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Database: UniProt
Entry: A0A455AKG9_PHYMC
LinkDB: A0A455AKG9_PHYMC
Original site: A0A455AKG9_PHYMC 
ID   A0A455AKG9_PHYMC        Unreviewed;       749 AA.
AC   A0A455AKG9;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
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_028336344.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028336344.1};
RN   [1] {ECO:0000313|RefSeq:XP_028336344.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_028336344.1};
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_028336344.1; XM_028480543.2.
DR   AlphaFoldDB; A0A455AKG9; -.
DR   Proteomes; UP000248484; Chromosome 19.
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:UP000248484};
KW   Transferase {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM        132..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        168..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          86..206
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   REGION          278..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          431..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          623..670
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          684..730
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..334
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        693..707
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   749 AA;  79795 MW;  40C0433A5308A467 CRC64;
     MLQCRGLWAG DRRPGSRRVC PWLTRAVSPA VPVYNGILFL FVLANFSMAT FMDPGVFPRA
     DEDEDKEDDF RAPLYKNVDV RGIQVRMKWC ATCHFYRPPR CSHCSVCDNC VEDFDHHCPW
     VNNCIGRRNY RYFFLFLLSL SAHMVGVVAF GLVYVLNHAE GLGAAHTAIT MAVMCVAGLF
     FIPVIGLTGF HVVLVTRGRT TNEQVTGKFR GGVNPFTRGC YGNVEHVLCS PLAPRYVVEP
     PRLPLAARLK PPFLRPELLE RAAPLKVKLS DNGLKAGLGH SKSKGSLDRL DEKPLDLGPP
     LPPKAEAGTF GSDLQTPRPG SAESALSAQR TSPPTPAMYK FRPAFPTGTK ASFCGPGEQV
     TGTDSLTLGE DSIHSLDFAS EPSLDVPDYP PSSLHAAYPP SPPLSAADTF SGALRSLSLK
     AASRRGGDHV ALQPLRSEGG PPTPHRGLFA PHALPNRNGS LSYDSLLNPG SPGGHTCPAH
     PSAGAASYRS PYLHAGAAGD PPRPPPRSFS PVLGLRPREP SPVRYDNLSR TIMASIQERK
     DREERERLLR SQADSLFGDS GVYDAPSSYS LQQASVLSEG PRGPALRCSS RDDLVAGPGF
     GGARNPALQA SLSSLSSAVS RAPRTSSSSL QADLANSGAP GARPASGSHR SPVRQVPPSP
     PSTPRSPSYV GPKAVAFIQA ELPEPPPSLS VQRDHPQLKT PPSKLNGQSP GLARLGPATG
     PTGPSASPAR HTLVKKVSGV GGTTYEISV
//
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