ZDH22_HUMAN
ID ZDH22_HUMAN Reviewed; 263 AA.
AC Q8N966; A6NH02; B7Z2L5; Q149P4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Palmitoyltransferase ZDHHC22 {ECO:0000305|PubMed:22399288};
DE EC=2.3.1.225 {ECO:0000269|PubMed:22399288};
DE AltName: Full=Zinc finger DHHC domain-containing protein 22 {ECO:0000312|HGNC:HGNC:20106};
DE Short=DHHC-22;
DE Short=zDHHC22;
GN Name=ZDHHC22 {ECO:0000312|HGNC:HGNC:20106}; Synonyms=C14orf59;
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].
RC TISSUE=Brain;
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].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16647879; DOI=10.1016/j.bbalip.2006.03.010;
RA Ohno Y., Kihara A., Sano T., Igarashi Y.;
RT "Intracellular localization and tissue-specific distribution of human and
RT yeast DHHC cysteine-rich domain-containing proteins.";
RL Biochim. Biophys. Acta 1761:474-483(2006).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22399288; DOI=10.1074/jbc.m111.335547;
RA Tian L., McClafferty H., Knaus H.G., Ruth P., Shipston M.J.;
RT "Distinct acyl protein transferases and thioesterases control surface
RT expression of calcium-activated potassium channels.";
RL J. Biol. Chem. 287:14718-14725(2012).
CC -!- FUNCTION: Palmitoyltransferase that could catalyze the addition of
CC palmitate onto various protein substrates and be involved in a variety
CC of cellular processes (PubMed:22399288). Catalyzes the palmitoylation
CC of KCNMA1, regulating localization of KCNMA1 to the plasma membrane
CC (PubMed:22399288). Might also mediate palmitoylation of CNN3 (By
CC similarity). {ECO:0000250|UniProtKB:A0PK84,
CC ECO:0000269|PubMed:22399288}.
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:22399288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000305|PubMed:22399288};
CC -!- SUBUNIT: Interacts with CNN3. {ECO:0000250|UniProtKB:A0PK84}.
CC -!- INTERACTION:
CC Q8N966; P11912: CD79A; NbExp=3; IntAct=EBI-10268111, EBI-7797864;
CC Q8N966; Q8WXI8: CLEC4D; NbExp=3; IntAct=EBI-10268111, EBI-12703404;
CC Q8N966; Q9BQT9: CLSTN3; NbExp=3; IntAct=EBI-10268111, EBI-11291074;
CC Q8N966; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-10268111, EBI-6942903;
CC Q8N966; Q96LA5-2: FCRL2; NbExp=3; IntAct=EBI-10268111, EBI-17263163;
CC Q8N966; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-10268111, EBI-12142257;
CC Q8N966; Q8TED1: GPX8; NbExp=3; IntAct=EBI-10268111, EBI-11721746;
CC Q8N966; O15165-2: LDLRAD4; NbExp=3; IntAct=EBI-10268111, EBI-13302279;
CC Q8N966; P15151: PVR; NbExp=3; IntAct=EBI-10268111, EBI-3919694;
CC Q8N966; Q9NS64: RPRM; NbExp=3; IntAct=EBI-10268111, EBI-1052363;
CC Q8N966; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-10268111, EBI-8638294;
CC Q8N966; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-10268111, EBI-2548832;
CC Q8N966; Q6PEY1: TMEM88; NbExp=3; IntAct=EBI-10268111, EBI-17198826;
CC Q8N966; Q8IWR1: TRIM59; NbExp=8; IntAct=EBI-10268111, EBI-10262539;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16647879}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:16647879};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16647879}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AK095612; BAC04590.1; -; mRNA.
DR EMBL; AK294840; BAH11901.1; -; mRNA.
DR EMBL; AC007375; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117676; AAI17677.1; -; mRNA.
DR CCDS; CCDS45140.1; -.
DR RefSeq; NP_777636.2; NM_174976.2.
DR RefSeq; XP_006720182.1; XM_006720119.3.
DR RefSeq; XP_011534963.1; XM_011536661.2.
DR AlphaFoldDB; Q8N966; -.
DR BioGRID; 129607; 19.
DR IntAct; Q8N966; 14.
DR STRING; 9606.ENSP00000318222; -.
DR BioMuta; ZDHHC22; -.
DR DMDM; 126302620; -.
DR MassIVE; Q8N966; -.
DR PaxDb; Q8N966; -.
DR PeptideAtlas; Q8N966; -.
DR PRIDE; Q8N966; -.
DR ProteomicsDB; 72495; -.
DR Antibodypedia; 70659; 28 antibodies from 12 providers.
DR DNASU; 283576; -.
DR Ensembl; ENST00000319374.4; ENSP00000318222.4; ENSG00000177108.5.
DR GeneID; 283576; -.
DR KEGG; hsa:283576; -.
DR MANE-Select; ENST00000319374.4; ENSP00000318222.4; NM_174976.2; NP_777636.2.
DR UCSC; uc010asp.3; human.
DR CTD; 283576; -.
DR GeneCards; ZDHHC22; -.
DR HGNC; HGNC:20106; ZDHHC22.
DR HPA; ENSG00000177108; Tissue enriched (brain).
DR neXtProt; NX_Q8N966; -.
DR OpenTargets; ENSG00000177108; -.
DR PharmGKB; PA134952477; -.
DR VEuPathDB; HostDB:ENSG00000177108; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00730000111268; -.
DR HOGENOM; CLU_027721_5_3_1; -.
DR InParanoid; Q8N966; -.
DR OMA; HFCFFIP; -.
DR OrthoDB; 1402394at2759; -.
DR PhylomeDB; Q8N966; -.
DR TreeFam; TF342115; -.
DR PathwayCommons; Q8N966; -.
DR SignaLink; Q8N966; -.
DR BioGRID-ORCS; 283576; 20 hits in 1066 CRISPR screens.
DR ChiTaRS; ZDHHC22; human.
DR GenomeRNAi; 283576; -.
DR Pharos; Q8N966; Tdark.
DR PRO; PR:Q8N966; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q8N966; protein.
DR Bgee; ENSG00000177108; Expressed in lateral nuclear group of thalamus and 93 other tissues.
DR ExpressionAtlas; Q8N966; baseline and differential.
DR Genevisible; Q8N966; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IBA:GO_Central.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; IMP:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR000731; SSD.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
DR PROSITE; PS50156; SSD; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Golgi apparatus; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..263
FT /note="Palmitoyltransferase ZDHHC22"
FT /id="PRO_0000212911"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..48
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..263
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 92..131
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 111
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT CONFLICT 137..160
FT /note="CLYSMVAGVAYISAVLSISFAHPL -> QELTRGLRKEVAAGPAGPHVQCRK
FT (in Ref. 1; BAC04590)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 29100 MW; 702A71D90A6F4C94 CRC64;
MLALRLLNVV APAYFLCISL VTFVLQLFLF LPSMREDPAA ARLFSPALLH GALFLFLSAN
ALGNYVLVIQ NSPDDLGACQ GASARKTPCP SPSTHFCRVC ARVTLRHDHH CFFTGNCIGS
RNMRNFVLFC LYTSLACLYS MVAGVAYISA VLSISFAHPL AFLTLLPTSI SQFFSGAVLG
SEMFVILMLY LWFAIGLACA GFCCHQLLLI LRGQTRHQVR KGVAVRARPW RKNLQEVFGK
RWLLGLLVPM FNVGSESSKQ QDK
