ZDHC9_PONAB
ID ZDHC9_PONAB Reviewed; 364 AA.
AC Q5R5J8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Palmitoyltransferase ZDHHC9;
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q9Y397};
DE AltName: Full=Zinc finger DHHC domain-containing protein 9;
DE Short=DHHC-9;
DE Short=DHHC9;
GN Name=ZDHHC9;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Palmitoyltransferase that could catalyze the addition of
CC palmitate onto various protein substrates. The ZDHHC9-GOLGA7 complex is
CC a palmitoyltransferase specific for HRAS and NRAS. May have a
CC palmitoyltransferase activity toward the beta-2 adrenergic
CC receptor/ADRB2 and therefore regulate G protein-coupled receptor
CC signaling. {ECO:0000250|UniProtKB:Q9Y397}.
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:Q9Y397};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q9Y397};
CC -!- SUBUNIT: Interacts with GOLGA7. {ECO:0000250|UniProtKB:Q9Y397}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Y397}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Y397};
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; CR860860; CAH92968.1; -; mRNA.
DR RefSeq; NP_001126752.1; NM_001133280.1.
DR AlphaFoldDB; Q5R5J8; -.
DR SMR; Q5R5J8; -.
DR STRING; 9601.ENSPPYP00000023183; -.
DR GeneID; 100173754; -.
DR KEGG; pon:100173754; -.
DR CTD; 51114; -.
DR eggNOG; KOG1311; Eukaryota.
DR InParanoid; Q5R5J8; -.
DR OrthoDB; 1264614at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:CAFA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031228; C:intrinsic component of Golgi membrane; ISS:CAFA.
DR GO; GO:0002178; C:palmitoyltransferase complex; ISS:CAFA.
DR GO; GO:0043849; F:Ras palmitoyltransferase activity; ISS:CAFA.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:CAFA.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR030292; ZDHHC9.
DR PANTHER; PTHR22883:SF71; PTHR22883:SF71; 1.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Endoplasmic reticulum; Golgi apparatus; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..364
FT /note="Palmitoyltransferase ZDHHC9"
FT /id="PRO_0000212882"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..63
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..183
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..228
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 139..189
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 303..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 169
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9Y397"
SQ SEQUENCE 364 AA; 40826 MW; 7C92BDAC373A7C96 CRC64;
MSVMVVRKKV TRKWEKLPGR NTFCCDGRVM MARQKGIFYL TLFLILGTCT LFFAFECRYL
AVQQSPAIPV FAAMLFLFSM ATLLRASFSD PGVIPRALPD EAAFIEMEIE ATNGAVPQGQ
RPPPRIKNSQ INNQIVKLKY CYTCKIFRPP RASHCSICDN CVERFDHHCP WVGNCVGKRN
YRYFYLFILS LSLLTIYVFA FNIVYVALKS LKIGFLETLK ETPGTVLEVL ICFFTLWSVV
GLTGFHTFLV ALNQTTNEDI KGSWTGKNRV QNPYSHGNIV KNCCEVLCGP LPPSVLDRRG
ILPLEESGSR PPSTQETSSS LLPQSPAPTE HLNSNEMPDD SSTPEEMPPP EPPEPPQEAA
EAEK
