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Database: UniProt
Entry: A0A3Q0CY80_MESAU
LinkDB: A0A3Q0CY80_MESAU
Original site: A0A3Q0CY80_MESAU 
ID   A0A3Q0CY80_MESAU        Unreviewed;       715 AA.
AC   A0A3Q0CY80;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN   Name=Zdhhc8 {ECO:0000313|RefSeq:XP_021087145.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021087145.1};
RN   [1] {ECO:0000313|RefSeq:XP_021087145.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00023340};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC         Evidence={ECO:0000256|ARBA:ARBA00023340};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004653}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC       {ECO:0000256|RuleBase:RU079119}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       ERF2/ZDHHC9 subfamily. {ECO:0000256|ARBA:ARBA00023463}.
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DR   RefSeq; XP_021087145.1; XM_021231486.1.
DR   AlphaFoldDB; A0A3Q0CY80; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   PANTHER; PTHR12349; ANKYRIN REPEAT AND LEM DOMAIN-CONTAINING PROTEIN 2; 1.
DR   PANTHER; PTHR12349:SF1; PALMITOYLTRANSFERASE ZDHHC8; 1.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU079119};
KW   Membrane {ECO:0000256|RuleBase:RU079119};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW   Transferase {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM        12..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          102..158
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   REGION          229..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          303..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          376..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          550..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..471
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..505
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..520
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..606
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   715 AA;  77134 MW;  699329F8CE205277 CRC64;
     MPRSPGTRLK PAKYIPVATA AALLVGSSTL FFVFTCPWLT RAVSPAIPVY NGILFLFVLA
     NFSMATFMDP GVFPRADEDE DKEDDFRAPL YKNVDVRGIQ VRMKWCATCH FYRPPRCSHC
     SVCDNCVEDF DHHCPWVNNC IGRRNYRYFF LFLLSLSAHM VTGKFRGGVN PFTRGCYGNV
     EHVLCSPLAP RYVVESPRMP LSISLKPPFL RPELLERAVP LKVKLSDNGL KAGRSKSKGS
     LDQLDEKPLD LGPPLPPKIE AGTFGRDLQT PRPGSAESAL SVQRTSPPTP AMYKFRPAFS
     TGPKTPFCGP SEQVPGPDSL TLADDSTHSL DFVSEPSLDL PDHGPGGLHP TYPPSPTLNA
     TDAFSGALRS LSLKAASRRG GDHMTLQPLR SEGGPPTPHR GLFAPHALPN RNGSLSYDSL
     LNPGSPSGHA CPTHPSIGMA SYHSPYLHPG PSDPPRPPPR SFSPVLGPRP REPSPVRYDN
     LSRTIMASIQ ERKDREERER LLRSQTDSLF GDSGVYDTPS SYSLQQANVL TEGPRGSGLR
     YGSRDDLVAG PGFGGARNPA LQTSMSSLSS SMSRAPRTSS SSLQADQANN NAPGTRPGSG
     SHRSPAHQGL PSPPGTPRSP SYTGSKAVAF IHTDLPDRAP SLAMQRGRIG TCSRGWGWRG
     PPRGTPGLHL CHLGHPEEHP PLRGPWSVAA GAPPRGTICR LHSAASSLFP SLSGP
//
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