ZDH22_MOUSE
ID ZDH22_MOUSE Reviewed; 263 AA.
AC A0PK84;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Palmitoyltransferase ZDHHC22 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q8N966};
DE AltName: Full=Zinc finger DHHC domain-containing protein 22 {ECO:0000312|MGI:MGI:2685108};
DE Short=DHHC-22;
DE Short=zDHHC22;
GN Name=Zdhhc22 {ECO:0000312|MGI:MGI:2685108}; Synonyms=Gm262;
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].
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 [2]
RP FUNCTION, AND INTERACTION WITH CCN3.
RX PubMed=29287726; DOI=10.1016/j.bbrc.2017.12.128;
RA Kim Y., Yang H., Min J.K., Park Y.J., Jeong S.H., Jang S.W., Shim S.;
RT "CCN3 secretion is regulated by palmitoylation via ZDHHC22.";
RL Biochem. Biophys. Res. Commun. 495:2573-2578(2018).
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 (By similarity). Catalyzes the palmitoylation of
CC KCNMA1, regulating localization of KCNMA1 to the plasma membrane (By
CC similarity). Might also mediate palmitoylation of CNN3 (Probable).
CC {ECO:0000250|UniProtKB:Q8N966, ECO:0000305|PubMed:29287726}.
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:Q8N966};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q8N966};
CC -!- SUBUNIT: Interacts with CNN3. {ECO:0000269|PubMed:29287726}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8N966}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8N966};
CC Multi-pass membrane protein {ECO:0000255}.
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; BC128021; AAI28022.1; -; mRNA.
DR CCDS; CCDS36500.1; -.
DR RefSeq; NP_001074412.1; NM_001080943.2.
DR RefSeq; XP_006515914.1; XM_006515851.2.
DR RefSeq; XP_006515915.1; XM_006515852.3.
DR AlphaFoldDB; A0PK84; -.
DR STRING; 10090.ENSMUSP00000093177; -.
DR PaxDb; A0PK84; -.
DR PRIDE; A0PK84; -.
DR ProteomicsDB; 275341; -.
DR Antibodypedia; 70659; 28 antibodies from 12 providers.
DR Ensembl; ENSMUST00000095521; ENSMUSP00000093177; ENSMUSG00000048483.
DR Ensembl; ENSMUST00000222543; ENSMUSP00000152660; ENSMUSG00000048483.
DR GeneID; 238331; -.
DR KEGG; mmu:238331; -.
DR UCSC; uc007oie.1; mouse.
DR CTD; 283576; -.
DR MGI; MGI:2685108; Zdhhc22.
DR VEuPathDB; HostDB:ENSMUSG00000048483; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00730000111268; -.
DR HOGENOM; CLU_027721_5_3_1; -.
DR InParanoid; A0PK84; -.
DR OMA; HFCFFIP; -.
DR OrthoDB; 1402394at2759; -.
DR PhylomeDB; A0PK84; -.
DR TreeFam; TF342115; -.
DR BioGRID-ORCS; 238331; 3 hits in 70 CRISPR screens.
DR PRO; PR:A0PK84; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; A0PK84; protein.
DR Bgee; ENSMUSG00000048483; Expressed in medial dorsal nucleus of thalamus and 62 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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; ISO:MGI.
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:MGI.
DR GO; GO:0018345; P:protein palmitoylation; IMP:MGI.
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_0000278772"
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 91..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"
SQ SEQUENCE 263 AA; 29318 MW; 32DA19CA24F9D60F CRC64;
MLALRLLNVV APAYFLCISL VTFVLQLFLF LPSMREDPTA TPLFSPAVLH GALFLFLSAN
ALGNYVLVIQ NSPDDLGTCQ GTMSQRPQCP PPSTHFCRVC SRVTLRHDHH CFFTGNCIGS
RNMRNFILFC LYTSLACLYS MVAGVAYISA VLSISFAHPL AFLTLLPTSI SQFFSGAVLG
SDMFVILMLY LWFAVGLACA GFCCHQLLLI LRGQTRYQVR KGMAVRARPW RKNLQEVFGK
RWLLGLLVPM FNVGTESSKQ QDK
