ID A8Y2W8_CAEBR Unreviewed; 593 AA.
AC A8Y2W8;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 2.
DT 24-JAN-2024, entry version 108.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN Name=dhhc-14 {ECO:0000313|WormBase:CBG22799};
GN Synonyms=Cbr-tag-233 {ECO:0000313|EMBL:CAP39302.2}, tag-233
GN {ECO:0000313|WormBase:CBG22799};
GN ORFNames=CBG22799 {ECO:0000313|WormBase:CBG22799}, CBG_22799
GN {ECO:0000313|EMBL:CAP39302.2};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP39302.2, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP39302.2, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP39302.2,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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 AKR/ZDHHC17 subfamily. {ECO:0000256|ARBA:ARBA00010104}.
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DR EMBL; HE601156; CAP39302.2; -; Genomic_DNA.
DR AlphaFoldDB; A8Y2W8; -.
DR STRING; 6238.A8Y2W8; -.
DR WormBase; CBG22799; CBP41123; WBGene00041272; Cbr-dhhc-14.
DR eggNOG; KOG0509; Eukaryota.
DR eggNOG; KOG1311; Eukaryota.
DR HOGENOM; CLU_012510_3_1_1; -.
DR InParanoid; A8Y2W8; -.
DR OMA; RCHNLLE; -.
DR OrthoDB; 33889at2759; -.
DR Proteomes; UP000008549; Chromosome X.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016409; F:palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
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:SF108; PALMITOYLTRANSFERASE HIP14; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF01529; DHHC; 1.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 4.
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 Reference proteome {ECO:0000313|Proteomes:UP000008549};
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 283..303
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 309..330
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 337..358
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 460..479
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 499..521
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT REPEAT 54..86
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 88..120
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 121..154
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 190..222
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 411..549
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
SQ SEQUENCE 593 AA; 66777 MW; AC09C632CF2C8758 CRC64;
MDGDTEVLTH NMRPPAVIDV FNLHAVISAT QHGQADLVRE ALKQGVSPNA TDDDGCSLLH
WAAINNRLEV ARLLISYNAD TNLVGGVLAS SPIHWAARNG LVAMCAMLVK AGAVCNIRDI
QGYTPIHLAI QGNHIGLVAY FLLKFDYAKD ISDNSGMTPA MLCAKKSYTM FPLRLIVRAG
ADLSLKEHFS GNTALHLAAH DRNSSAVIEL LQGNADVNIR NKQSETPLDM ARAIKNPHIL
GDSLSIYQKH TKLSLITEMM EEAARKQGVS RTSCFRKCFV PPLSTYFFFM VPMFGFFITY
LLFKYLPLVV ATFTTLISCI FLMVLIRFDY HDPTYKLLPY GVTIAEALLM IFSWTAYAHW
FVPWWAQMLF VLSVIALGFT LFRIGTVDPG IVKAPKNCHQ LYVNEAEAGI QHQHKYCFTC
FIRKLEHTKH CAVCGFCVNN FDHHCPWLNS CVTRRNMREF IMFIISVAVS SFIYCVATTH
YAVMKIDENG LEKFLETEAF LMITIILSAM HAFMLAVLFC VQLNQKIDSQ ALKMSKKKTI
SQGVTTNERI KARRAGHHHS HNSDYNVIHH RPSVSKRCHN LLEFFSSNGD PNW
//