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Database: UniProt
Entry: A0A3Q4GSW2_NEOBR
LinkDB: A0A3Q4GSW2_NEOBR
Original site: A0A3Q4GSW2_NEOBR 
ID   A0A3Q4GSW2_NEOBR        Unreviewed;       640 AA.
AC   A0A3Q4GSW2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-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};
OS   Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX   NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000006612.1, ECO:0000313|Proteomes:UP000261580};
RN   [1] {ECO:0000313|Ensembl:ENSNBRP00000006612.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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: 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   AlphaFoldDB; A0A3Q4GSW2; -.
DR   STRING; 32507.ENSNBRP00000006612; -.
DR   Ensembl; ENSNBRT00000006809.1; ENSNBRP00000006612.1; ENSNBRG00000005159.1.
DR   GeneTree; ENSGT00940000156001; -.
DR   OMA; LAPRYMG; -.
DR   Proteomes; UP000261580; Unplaced.
DR   Bgee; ENSNBRG00000005159; Expressed in blood and 8 other cell types or tissues.
DR   GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR   GO; GO:0005886; C:plasma membrane; 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:SF3; PALMITOYLTRANSFERASE ZDHHC5; 1.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU079119};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU079119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261580};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU079119};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM        29..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        60..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        161..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        197..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          115..234
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   REGION          303..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..403
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..514
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   640 AA;  68785 MW;  2FDC5B6DE9197145 CRC64;
     MPGFSSGGVG GGVGGVASAP PRPFRPSRYV PVSAATTFLV GATTLFFCFC PWLSEHFSSV
     IPIYNGVIFL FTLANFCMAT FMDPGIFPRE EDEDKEDDFR APLYKTVEIK GIQVRMKWCS
     TCRFYRPPRC SHCSVCDNCV EDFDHHCPWV NNCIGRRNYR YFFLFLLSLT THIMNVFGFG
     LVYVLHHQQE LDTPGAAVMG VMCVAGLFFV PVAGLTGFHI VLVARGRTTN EQVTGKFRGG
     VNPFTNGCLR NITHVLCSSQ APYIGRWRGR QMMEVQPPFL RPALTEAQLE AKVLDNGIQN
     SKSSLDQMES QSADAEAPPP PKPELRYPGL PRADTESSLL TEAPPTPSMY KYRPTFNSPG
     RNHTALTHPN KMIRGESLDS PSPSILQSSR QPSYRSEPSS LDGTTVVGGG VGVRRGGGER
     GEGPGGPGGT AGGVLGGMSG YSLTGRSYTS YPSSLVLSTG GSHSSSLRSA HTAHNPLATL
     HSEGTTDTSY KSLANQTPRN GSLSYDSLLT PSESPEFESA AHELSPQKLH APFLSSAVRG
     QTEVVSPSTP LQGYTSPFLS AQIAQQREGQ LLQGSATFSS PHKAYLRAVS PPLPSSAGPL
     ETHHLLSTSR PVLANHTTSK PGGGVKKVTG VGGTTYEISV
//
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