ID A0A3B4XKU8_SERLL Unreviewed; 642 AA.
AC A0A3B4XKU8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000012528.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000012528.1}
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|RuleBase:RU079119};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004439}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004439}. 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 {ECO:0000256|RuleBase:RU079119}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU079119}.
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DR AlphaFoldDB; A0A3B4XKU8; -.
DR STRING; 1841481.ENSSLDP00000012528; -.
DR Ensembl; ENSSLDT00000012982.1; ENSSLDP00000012528.1; ENSSLDG00000009964.1.
DR GeneTree; ENSGT00530000063074; -.
DR OrthoDB; 33889at2759; -.
DR Proteomes; UP000261360; Unplaced.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0042665; P:regulation of ectodermal cell fate specification; IEA:Ensembl.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR PANTHER; PTHR24161; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24161:SF16; PALMITOYLTRANSFERASE ZDHHC13; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF01529; DHHC; 1.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU079119};
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Membrane {ECO:0000256|RuleBase:RU079119};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU079119};
KW Transmembrane {ECO:0000256|RuleBase:RU079119};
KW Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT TRANSMEM 312..330
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 336..354
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 366..388
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 394..412
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 490..513
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 525..549
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 556..573
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT REPEAT 101..133
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 135..167
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 168..200
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 201..234
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 236..268
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 446..577
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 642 AA; 71686 MW; 692FD892CA557D93 CRC64;
MDWTGDGNQD HGHDSCHHGH AGHGHSHGPR AAAFGGTGHP FMPAFHGQFG KIVEQTQQPK
KRSHMDDSSS WDIVKATQFG ILERCKELVE AGYDVRQPDK ENVTLLHWAA INNRSELVKY
FISKGAIVDQ LGGDLNSTPL HWAIRQGHLP MVIQLMRYGA DPSVADGEGY RALHLAILFQ
HMAIAAYLMA KGQEVDGPDC NGQTPLMLAA QKIIGPEPTN FLIKNNASVS AVDKVNRNTP
LHCAVLAGNV DAAHILLEAG ASVDADNING HTPIDLAHQV HSPLLIHMLN HIKQERIRSN
SRCLRIVNRY RVILQFLLCT AMFGSVGAIV DMNSESWLLK AILLACVIGV MNLASRNFPT
PAFQSLLPAT SLMASIFWML VTWCLWFLPD GPSATVQVLF TLNATALLYY YLRTCRTDPG
FVKATEEEKK MNVLVLAEAG CLDPRIFCTS CMIKKPMRTN HCFNCDACVA KQDHHSVWTN
GCIGARNHHY FILFLLSLML MGAWMFYGCL VYWSTHCVLH YEEQGLWGVV SALVSCSPWL
LSIFVLAFYH TCWSGLILLL QLYQIAFLGL TTAERTNLMS HQRKIRQPVS LKQNPYNLGV
VRNLVSFFQL RCCGLFKPTV IDWTQQFPPG RDQHMFGLTD MV
//
