ZDHC2_RAT
ID ZDHC2_RAT Reviewed; 366 AA.
AC Q9JKR5; A0P8F1;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Palmitoyltransferase ZDHHC2 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q9UIJ5};
DE AltName: Full=Acyltransferase ZDHHC2 {ECO:0000250|UniProtKB:P59267};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:P59267};
DE AltName: Full=Zinc finger DHHC domain-containing protein 2 {ECO:0000312|RGD:628681};
DE Short=DHHC-2;
GN Name=Zdhhc2 {ECO:0000312|RGD:628681};
GN Synonyms=Srec {ECO:0000312|EMBL:AAF43032.1};
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].
RC TISSUE=Pituitary;
RA Kullmann S., Esche H., Brockmann D.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang R., Tian Q., Okano A., Suzuki T.;
RT "Rattus norvegicus dhhc2 mRNA.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19596852; DOI=10.1083/jcb.200903101;
RA Noritake J., Fukata Y., Iwanaga T., Hosomi N., Tsutsumi R., Matsuda N.,
RA Tani H., Iwanari H., Mochizuki Y., Kodama T., Matsuura Y., Bredt D.S.,
RA Hamakubo T., Fukata M.;
RT "Mobile DHHC palmitoylating enzyme mediates activity-sensitive synaptic
RT targeting of PSD-95.";
RL J. Cell Biol. 186:147-160(2009).
RN [4]
RP FUNCTION.
RX PubMed=21343290; DOI=10.1074/jbc.m110.193763;
RA Jia L., Linder M.E., Blumer K.J.;
RT "Gi/o signaling and the palmitoyltransferase DHHC2 regulate palmitate
RT cycling and shuttling of RGS7 family-binding protein.";
RL J. Biol. Chem. 286:13695-13703(2011).
RN [5]
RP FUNCTION.
RX PubMed=25589740; DOI=10.1523/jneurosci.2243-14.2015;
RA Woolfrey K.M., Sanderson J.L., Dell'Acqua M.L.;
RT "The palmitoyl acyltransferase DHHC2 regulates recycling endosome
RT exocytosis and synaptic potentiation through palmitoylation of
RT AKAP79/150.";
RL J. Neurosci. 35:442-456(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 (PubMed:19596852, PubMed:21343290, PubMed:25589740).
CC Has no stringent fatty acid selectivity and in addition to palmitate
CC can also transfer onto target proteins myristate from tetradecanoyl-CoA
CC and stearate from octadecanoyl-CoA (By similarity). In the nervous
CC system, plays a role in long term synaptic potentiation by
CC palmitoylating AKAP5 through which it regulates protein trafficking
CC from the dendritic recycling endosomes to the plasma membrane and
CC controls both structural and functional plasticity at excitatory
CC synapses (PubMed:25589740). In dendrites, mediates the palmitoylation
CC of DLG4 when synaptic activity decreases and induces synaptic
CC clustering of DLG4 and associated AMPA-type glutamate receptors
CC (PubMed:19596852). Also mediates the de novo and turnover
CC palmitoylation of RGS7BP, a shuttle for Gi/o-specific GTPase-activating
CC proteins/GAPs, promoting its localization to the plasma membrane in
CC response to the activation of G protein-coupled receptors. Through the
CC localization of these GTPase-activating proteins/GAPs, it also probably
CC plays a role in G protein-coupled receptors signaling in neurons
CC (PubMed:21343290). Also probably plays a role in cell adhesion by
CC palmitoylating CD9 and CD151 to regulate their expression and function.
CC Palmitoylates the endoplasmic reticulum protein CKAP4 and regulates its
CC localization to the plasma membrane. Could also palmitoylate LCK and
CC regulate its localization to the plasma membrane (By similarity).
CC {ECO:0000250|UniProtKB:P59267, ECO:0000250|UniProtKB:Q9UIJ5,
CC ECO:0000269|PubMed:19596852, ECO:0000269|PubMed:21343290,
CC ECO:0000269|PubMed:25589740}.
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:Q9UIJ5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q9UIJ5};
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:P59267};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59737;
CC Evidence={ECO:0000250|UniProtKB:P59267};
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:P59267};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741;
CC Evidence={ECO:0000250|UniProtKB:P59267};
CC -!- SUBUNIT: Monomer. Homodimer. The monomeric form has a higher catalytic
CC activity. {ECO:0000250|UniProtKB:Q9UIJ5}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic density
CC {ECO:0000269|PubMed:19596852}. Postsynaptic recycling endosome membrane
CC {ECO:0000250|UniProtKB:P59267}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9UIJ5}; Multi-pass
CC membrane protein {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9UIJ5}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9UIJ5};
CC Multi-pass membrane protein {ECO:0000255}. Note=Translocates to
CC postsynaptic density when synaptic activity decreases.
CC {ECO:0000269|PubMed:19596852}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- PTM: Autopalmitoylated. {ECO:0000250|UniProtKB:Q9UIJ5}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF228917; AAF43032.1; -; mRNA.
DR EMBL; AB217870; BAF37828.1; -; mRNA.
DR RefSeq; NP_659564.2; NM_145096.2.
DR AlphaFoldDB; Q9JKR5; -.
DR SMR; Q9JKR5; -.
DR STRING; 10116.ENSRNOP00000033473; -.
DR iPTMnet; Q9JKR5; -.
DR PhosphoSitePlus; Q9JKR5; -.
DR PaxDb; Q9JKR5; -.
DR PRIDE; Q9JKR5; -.
DR Ensembl; ENSRNOT00000119635; ENSRNOP00000084203; ENSRNOG00000022686.
DR GeneID; 246326; -.
DR KEGG; rno:246326; -.
DR CTD; 51201; -.
DR RGD; 628681; Zdhhc2.
DR eggNOG; KOG1315; Eukaryota.
DR GeneTree; ENSGT00940000153716; -.
DR HOGENOM; CLU_027721_1_3_1; -.
DR InParanoid; Q9JKR5; -.
DR OMA; DFPTRSD; -.
DR PhylomeDB; Q9JKR5; -.
DR PRO; PR:Q9JKR5; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000022686; Expressed in cerebellum and 20 other tissues.
DR Genevisible; Q9JKR5; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0098837; C:postsynaptic recycling endosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISO:RGD.
DR GO; GO:0016409; F:palmitoyltransferase activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0019705; F:protein-cysteine S-myristoyltransferase activity; IEA:RHEA.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; ISO:RGD.
DR GO; GO:0140439; F:protein-cysteine S-stearoyltransferase activity; IEA:RHEA.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IMP:UniProtKB.
DR GO; GO:1904719; P:positive regulation of AMPA glutamate receptor clustering; IMP:UniProtKB.
DR GO; GO:1905751; P:positive regulation of endosome to plasma membrane protein transport; IMP:UniProtKB.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:1903539; P:protein localization to postsynaptic membrane; IMP:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; ISO:RGD.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:UniProtKB.
DR GO; GO:0042176; P:regulation of protein catabolic process; ISS:UniProtKB.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0016188; P:synaptic vesicle maturation; IBA:GO_Central.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Cell membrane; Endoplasmic reticulum; Endosome;
KW Golgi apparatus; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Synapse; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..366
FT /note="Palmitoyltransferase ZDHHC2"
FT /id="PRO_0000212861"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..47
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..207
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 126..176
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 297..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..366
FT /note="Mediates localization to plasma membrane and
FT recycling endosomes"
FT /evidence="ECO:0000250|UniProtKB:P59267"
FT MOTIF 334..335
FT /note="Non-canonical dileucine endocytic signal"
FT /evidence="ECO:0000250|UniProtKB:P59267"
FT MOTIF 357..360
FT /note="NPxY-like endocytic signal"
FT /evidence="ECO:0000250|UniProtKB:P59267"
FT COMPBIAS 297..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 156
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
SQ SEQUENCE 366 AA; 42086 MW; 3D689A3045D52D18 CRC64;
MAPSGPGGVR RRCRRVLYWI PVVFISLLLG WSYYAYAIQL CIVSMENIGE QVVCLMAYHL
LFAMFVWSYW KTIFTLPMNP SKEFHLSYAE KELLEREPRG EAHQEVLRRA AKDLPIYTRT
MSGAIRYCDR CRLIKPDRCH HCSVCDKCIL KMDHHCPWVN NCVGFSNYKF FLLFLAYSLL
YCLFIAATDL QYFIRFWTNG LPDTQAKFHI MFLFFAAAMF SVSLSSLFGY HCWLVSKNKS
TLEAFRNPVF RHGTDKNGFS LGFSKNMRQV FGDEKKYWLL PIFSSQGDGC SFPTCLVNQD
PEQPSTPAGL NSTAKNPENH QFPAKPLRES QSHLLTDSQT WTENSSNSGR CKAGMSNPAL
TMENET
