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Database: UniProt
Entry: A0A194PX50_PAPXU
LinkDB: A0A194PX50_PAPXU
Original site: A0A194PX50_PAPXU 
ID   A0A194PX50_PAPXU        Unreviewed;       635 AA.
AC   A0A194PX50;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, 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};
GN   ORFNames=RR46_11433 {ECO:0000313|EMBL:KPI95720.1};
OS   Papilio xuthus (Asian swallowtail butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Papilionidae; Papilioninae; Papilio.
OX   NCBI_TaxID=66420 {ECO:0000313|EMBL:KPI95720.1, ECO:0000313|Proteomes:UP000053268};
RN   [1] {ECO:0000313|EMBL:KPI95720.1, ECO:0000313|Proteomes:UP000053268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPI95720.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KPI95720.1};
RX   PubMed=26354079; DOI=10.1038/ncomms9212;
RA   Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA   Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA   Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA   Wang W.;
RT   "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL   Nat. Commun. 6:8212-8212(2015).
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; KQ459595; KPI95720.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A194PX50; -.
DR   STRING; 66420.A0A194PX50; -.
DR   Proteomes; UP000053268; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000053268};
KW   Transferase {ECO:0000256|RuleBase:RU079119, ECO:0000313|EMBL:KPI95720.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        143..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        178..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          97..216
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   REGION          308..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          478..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          539..603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..527
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..598
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   635 AA;  70925 MW;  A81AE1010A9C2BAF CRC64;
     MPKCDLKTRY IPATFAWTLL LGTTSLFFYF PCQYYLHRHP WVPAYQGVIT FFVLANFTLA
     TFMDPGVIPK APPDEDREDD FRAPLYRSVE INGITVRMKW CVTCKFYRPP RCSHCSVCNH
     CIETFDHHCP WVNNCIGRRN YRFFFFFLIS LSIHMLSIFG FSLYFVMYNK NLTQVEPIVS
     MVIMGVIVLL AIPIFGLTGF HMVLVSRGRT TNEQVTGKFT GGYNPFSKGC WYNCCYTQFG
     PQYPSLVRPS KYIYKGGKKR RDPGIVGQSA SAISTIATDT HQVKTYTADN GSAHRAVGAH
     AHYNKLSPGR EEHEHEGELE GPGASQSADC EPTPPPLQRR GSAANLFPPP ERQPRPHHYP
     RLSPLPRNTG HGTTTSGYRV VMEPLRYETG ANGARPSPTM QQRIKALGVP TPLAVSSPVR
     SSVVYDSVCV LYCNEHVALH VPRYCGRARR AFRTATAAAP PAACRGTSLP ISIYKDSVSA
     AHRSNPGTPT QPRRADFAPR GSPQRRFLSE GELLRAEPPA HRPTADDIRE LAASPQRGYT
     WAERPPHPAH PAHPARPAHP AHAQPHPAHP AHPPHPSPLS RRRTPAVPSH PHPPRPARPL
     SFVRALEVQD QLERAPPVEP PDRASVYDCN YEISV
//
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