ZDHC8_CANLF
ID ZDHC8_CANLF Reviewed; 765 AA.
AC Q2THW8;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Palmitoyltransferase ZDHHC8 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q9ULC8};
DE AltName: Full=Zinc finger DHHC domain-containing protein 8 {ECO:0000250|UniProtKB:Q9ULC8};
DE Short=DHHC-8 {ECO:0000250|UniProtKB:Q9ULC8};
GN Name=ZDHHC8 {ECO:0000250|UniProtKB:Q9ULC8};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chen Y., Huang C.-H.;
RT "A superfamily of membrane-associated DHHC type zinc finger proteins.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate
CC onto various protein substrates and therefore functions in several
CC unrelated biological processes. Through the palmitoylation of ABCA1
CC regulates the localization of the transporter to the plasma membrane
CC and thereby regulates its function in cholesterol and phospholipid
CC efflux (By similarity). Could also pamitoylate the D(2) dopamine
CC receptor DRD2 and regulate its stability and localization to the plasma
CC membrane (By similarity). Could also play a role in glutamatergic
CC transmission (By similarity). {ECO:0000250|UniProtKB:Q5Y5T5,
CC ECO:0000250|UniProtKB:Q9ULC8}.
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:Q9ULC8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q9ULC8};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9ULC8}; Multi-pass membrane protein
CC {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q5Y5T5};
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 ERF2/ZDHHC9 subfamily. {ECO:0000305}.
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DR EMBL; AY871202; AAX68535.1; -; mRNA.
DR RefSeq; NP_001104240.1; NM_001110770.1.
DR AlphaFoldDB; Q2THW8; -.
DR SMR; Q2THW8; -.
DR STRING; 9612.ENSCAFP00000038379; -.
DR PaxDb; Q2THW8; -.
DR GeneID; 486415; -.
DR KEGG; cfa:486415; -.
DR CTD; 29801; -.
DR eggNOG; KOG1311; Eukaryota.
DR InParanoid; Q2THW8; -.
DR OrthoDB; 1264614at2759; -.
DR Proteomes; UP000002254; Unplaced.
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:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:UniProtKB.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISS:UniProtKB.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR030291; ZDHHC8.
DR PANTHER; PTHR12349:SF1; PTHR12349:SF1; 1.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Golgi apparatus; Lipoprotein; Membrane; Methylation;
KW Mitochondrion; Palmitate; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..765
FT /note="Palmitoyltransferase ZDHHC8"
FT /id="PRO_0000269229"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..52
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..190
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..765
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 104..154
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 290..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..534
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 134
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5Y5T5"
FT MOD_RES 441
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5Y5T5"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULC8"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5Y5T5"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULC8"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULC8"
FT MOD_RES 725
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULC8"
FT MOD_RES 743
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULC8"
SQ SEQUENCE 765 AA; 81292 MW; 2C6168E85C47DAAE CRC64;
MPRSPGTRLK PAKYIPVATA AALLVGSSTL FFVFTCPWLT RAVSPAVPVY NGIIFLFVLA
NFSMATFMDP GVFPRADEDE DKEDDFRAPL YKNVDVRGIQ VRMKWCATCH FYRPPRCSHC
SVCDNCVEDF DHHCPWVNNC IGRRNYRYFF LFLLSLSAHM VGVVAFGLVY VLNHAEGLGA
AHTTITMAVM CVAGLFFIPV IGLTGFHVVL VTRGRTTNEH VTGKFRGGVN PFTRGCYGNV
EHVLCSPLAP RYVVEPPRLP LAARLKPPFL RPELLERAAP LKVKLSDNGL KAGLGRSKSK
GSLDRLDEKP LDLGPPLPPK AEAGTFGGDL QTPRPSSAES ALSAQRTSPP TPAMYKFRPA
FPSGPKAPFC GPGEQVPGPD SLTLGEDSIH SLDFASEPSL DLPDYTPGGL HAAYPPSPPL
SAADTFSGAL RSLSLKAAGR RGGDHVALQP LRSEGGPPTP HRGIFAPHAL PNRNGSLSYD
SLLNPGSPGG HTCPAHPSAG VASYRSPYLH PGAVGEPPRP PPRSFSPVLG PRPREPSPVR
YDNLSRTIMA SIQERKDREE RERLLRSQAD SLFGDSGVYD APSSYSLQQA SALADGARGP
ALRYGSRDDL VAGPGFGGAR NPALQTSVSS LSSAVSRAPR TSSSSLQADL ANNNAPGPRP
GSGSHRSPVR QGPPSPPSTP RSPSYAGPKA VAFIHTDLPE SPPSLAVQRD HPQLKTPPSK
LNGQSPGLAR LGPAAGPPGP SASPARHTLV KKVSGVGGTT YEISV
