ZDH16_MACFA
ID ZDH16_MACFA Reviewed; 377 AA.
AC Q4R7E2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Palmitoyltransferase ZDHHC16 {ECO:0000250|UniProtKB:Q969W1};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q969W1};
DE AltName: Full=Zinc finger DHHC domain-containing protein 16 {ECO:0000250|UniProtKB:Q969W1};
DE Short=DHHC-16 {ECO:0000250|UniProtKB:Q969W1};
GN Name=ZDHHC16 {ECO:0000250|UniProtKB:Q969W1};
GN ORFNames=QtsA-15522 {ECO:0000303|Ref.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Palmitoyl acyltransferase that mediates palmitoylation of
CC proteins such as PLN and ZDHHC6 (By similarity). Required during
CC embryonic heart development and cardiac function, possibly by mediating
CC palmitoylation of PLN, thereby affecting PLN phosphorylation and
CC homooligomerization (By similarity). Also required for eye development
CC (By similarity). Palmitoylates ZDHHC6, affecting the quaternary
CC assembly of ZDHHC6, its localization, stability and function (By
CC similarity). May play a role in DNA damage response (By similarity).
CC May be involved in apoptosis regulation (By similarity). Involved in
CC the proliferation of neural stem cells by regulating the FGF/ERK
CC pathway (By similarity). {ECO:0000250|UniProtKB:B8A4F0,
CC ECO:0000250|UniProtKB:Q969W1, ECO:0000250|UniProtKB:Q9ESG8}.
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:Q969W1};
CC -!- SUBUNIT: Interacts with ABL1 (By similarity). Interacts with COPS5/JAB1
CC (By similarity). {ECO:0000250|UniProtKB:Q969W1,
CC ECO:0000250|UniProtKB:Q9ESG8}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q969W1}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9ESG8}.
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; AB168877; BAE00980.1; -; mRNA.
DR RefSeq; NP_001272132.1; NM_001285203.1.
DR AlphaFoldDB; Q4R7E2; -.
DR SMR; Q4R7E2; -.
DR STRING; 9541.XP_005566169.1; -.
DR GeneID; 101926118; -.
DR CTD; 84287; -.
DR VEuPathDB; HostDB:ENSMFAG00000041608; -.
DR eggNOG; KOG1313; Eukaryota.
DR OMA; CPVRINQ; -.
DR OrthoDB; 1491968at2759; -.
DR Proteomes; UP000233100; Chromosome 9.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016409; F:palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; ISS:UniProtKB.
DR GO; GO:0021537; P:telencephalon development; ISS:UniProtKB.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR039859; ZDH16.
DR PANTHER; PTHR12246; PTHR12246; 1.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Apoptosis; DNA damage; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..377
FT /note="Palmitoyltransferase ZDHHC16"
FT /id="PRO_0000212898"
FT TOPO_DOM 1..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..116
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..266
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 155..205
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 185
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q8IUH5"
SQ SEQUENCE 377 AA; 43645 MW; 795C7FCDF998A81E CRC64;
MRGQRSLLLG PARLCLRLLL LLGYRRRCPP LLRGLVQRWR YGKVCLRSLL YNSFGGSDTA
VDAAFEPVYW LVDNVIRWFG VVFVVLVIVL TGSIVAIAYL CVLPLILRTY SVPRLCWHFF
YSHWNLILIV FHYYQAITTP PGYPPQGRND IATVSICKKC IYPKPARTHH CSICNRCVLK
MDHHCPWLNN CVGHYNHRYF FSFCFFMTLG CVYCSYGSWD LFREAYAAIE KMKQLDKNKL
QAVANQTYHQ TPPPIFSFRE RMTHKSLVYL WFLCSSVALA LGALTVWHAV LISRGETSIE
RHINKKERRR LQAKGRVFRN PYNYGCLDNW KVFLGVDTGR HWLTRVLLPS SHLPHGNGMS
WEPPPWVTAH SASVMAV
