ZDH21_BOVIN
ID ZDH21_BOVIN Reviewed; 265 AA.
AC A2VDT6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Palmitoyltransferase ZDHHC21 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q8IVQ6};
DE AltName: Full=Zinc finger DHHC domain-containing protein 21 {ECO:0000250|UniProtKB:Q8IVQ6};
GN Name=ZDHHC21 {ECO:0000250|UniProtKB:Q8IVQ6};
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].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Palmitoyltransferase that catalyzes the addition of palmitate
CC onto various protein substrates (By similarity). Palmitoylates sex
CC steroid hormone receptors, including ESR1, PGR and AR, thereby
CC regulating their targeting to the plasma membrane. This affects rapid
CC intracellular signaling by sex hormones via ERK and AKT kinases and the
CC generation of cAMP, but does not affect that mediated by their nuclear
CC receptor (By similarity). Palmitoylates FYN, regulates its localization
CC in hair follicles and plays a key role in epidermal homeostasis and
CC hair follicle differentiation. Through the palmitoylation of PLCB1 and
CC the regulation of PLCB1 downstream signaling may indirectly regulate
CC the function of the endothelial barrier and the adhesion of leukocytes
CC to the endothelium. Has also a palmitoyltransferase activity toward
CC ADRA1D, positively regulating its activity and expression and may
CC thereby play a role in vascular contraction. May also palmitoylate eNOS
CC and LCK (By similarity). {ECO:0000250|UniProtKB:Q8IVQ6,
CC ECO:0000250|UniProtKB:Q9D270}.
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:Q9D270};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q9D270};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8IVQ6}; Multi-pass membrane protein
CC {ECO:0000255}. Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q9D270}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q8IVQ6}; Multi-pass
CC 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 {ECO:0000305}.
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DR EMBL; BC133395; AAI33396.1; -; mRNA.
DR RefSeq; NP_001075003.1; NM_001081534.1.
DR RefSeq; XP_005209984.1; XM_005209927.3.
DR RefSeq; XP_010806101.1; XM_010807799.2.
DR RefSeq; XP_015327924.1; XM_015472438.1.
DR AlphaFoldDB; A2VDT6; -.
DR SMR; A2VDT6; -.
DR STRING; 9913.ENSBTAP00000008139; -.
DR PaxDb; A2VDT6; -.
DR PRIDE; A2VDT6; -.
DR Ensembl; ENSBTAT00000008139; ENSBTAP00000008139; ENSBTAG00000006197.
DR Ensembl; ENSBTAT00000076731; ENSBTAP00000064041; ENSBTAG00000006197.
DR GeneID; 535814; -.
DR KEGG; bta:535814; -.
DR CTD; 340481; -.
DR VEuPathDB; HostDB:ENSBTAG00000006197; -.
DR VGNC; VGNC:37137; ZDHHC21.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000158006; -.
DR HOGENOM; CLU_048061_3_0_1; -.
DR InParanoid; A2VDT6; -.
DR OMA; GTHWKIL; -.
DR OrthoDB; 1491968at2759; -.
DR TreeFam; TF319798; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000006197; Expressed in semen and 103 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0071875; P:adrenergic receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR GO; GO:1903140; P:regulation of establishment of endothelial barrier; ISS:UniProtKB.
DR GO; GO:1904997; P:regulation of leukocyte adhesion to arterial endothelial cell; ISS:UniProtKB.
DR GO; GO:0003056; P:regulation of vascular associated smooth muscle contraction; ISS:UniProtKB.
DR GO; GO:0048733; P:sebaceous gland development; IEA:Ensembl.
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; Golgi apparatus; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..265
FT /note="Palmitoyltransferase ZDHHC21"
FT /id="PRO_0000288683"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..44
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..185
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 90..140
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 120
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9D270"
SQ SEQUENCE 265 AA; 31463 MW; D32AE447AEAEAC0B CRC64;
MGLRIHFVVD PHGWCCMGLI VFVWLYNFFL IPKIVLFPHY EEGHIPGILI IIFYGIAMFC
LVALVRASIT DPGRLPENPK IPHGEREFWE LCNKCNLMRP KRSHHCSRCG HCVRRMDHHC
PWINNCVGED NHWLFLQLCF YTELLTCYAL MFSFCHYYYF LPLKKRNLDL FVVRHELAIM
RLAAFMGITM LVGITGLFYT QLIGIITDTT SIEKMSNCCE EISRPRKPWQ QTFSEVFGTR
WKILWFIPFR RRQPLRVPYH FANHV
