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Database: UniProt
Entry: A0A0L8HJN1_OCTBM
LinkDB: A0A0L8HJN1_OCTBM
Original site: A0A0L8HJN1_OCTBM 
ID   A0A0L8HJN1_OCTBM        Unreviewed;       623 AA.
AC   A0A0L8HJN1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN   ORFNames=OCBIM_22013090mg {ECO:0000313|EMBL:KOF89432.1};
OS   Octopus bimaculoides (California two-spotted octopus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX   NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF89432.1};
RN   [1] {ECO:0000313|EMBL:KOF89432.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF89432.1};
RC   TISSUE=Gonad {ECO:0000313|EMBL:KOF89432.1};
RA   Tran T., Druce J.;
RT   "MeaNS - Measles Nucleotide Surveillance Program.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU079119};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {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   EMBL; KQ417980; KOF89432.1; -; Genomic_DNA.
DR   RefSeq; XP_014771794.1; XM_014916308.1.
DR   AlphaFoldDB; A0A0L8HJN1; -.
DR   STRING; 37653.A0A0L8HJN1; -.
DR   EnsemblMetazoa; Ocbimv22013090m; Ocbimv22013090m.p; Ocbimv22013090m.g.
DR   EnsemblMetazoa; XM_014916308.1; XP_014771794.1; LOC106870287.
DR   GeneID; 106870287; -.
DR   KEGG; obi:106870287; -.
DR   OrthoDB; 5480099at2759; -.
DR   GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:SF2; 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   Transferase {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        44..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        144..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        180..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          96..218
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   REGION          281..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          528..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..296
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..347
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        414..438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   623 AA;  70778 MW;  8AEA5BB2F2ED167E CRC64;
     MGRCEFSTRI LPATCAWSLL LVATGLFFIF IVPDHLEKYH MAIPIYQGIL SLFVVANFAL
     ATFMDPGVYP KAHEDEFRDD DFRAPLYKNV EIKGITMRMK WCTTCQFYRP PRCSHCSVCN
     NCIETFDHHC PWVNNCIGRR NYRYFFLFLI SLTIHKISIF SLCLLYVLDH KKELAQAGSI
     VAFIVMVIIG ILIIPVAGLT GFHTVLVARG RTTNEQVTGK FRGSQNPFTR GCCKNCKYAL
     CGPQWPRLVS YKPRTKTVQF ESSRVTYVAA DKDVKIFMDN SNGIKHDNTS NHRQASLSLD
     EETERQSQSM DCEPSPPKQS GSYSNLFDPT NPTSVGAAMQ ANQGNHIGRI SPRIPPRNLY
     TQSPQRTRSA DKKAPVATPE VVSPISSPTV KSQSSSPSPT KYNYAKPPIG YHTPRSNGFT
     SLTPGPQMTM PSTGSSHPPY MGSSVNRGFS RTGSPVIYTL DKSKPQHCQY STGVGQPPYE
     HGNNVNYSSP SHRYMPVEYS SVTYDPDKVR VPRRPMSFVR ALEVSEAVEQ KEKQHATPSK
     RSEAYQEEEK PRNMRVNVAK RWKKHKKQKR IRKRNKDEKR IIYFRSNSNV DETVKRKIGK
     FKNIKVLGMK TTRIKKMKRP DLR
//
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