ZDH13_MACFA
ID ZDH13_MACFA Reviewed; 622 AA.
AC Q4R690;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Palmitoyltransferase ZDHHC13 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q9CWU2};
DE AltName: Full=Zinc finger DHHC domain-containing protein 13 {ECO:0000250|UniProtKB:Q8IUH4};
DE Short=DHHC-13 {ECO:0000250|UniProtKB:Q9CWU2};
GN Name=ZDHHC13 {ECO:0000250|UniProtKB:Q8IUH4}; ORFNames=QtsA-18740;
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: Palmitoyltransferase that could catalyze the addition of
CC palmitate onto various protein substrates. Palmitoyltransferase for HTT
CC and GAD2. May play a role in Mg(2+) transport.
CC {ECO:0000250|UniProtKB:Q9CWU2}.
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:Q9CWU2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000250|UniProtKB:Q9CWU2};
CC -!- SUBUNIT: Interacts (via ANK repeats) with CLIP3. Interacts (via ANK
CC repeats) with DNAJC5 (via C-terminus). Interacts (via ANK repeats) with
CC HTT. Interacts (via ANK repeats) with MAP6. Interacts (via ANK repeats)
CC with SNAP23. Interacts (via ANK repeats) with SNAP25. May interact (via
CC ANK repeats) with SPRED2. {ECO:0000250|UniProtKB:Q9CWU2}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9CWU2}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q9CWU2}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Low extracellular Mg(2+) induces increase in Golgi
CC and in post-Golgi vesicles. {ECO:0000250|UniProtKB:Q9CWU2}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q8IUH5}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC AKR/ZDHHC17 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB169298; BAE01385.1; -; mRNA.
DR RefSeq; NP_001271600.1; NM_001284671.1.
DR AlphaFoldDB; Q4R690; -.
DR SMR; Q4R690; -.
DR STRING; 9541.XP_005578474.1; -.
DR PRIDE; Q4R690; -.
DR GeneID; 101865635; -.
DR CTD; 54503; -.
DR eggNOG; KOG0509; Eukaryota.
DR OrthoDB; 445686at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0030660; C:Golgi-associated vesicle membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0016409; F:palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR030290; ZDHHC13.
DR PANTHER; PTHR24161:SF16; PTHR24161:SF16; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 2.
DR Pfam; PF01529; DHHC; 1.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50216; DHHC; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Acyltransferase; ANK repeat; Cytoplasmic vesicle;
KW Golgi apparatus; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Repeat; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..622
FT /note="Palmitoyltransferase ZDHHC13"
FT /id="PRO_0000212888"
FT TOPO_DOM 1..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..320
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..370
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..518
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 43..78
FT /note="ANK 1"
FT /evidence="ECO:0000250|UniProtKB:Q8IUH5"
FT REPEAT 81..110
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 115..144
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 148..177
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 181..211
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 216..245
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT REPEAT 249..279
FT /note="ANK 7"
FT /evidence="ECO:0000255"
FT DOMAIN 426..476
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 456
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8IUH4"
SQ SEQUENCE 622 AA; 71077 MW; F66B988E45A287B2 CRC64;
MEGPGLGSQC RNHSHGPHPP GFGRYGICAH ENKELANARE ALPLIEDSSN CDIVKATQYG
IFERCKELVE AGYDVRQPDK ENVSLLHWAA INNRLDLVKF YISKGAVVDQ LGGDLNSTPL
HWAIRQGHLP MVILLLQHGA DPTLTDGEGF SSIHLAVLFQ HMPIIAYLIS KRQSVNMTDV
NGQTPLMLSA HKVIGPEPTG FLLKFNPSLN VVDKIHQNTP LHWAVAAGNV NAVDKLLEAG
SSLDIQNVKG ETPLDMALQN KNQLIIHMLK TEAKMRTNQK FRLWRWLQKC ELFLLLMLSV
ITMWAVGYIL DFNSDSWLLK GCLLVTLFFL TSLFPRFLVG YKNLIYLPTA FLLSSIFWIF
MTWFILFFPD LAGAPFYFSF IFSIVAFLYF FYKTWATDPG FTKASEEEKK VNIITLAETG
CLDFRTFCTS CLIRKPLRSL HCHVCNSCVA RYDQHCLWTG RCIGFGNHHY YIFFLFFLSM
VCGWIIYGSF IYWSNHCATT FKEDGLWTYL NQIVACSPWV LYILMLATFH FSWSTFLLLN
QLFQIAFLGL TSHERISLLK QSKHMKQTLS LRKTPYNLGF MQNLADFFQC GCFGLVKPCV
VDWTSQYTMV FHPAREKVLR SV
