ID I1KQU7_SOYBN Unreviewed; 541 AA.
AC I1KQU7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 79.
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 Name=100807263 {ECO:0000313|EnsemblPlants:KRH42025};
GN ORFNames=GLYMA_08G064300 {ECO:0000313|EMBL:KRH42025.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRH42025};
RN [1] {ECO:0000313|EMBL:KRH42025.1, ECO:0000313|EnsemblPlants:KRH42025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH42025};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH42025.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH42025}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH42025};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH42025.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH42025.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU079119}.
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DR EMBL; CM000841; KRH42025.1; -; Genomic_DNA.
DR RefSeq; XP_003531002.1; XM_003530954.3.
DR AlphaFoldDB; I1KQU7; -.
DR SMR; I1KQU7; -.
DR STRING; 3847.I1KQU7; -.
DR PaxDb; 3847-GLYMA08G06860-1; -.
DR EnsemblPlants; KRH42025; KRH42025; GLYMA_08G064300.
DR GeneID; 100807263; -.
DR Gramene; KRH42025; KRH42025; GLYMA_08G064300.
DR KEGG; gmx:100807263; -.
DR eggNOG; KOG0509; Eukaryota.
DR HOGENOM; CLU_031257_3_0_1; -.
DR InParanoid; I1KQU7; -.
DR OMA; ICMRCVE; -.
DR OrthoDB; 246226at2759; -.
DR Proteomes; UP000008827; Chromosome 8.
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; 3.
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:SF101; PROTEIN S-ACYLTRANSFERASE 23-RELATED; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF01529; DHHC; 1.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 4.
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 Reference proteome {ECO:0000313|Proteomes:UP000008827};
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 268..292
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 304..323
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 409..428
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 448..472
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT REPEAT 57..89
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 90..122
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 123..156
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 157..189
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 364..492
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 541 AA; 59678 MW; 5BF69ADB2A582A09 CRC64;
MASSEIEVVS SSSSVSKPNN DQPPILDVFT ASAHGDFNKL RTFVEQDGAS VSLPDFSGYY
ALQWASLNNF HDIAHYLIQH GADVNAKDNM QQTALHWAAV HGSTLAADVL VENGARVEAA
DVNGYRAVHV AAQFGQTAFL NHIVVKYHAD FDVPDNDGRS PLHWAAYKGF ADTVRLLLFR
DASQGRQDKD GCTPLHWAAL RGNAEACAVL VHAGTKEELM MKDNAGNTPV QLAYDKGHRH
VAPFLSNQQR AHSNYWKGKL CSGIVTDIGY APILFCTIIF LSILFINSVV AAPNLKKITA
VVGLWAWTAL SSAVGSLIMF YKCSSKDPGY IKRLGELGTQ SDTEDPLLNI DLNSSSVWMG
NWSQLCPTCK IIRPVRSKHC PTCKRCVEQF DHHCPWISNC VGKRNKRDFF IFICLGTLTS
SLSGAVAVQR ICTSKPALLA GETWIHYVLV RHLGLVVFLV MDAVVFVATT TLTITQASMI
ARNVTTNELA NSSRYDYLRG PDGRFRNPYN HGCWKNCADF FFLGYTNDDE IAWPPLQQVA
T
//
