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WSD11_ARATH
ID   WSD11_ARATH             Reviewed;         486 AA.
AC   Q5KS41; Q8GXG7; Q9FK03;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Wax ester synthase/diacylglycerol acyltransferase 11 {ECO:0000303|PubMed:18621978};
DE            Short=WS/DGAT 11 {ECO:0000303|PubMed:18621978};
DE   AltName: Full=Diacylglycerol O-acyltransferase WSD11 {ECO:0000303|PubMed:18621978};
DE            EC=2.3.1.20 {ECO:0000250|UniProtKB:Q93ZR6};
DE   AltName: Full=Long-chain-alcohol O-fatty-acyltransferase WSD11 {ECO:0000303|PubMed:18621978};
DE            EC=2.3.1.75 {ECO:0000250|UniProtKB:Q93ZR6};
DE   AltName: Full=Protein FOLDED PETALS 1 {ECO:0000303|PubMed:27135508};
GN   Name=WSD11 {ECO:0000303|PubMed:18621978};
GN   Synonyms=FOP1 {ECO:0000303|PubMed:27135508};
GN   OrderedLocusNames=At5g53390 {ECO:0000312|EMBL:AED96347.1};
GN   ORFNames=K19E1.19 {ECO:0000312|EMBL:AED96347.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia, cv. Landsberg erecta, and cv. Wassilewskija;
RX   PubMed=27135508; DOI=10.3390/plants3030348;
RA   Takeda S., Iwasaki A., Tatematsu K., Okada K.;
RT   "The half-Size ABC transporter FOLDED PETALS 2/ABCG13 is involved in petal
RT   elongation through narrow spaces in Arabidopsis thaliana floral buds.";
RL   Plants (Basel) 3:348-358(2014).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [5]
RP   GENE FAMILY.
RX   PubMed=12502715; DOI=10.1074/jbc.m210533200;
RA   Kalscheuer R., Steinbuchel A.;
RT   "A novel bifunctional wax ester synthase/acyl-CoA:diacylglycerol
RT   acyltransferase mediates wax ester and triacylglycerol biosynthesis in
RT   Acinetobacter calcoaceticus ADP1.";
RL   J. Biol. Chem. 278:8075-8082(2003).
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=18621978; DOI=10.1104/pp.108.123471;
RA   Li F., Wu X., Lam P., Bird D., Zheng H., Samuels A.L., Jetter R., Kunst L.;
RT   "Identification of the wax ester synthase/acyl-coenzyme A: diacylglycerol
RT   acyltransferase WSD1 required for stem wax ester biosynthesis in
RT   Arabidopsis.";
RL   Plant Physiol. 148:97-107(2008).
RN   [7]
RP   REVIEW ON ACYL-LIPID METABOLISM.
RX   PubMed=23505340; DOI=10.1199/tab.0161;
RA   Li-Beisson Y., Shorrosh B., Beisson F., Andersson M.X., Arondel V.,
RA   Bates P.D., Baud S., Bird D., Debono A., Durrett T.P., Franke R.B.,
RA   Graham I.A., Katayama K., Kelly A.A., Larson T., Markham J.E., Miquel M.,
RA   Molina I., Nishida I., Rowland O., Samuels L., Schmid K.M., Wada H.,
RA   Welti R., Xu C., Zallot R., Ohlrogge J.;
RT   "Acyl-lipid metabolism.";
RL   Arabidopsis Book 11:E0161-E0161(2013).
RN   [8]
RP   FUNCTION, MUTAGENESIS OF GLY-274, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX   PubMed=23314942; DOI=10.1104/pp.112.212084;
RA   Takeda S., Iwasaki A., Matsumoto N., Uemura T., Tatematsu K., Okada K.;
RT   "Physical interaction of floral organs controls petal morphogenesis in
RT   Arabidopsis.";
RL   Plant Physiol. 161:1242-1250(2013).
RN   [9]
RP   TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=30729606; DOI=10.1111/tpj.14269;
RA   Patwari P., Salewski V., Gutbrod K., Kreszies T., Dresen-Scholz B.,
RA   Peisker H., Steiner U., Meyer A.J., Schreiber L., Doermann P.;
RT   "Surface wax esters contribute to drought tolerance in Arabidopsis.";
RL   Plant J. 98:727-744(2019).
CC   -!- FUNCTION: Bifunctional wax ester synthase/diacylglycerol
CC       acyltransferase (By similarity). Involved in cuticular wax biosynthesis
CC       (By similarity). Required for petals development, probably by mediating
CC       the production of fatty acids at the plasma membrane in the petal
CC       epidermis acting as lubricants that makes petal elongation smooth in
CC       narrow space between the sepals and the anthers inside floral buds
CC       (PubMed:27135508, PubMed:23314942). {ECO:0000250|UniProtKB:Q93ZR6,
CC       ECO:0000269|PubMed:23314942, ECO:0000269|PubMed:27135508}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol
CC         + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20;
CC         Evidence={ECO:0000250|UniProtKB:Q93ZR6};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-CoA + a long chain fatty alcohol = a wax ester +
CC         CoA; Xref=Rhea:RHEA:38443, ChEBI:CHEBI:10036, ChEBI:CHEBI:17135,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; EC=2.3.1.75;
CC         Evidence={ECO:0000250|UniProtKB:Q93ZR6};
CC   -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC       {ECO:0000250|UniProtKB:Q93ZR6}.
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000250|UniProtKB:Q93ZR6}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23314942};
CC       Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC       membrane {ECO:0000250|UniProtKB:Q93ZR6}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in inflorescences and flowers,
CC       especially at the periphery of petal epidermal cells.
CC       {ECO:0000269|PubMed:23314942, ECO:0000269|PubMed:30729606}.
CC   -!- DEVELOPMENTAL STAGE: First observed in sepal primordia and floral
CC       meristems (PubMed:23314942). High levels in petal primordia and
CC       elongating petals margins but weak expression in the other floral
CC       organs (PubMed:23314942). In mature flowers, accumulates in the
CC       marginal region of petals and in ovules (PubMed:23314942).
CC       {ECO:0000269|PubMed:23314942}.
CC   -!- DISRUPTION PHENOTYPE: Disturbed petal development during their growth
CC       through the narrow space between sepals and anthers, leading to stuck
CC       petals in the bud during elongation, and resulting in the formation of
CC       folded petals in the open flower (PubMed:27135508, PubMed:23314942).
CC       Flattened conical-shaped petal epidermal cells associated with abnormal
CC       contacts of petals with the sepal surface (PubMed:23314942).
CC       {ECO:0000269|PubMed:23314942, ECO:0000269|PubMed:27135508}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the long-chain O-
CC       acyltransferase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB09801.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB189175; BAD83884.1; -; mRNA.
DR   EMBL; AB013388; BAB09801.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED96347.1; -; Genomic_DNA.
DR   EMBL; AK118253; BAC42871.1; -; mRNA.
DR   RefSeq; NP_200151.2; NM_124718.4.
DR   AlphaFoldDB; Q5KS41; -.
DR   SMR; Q5KS41; -.
DR   IntAct; Q5KS41; 6.
DR   STRING; 3702.AT5G53390.1; -.
DR   PaxDb; Q5KS41; -.
DR   PRIDE; Q5KS41; -.
DR   ProteomicsDB; 182957; -.
DR   EnsemblPlants; AT5G53390.1; AT5G53390.1; AT5G53390.
DR   GeneID; 835420; -.
DR   Gramene; AT5G53390.1; AT5G53390.1; AT5G53390.
DR   KEGG; ath:AT5G53390; -.
DR   Araport; AT5G53390; -.
DR   TAIR; locus:2154287; AT5G53390.
DR   eggNOG; ENOG502QTZ2; Eukaryota.
DR   HOGENOM; CLU_027831_0_0_1; -.
DR   InParanoid; Q5KS41; -.
DR   OMA; NTCLLEM; -.
DR   OrthoDB; 828506at2759; -.
DR   PhylomeDB; Q5KS41; -.
DR   UniPathway; UPA00282; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q5KS41; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0102966; F:arachidoyl-CoA:1-dodecanol O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0047196; F:long-chain-alcohol O-fatty-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0048441; P:petal development; IMP:UniProtKB.
DR   GO; GO:0048446; P:petal morphogenesis; IMP:TAIR.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.30.559.10; -; 1.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR045034; O-acyltransferase_WSD1-like.
DR   InterPro; IPR009721; O-acyltransferase_WSD1_C.
DR   InterPro; IPR004255; O-acyltransferase_WSD1_N.
DR   PANTHER; PTHR31650; PTHR31650; 1.
DR   Pfam; PF03007; WES_acyltransf; 1.
DR   Pfam; PF06974; WS_DGAT_C; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Cell membrane; Endoplasmic reticulum; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..486
FT                   /note="Wax ester synthase/diacylglycerol acyltransferase
FT                   11"
FT                   /id="PRO_0000452621"
FT   TOPO_DOM        1..192
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        214..486
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        144
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         274
FT                   /note="G->R: In fop1-1; disturbed petal development due to
FT                   stuck petals in the bud during elongation, and resulting in
FT                   the formation of folded petals in the open flower."
FT                   /evidence="ECO:0000269|PubMed:23314942"
FT   CONFLICT        133
FT                   /note="N -> S (in Ref. 4; BAC42871)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   486 AA;  54849 MW;  46B135463AC47640 CRC64;
     MGEDKKTARE TVEEEPLSPC SRLFNSPDFN CAIIVTMGSK VKGDTPAIIH GLEHTLVNHP
     RFSSILEMNN GKKPRWVRTK VKVEEHVIVP DVDPDIENPD QYLEDYISKL TTIPMDLSKP
     LWEMHLLGVK TSNAESYAIL KIHHSLGDGM SLMSLLLACT RKTSDPEALP TVAVHKKRFG
     PSCNSGFFNK IWWLFVGLWF ILRLLFNTFV DILMFALTIF VLRDTETPLL AKPGSELIPK
     RFVHRIISFD DVKLVKNAMK MTVNDVLLGV TQAGLSRYLS RKYDQEATPK SKESMRRIRL
     RSAIMINLRP NAGIEALADM MAKKSKCRWG NLFGYILLPF SVGLETDPLE YVRQAKATID
     RKKHSLEAVF SMAFFKLILK VLGLKASVVL VRKVIHSTTL SFSNVVGPKE EITFHGHPLN
     YISPCVFGHP HALTLHFQTY ANKVIISVTA DPTVIPDPHK MCDDLVESLK MIKAAVLERG
     LYEIEV
 
 
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