR EMBL; AK001714; BAA91856.1; ALT_SEQ; mRNA.
DR EMBL; AK001831; BAA91930.1; -; mRNA.
DR EMBL; AC009652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050690; AAH50690.2; -; mRNA.
DR EMBL; BC036020; AAH36020.1; -; mRNA.
DR EMBL; BC056152; AAH56152.1; -; mRNA.
DR CCDS; CCDS44550.1; -. [Q8IUH4-1]
DR CCDS; CCDS44551.1; -. [Q8IUH4-3]
DR RefSeq; NP_001001483.1; NM_001001483.2. [Q8IUH4-3]
DR RefSeq; NP_061901.2; NM_019028.2. [Q8IUH4-1]
DR RefSeq; XP_005253053.1; XM_005252996.2. [Q8IUH4-3]
DR RefSeq; XP_011518497.1; XM_011520195.1. [Q8IUH4-3]
DR AlphaFoldDB; Q8IUH4; -.
DR SMR; Q8IUH4; -.
DR BioGRID; 119999; 70.
DR IntAct; Q8IUH4; 9.
DR MINT; Q8IUH4; -.
DR STRING; 9606.ENSP00000400113; -.
DR TCDB; 8.A.114.1.7; the huntington-interacting protein 14 (hip14) family.
DR iPTMnet; Q8IUH4; -.
DR PhosphoSitePlus; Q8IUH4; -.
DR SwissPalm; Q8IUH4; -.
DR BioMuta; ZDHHC13; -.
DR DMDM; 269849714; -.
DR EPD; Q8IUH4; -.
DR jPOST; Q8IUH4; -.
DR MassIVE; Q8IUH4; -.
DR MaxQB; Q8IUH4; -.
DR PaxDb; Q8IUH4; -.
DR PeptideAtlas; Q8IUH4; -.
DR PRIDE; Q8IUH4; -.
DR ProteomicsDB; 70569; -. [Q8IUH4-1]
DR ProteomicsDB; 70570; -. [Q8IUH4-2]
DR ProteomicsDB; 70571; -. [Q8IUH4-3]
DR Antibodypedia; 6224; 173 antibodies from 35 providers.
DR DNASU; 54503; -.
DR Ensembl; ENST00000399351.7; ENSP00000382288.3; ENSG00000177054.14. [Q8IUH4-3]
DR Ensembl; ENST00000446113.7; ENSP00000400113.2; ENSG00000177054.14. [Q8IUH4-1]
DR GeneID; 54503; -.
DR KEGG; hsa:54503; -.
DR MANE-Select; ENST00000446113.7; ENSP00000400113.2; NM_019028.3; NP_061901.2.
DR UCSC; uc001mpi.4; human. [Q8IUH4-1]
DR CTD; 54503; -.
DR DisGeNET; 54503; -.
DR GeneCards; ZDHHC13; -.
DR HGNC; HGNC:18413; ZDHHC13.
DR HPA; ENSG00000177054; Low tissue specificity.
DR MIM; 612815; gene.
DR neXtProt; NX_Q8IUH4; -.
DR OpenTargets; ENSG00000177054; -.
DR PharmGKB; PA134955878; -.
DR VEuPathDB; HostDB:ENSG00000177054; -.
DR eggNOG; KOG0509; Eukaryota.
DR GeneTree; ENSGT00530000063074; -.
DR HOGENOM; CLU_012510_3_1_1; -.
DR InParanoid; Q8IUH4; -.
DR OMA; DVPDCNG; -.
DR OrthoDB; 445686at2759; -.
DR PhylomeDB; Q8IUH4; -.
DR TreeFam; TF317342; -.
DR PathwayCommons; Q8IUH4; -.
DR SignaLink; Q8IUH4; -.
DR BioGRID-ORCS; 54503; 16 hits in 1088 CRISPR screens.
DR ChiTaRS; ZDHHC13; human.
DR GenomeRNAi; 54503; -.
DR Pharos; Q8IUH4; Tbio.
DR PRO; PR:Q8IUH4; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8IUH4; protein.
DR Bgee; ENSG00000177054; Expressed in buccal mucosa cell and 173 other tissues.
DR Genevisible; Q8IUH4; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0030660; C:Golgi-associated vesicle membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0016409; F:palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
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; 2.
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; Alternative splicing; ANK repeat;
KW Cytoplasmic vesicle; Golgi apparatus; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..622
FT /note="Palmitoyltransferase ZDHHC13"
FT /id="PRO_0000212887"
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..370
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..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:0007744|PubMed:22814378"
FT VAR_SEQ 1..176
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010029"
FT VAR_SEQ 1..130
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010028"
FT VARIANT 99
FT /note="K -> R (in dbSNP:rs2271001)"
FT /evidence="ECO:0000269|PubMed:12393793,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT /id="VAR_023835"
FT VARIANT 392
FT /note="Y -> C (in dbSNP:rs12798330)"
FT /id="VAR_057490"
FT CONFLICT 467
FT /note="N -> T (in Ref. 1; BAC22090)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="N -> D (in Ref. 3; BAA91856)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 70861 MW; FD366E02728A0358 CRC64;
MEGPGLGSQC RNHSHGPHPP GFGRYGICAH ENKELANARE ALPLIEDSSN CDIVKATQYG
IFERCKELVE AGYDVRQPDK ENVSLLHWAA INNRLDLVKF YISKGAVVDQ LGGDLNSTPL
HWAIRQGHLP MVILLLQHGA DPTLIDGEGF SSIHLAVLFQ HMPIIAYLIS KGQSVNMTDV
NGQTPLMLSA HKVIGPEPTG FLLKFNPSLN VVDKIHQNTP LHWAVAAGNV NAVDKLLEAG
SSLDIQNVKG ETPLDMALQN KNQLIIHMLK TEAKMRANQK FRLWRWLQKC ELFLLLMLSV
ITMWAIGYIL DFNSDSWLLK GCLLVTLFFL TSLFPRFLVG YKNLVYLPTA FLLSSVFWIF
MTWFILFFPD LAGAPFYFSF IFSIVAFLYF FYKTWATDPG FTKASEEEKK VNIITLAETG
SLDFRTFCTS CLIRKPLRSL HCHVCNCCVA RYDQHCLWTG RCIGFGNHHY YIFFLFFLSM
VCGWIIYGSF IYLSSHCATT FKEDGLWTYL NQIVACSPWV LYILMLATFH FSWSTFLLLN
QLFQIAFLGL TSHERISLQK QSKHMKQTLS LRKTPYNLGF MQNLADFFQC GCFGLVKPCV
VDWTSQYTMV FHPAREKVLR SV
