ZDHC8_PANTR
ID ZDHC8_PANTR Reviewed; 765 AA.
AC Q2THX0;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 81.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
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; AY871200; AAX68533.1; -; mRNA.
DR RefSeq; NP_001033745.1; NM_001038656.1.
DR AlphaFoldDB; Q2THX0; -.
DR SMR; Q2THX0; -.
DR STRING; 9598.ENSPTRP00000024252; -.
DR PaxDb; Q2THX0; -.
DR GeneID; 458662; -.
DR KEGG; ptr:458662; -.
DR CTD; 29801; -.
DR eggNOG; KOG1311; Eukaryota.
DR InParanoid; Q2THX0; -.
DR Proteomes; UP000002277; 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_0000232438"
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 293..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..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 622..669
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 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; 81549 MW; 55AD401838EE236B CRC64;
MPRSPGTRLK PAKYIPVATA AALLVGSSTL FFVFTCPWLT RAVSPAVPVY NGIIFLFVLA
NFSMATFMDP GVFPRADEDE DKEDDFRAPL YKNVDVRGIQ VRMKWCATCH FYRPPRCSHC
SVCDNCVEDF DHHCPWVNNC IGRRNYRYFF LFLLSLSAHM VGVVAFGLVY VLNHAEGLGA
AHTTITMAVM CVAGLFFIPV IGLTGFHVVL VTRGRTTNEQ VTGKFRGGVN PFTRGCCGNV
EHVLCSPLAP RYVVEPPRLP LAVSLKPPFL RPELLDRAAP LKVKLSDNGL KAGLGRSKSK
GSLDRLDEKP LDLGPPLPPK IEAGTFSSDL QTPRPGSAES ALSVQRTSPP TPAMYKFRPA
FPTGPKVPFC GPGEQVPGPD SLTLGDDSIR SLDFVSEPSL DLPDYGPGGL HAAYPPSPPL
SASDAFSGAL RSLSLKASSR RGGDHVALQP LRSEGGPPTP HRSIFAPHAL PNRNGSLSYD
SLLNPGSPGG HACPAHPAVG MAGYHSPYLH PGATGDPPRP LPRSFSPVLG PRPREPSPVR
YDNLSRTIMA SIQERKDREE RERLLRSQAD SLFGDSGVYD APSSYSLQQA SVLSEGPRGP
ALRYGSRDDL VAGPGFGGAR NPALQTSLSS LSSSVSRAPR TSSSSLQADQ ASSNAPGPRP
SSGSHRSPAR QGLPSPPGTP HLTILRGPQS CRLHPHGPPR ATALADRAED HPQLKTPPSK
LNGQSPGLAR LGLATGPPGP SASPTRHTLV KKVSGVGGTT YEISV
