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Database: UniProt
Entry: A0A251TIW6_HELAN
LinkDB: A0A251TIW6_HELAN
Original site: A0A251TIW6_HELAN 
ID   A0A251TIW6_HELAN        Unreviewed;       417 AA.
AC   A0A251TIW6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=S-acyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
DE   AltName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
GN   ORFNames=HannXRQ_Chr10g0291931 {ECO:0000313|EMBL:OTG10824.1};
OS   Helianthus annuus (Common sunflower).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC   Heliantheae alliance; Heliantheae; Helianthus.
OX   NCBI_TaxID=4232 {ECO:0000313|EMBL:OTG10824.1, ECO:0000313|Proteomes:UP000215914};
RN   [1] {ECO:0000313|Proteomes:UP000215914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. SF193 {ECO:0000313|Proteomes:UP000215914};
RX   PubMed=28538728; DOI=10.1038/nature22380;
RA   Badouin H., Gouzy J., Grassa C.J., Murat F., Staton S.E., Cottret L.,
RA   Lelandais-Briere C., Owens G.L., Carrere S., Mayjonade B., Legrand L.,
RA   Gill N., Kane N.C., Bowers J.E., Hubner S., Bellec A., Berard A.,
RA   Berges H., Blanchet N., Boniface M.C., Brunel D., Catrice O., Chaidir N.,
RA   Claudel C., Donnadieu C., Faraut T., Fievet G., Helmstetter N., King M.,
RA   Knapp S.J., Lai Z., Le Paslier M.C., Lippi Y., Lorenzon L., Mandel J.R.,
RA   Marage G., Marchand G., Marquand E., Bret-Mestries E., Morien E.,
RA   Nambeesan S., Nguyen T., Pegot-Espagnet P., Pouilly N., Raftis F.,
RA   Sallet E., Schiex T., Thomas J., Vandecasteele C., Vares D., Vear F.,
RA   Vautrin S., Crespi M., Mangin B., Burke J.M., Salse J., Munos S.,
RA   Vincourt P., Rieseberg L.H., Langlade N.B.;
RT   "The sunflower genome provides insights into oil metabolism, flowering and
RT   Asterid evolution.";
RL   Nature 546:148-152(2017).
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       {ECO:0000256|ARBA:ARBA00008574, ECO:0000256|RuleBase:RU079119}.
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DR   EMBL; CM007899; OTG10824.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A251TIW6; -.
DR   STRING; 4232.A0A251TIW6; -.
DR   EnsemblPlants; mRNA:HanXRQr2_Chr10g0435621; mRNA:HanXRQr2_Chr10g0435621; HanXRQr2_Chr10g0435621.
DR   Gramene; mRNA:HanXRQr2_Chr10g0435621; mRNA:HanXRQr2_Chr10g0435621; HanXRQr2_Chr10g0435621.
DR   InParanoid; A0A251TIW6; -.
DR   OMA; WINIVQE; -.
DR   Proteomes; UP000215914; Chromosome 10.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   PANTHER; PTHR22883:SF419; S-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR22883; ZINC FINGER DHHC DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU079119}; Membrane {ECO:0000256|RuleBase:RU079119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215914};
KW   Transferase {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM        37..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        71..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        193..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        236..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          149..269
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
SQ   SEQUENCE   417 AA;  48320 MW;  13885E6F2B4C7D73 CRC64;
     MAEQGNQNPI RLYQAWKGSN RFFCWGRLIF GPDVSSLYLT IVLIGGPALC FCIRVYQNIN
     DNDKHGKDSD YWYIVLFVAA FLTCLDILFL LMTSSRDPGI IPRNTKPPES EEAFDMNTPS
     MEWINDKTPH LRLPRTKEVI VNGHPVNVKY CDTCMLYRPP RASHCSICNN CVQKFDHHCP
     WVGQCIGLRN YRFFYLFIST STVLCLYVLG FSWVHIAQNK EGVLKAMQKD ILSDVLIVYC
     FITVWFVGGL SVFHFYLICT NQTTYENFRY RYDKKENPYH KGIIRNLQEV FLSKISPSLN
     NFRAFACEAE NVVAEETGTD NVRTSKEKID IEMGNRFAES EGISLPEILQ NLHYDELEGN
     SKGKEGIVDF DIQPSPFIFE PEKRDEEIIA RETETMHQWL FRVSSECGRR MQKPFAD
//
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