ZDHC9_BOVIN
ID ZDHC9_BOVIN Reviewed; 363 AA.
AC Q58DA8; Q2KJI5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
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;
GN Name=ZDHHC9;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) 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; BT021689; AAX46536.1; -; mRNA.
DR EMBL; BC105325; AAI05326.1; -; mRNA.
DR RefSeq; NP_001029733.2; NM_001034561.2.
DR RefSeq; XP_005227547.1; XM_005227490.2.
DR RefSeq; XP_005227548.1; XM_005227491.2.
DR AlphaFoldDB; Q58DA8; -.
DR SMR; Q58DA8; -.
DR STRING; 9913.ENSBTAP00000020418; -.
DR PaxDb; Q58DA8; -.
DR Ensembl; ENSBTAT00000020418; ENSBTAP00000020418; ENSBTAG00000015354.
DR Ensembl; ENSBTAT00000048680; ENSBTAP00000045675; ENSBTAG00000015354.
DR Ensembl; ENSBTAT00000075844; ENSBTAP00000057864; ENSBTAG00000015354.
DR GeneID; 527885; -.
DR KEGG; bta:527885; -.
DR CTD; 51114; -.
DR VEuPathDB; HostDB:ENSBTAG00000015354; -.
DR VGNC; VGNC:37146; ZDHHC9.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000159999; -.
DR HOGENOM; CLU_018741_3_1_1; -.
DR InParanoid; Q58DA8; -.
DR OMA; PLVYQRW; -.
DR OrthoDB; 1264614at2759; -.
DR TreeFam; TF312923; -.
DR Reactome; R-BTA-9648002; RAS processing.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000015354; Expressed in floor plate of diencephalon and 101 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0043849; F:Ras palmitoyltransferase activity; ISS:CAFA.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:CAFA.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
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..363
FT /note="Palmitoyltransferase ZDHHC9"
FT /id="PRO_0000212879"
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..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 139..189
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 303..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
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"
FT CONFLICT 281
FT /note="K -> E (in Ref. 2; AAI05326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 40826 MW; 6A6651A7F8813322 CRC64;
MSVMVVRKKV TRKWEKLPGR NTFCCDGRVM MARQKGIFYL TLFLILGTCT LFFAFECRYL
AVQLSPAIPV FAAMLFLFSM ATLLRTSFSD PGVIPRALPD EAAFIEMEIE ATNGAVPQGQ
RPPPRIKNFQ INNQIVKLKY CYTCKIFRPP RASHCSICDN CVERFDHHCP WVGNCVGKRN
YRYFYLFILS LSLLTIYVFA FNIVYVALKS LKIGFLETLK ETPGTVLEVL ICFFTLWSVV
GLTGFHTFLV ALNQTTNEDI KGSWTGKNRV QNPYSHGNIV KNCCEVLCGP LPPSVLDRRG
ILPLEESGSR PPSTQEASTS LLPQGPAPID HLSNEMPEDT STPEEMPPPE PPEPPQEVTE
AEK
