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Q941L0 (CESA3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cellulose synthase A catalytic subunit 3 [UDP-forming]

Short name=AtCesA3
EC=2.4.1.12
Alternative name(s):
Constitutive expression of VSP1 protein 1
Isoxaben-resistant protein 1
Short name=Ath-B
Protein ECTOPIC LIGNIN 1
Protein RADIALLY SWOLLEN 5
Short name=AtRSW5
Gene names
Name:CESA3
Synonyms:ATHB, CEV1, ELI1, IXR1, RSW5
Ordered Locus Names:At5g05170
ORF Names:K2A11.4
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length1065 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation. Involved in the primary cell wall formation, especially in roots. Ref.7 Ref.10 Ref.11 Ref.14 Ref.19 Ref.20

Catalytic activity

UDP-glucose + (1,4-beta-D-glucosyl)(n) = UDP + (1,4-beta-D-glucosyl)(n+1).

Cofactor

Binds 2 zinc ions per subunit By similarity.

Pathway

Glycan metabolism; plant cellulose biosynthesis.

Subunit structure

Interacts with CESA1 and CESA6. Ref.19 Ref.20

Subcellular location

Cell membrane; Multi-pass membrane protein Probable.

Tissue specificity

Expressed in young plants, flowers and roots, and to a lower extent in leaves and stems. Localized in all cells except meristematic cells. Accumulates particularly in root caps, root hairs, epidermal layer, midveins of leaves and anthers. Not present in old tissues. Ref.8 Ref.10 Ref.11 Ref.12

Developmental stage

Mostly expressed in cotyledons during all steps of embryogenesis, and decrease toward the bent-cotyledon stage. Ref.12

Post-translational modification

Phosphorylation level varies significantly during early response to general elicitors.

Disruption phenotype

Mutants cev1 are dark green and contains more jasmonates and ethylene, that leads to shorter and thickened hypocotyls and roots, with prolific root hairs, and the accumulation of purple anthocyanins. They exhibit constitutive and high expression in leaves lamina of vegetative storage proteins (VSP1 and VSP2), basic chitinase CHI-B and plant defensin PDF1.2. In addition, this mutation confers resistance to powdery mildew pathogens such as E.cichoracearum, E.orontii and O.lycopersicum, to the bacterial pathogen P.syringae pv maculicola, and also to the green peach aphid M.persicae. Ref.7

Sequence similarities

Belongs to the glycosyltransferase 2 family. Plant cellulose synthase subfamily.

Contains 1 RING-type zinc finger.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
Cellulose biosynthesis
   Cellular componentCell membrane
Membrane
   DomainCoiled coil
Transmembrane
Transmembrane helix
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellulose biosynthetic process

Inferred from mutant phenotype Ref.11. Source: TAIR

defense response

Traceable author statement PubMed 16255250. Source: TAIR

lignin biosynthetic process

Inferred from genetic interaction PubMed 16159327. Source: TAIR

primary cell wall biogenesis

Inferred from mutant phenotype Ref.11. Source: TAIR

regulation of carbohydrate biosynthetic process

Inferred from genetic interaction PubMed 16159327. Source: TAIR

secondary cell wall biogenesis

Inferred from mutant phenotype PubMed 10887094. Source: TAIR

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 16618929PubMed 22430844PubMed 22923678. Source: TAIR

endosome

Inferred from direct assay PubMed 22923678. Source: TAIR

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay Ref.13Ref.17. Source: TAIR

plasmodesma

Inferred from direct assay PubMed 21533090. Source: TAIR

trans-Golgi network

Inferred from direct assay PubMed 22923678. Source: TAIR

   Molecular_functioncellulose synthase (UDP-forming) activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10651065Cellulose synthase A catalytic subunit 3 [UDP-forming]
PRO_0000166369

Regions

Topological domain1 – 260260Cytoplasmic Potential
Transmembrane261 – 28121Helical; Potential
Topological domain282 – 2832Extracellular Potential
Transmembrane284 – 30421Helical; Potential
Topological domain305 – 842538Cytoplasmic Potential
Transmembrane843 – 86321Helical; Potential
Topological domain864 – 87411Extracellular Potential
Transmembrane875 – 89521Helical; Potential
Topological domain896 – 91015Cytoplasmic Potential
Transmembrane911 – 93121Helical; Potential
Topological domain932 – 96130Extracellular Potential
Transmembrane962 – 98221Helical; Potential
Topological domain983 – 99311Cytoplasmic Potential
Transmembrane994 – 101421Helical; Potential
Topological domain1015 – 10239Extracellular Potential
Transmembrane1024 – 104421Helical; Potential
Topological domain1045 – 106521Cytoplasmic Potential
Zinc finger20 – 6647RING-type; degenerate
Coiled coil433 – 45725 Potential
Compositional bias633 – 66432Lys-rich

Sites

Active site3791 Potential
Active site7651 Potential
Metal binding201Zinc 1 By similarity
Metal binding231Zinc 1 By similarity
Metal binding391Zinc 2 By similarity
Metal binding421Zinc 2 By similarity
Metal binding471Zinc 1 By similarity
Metal binding501Zinc 1 By similarity
Metal binding621Zinc 2 By similarity
Metal binding651Zinc 2 By similarity
Binding site5451Substrate Potential
Binding site5471Substrate Potential

Amino acid modifications

Modified residue31Phosphoserine Ref.15 Ref.18
Modified residue1431Phosphothreonine Ref.21
Modified residue1511Phosphoserine Ref.15 Ref.17 Ref.18 Ref.21
Modified residue1761Phosphoserine Ref.21
Modified residue2111Phosphoserine Ref.13 Ref.15 Ref.18 Ref.21
Modified residue2121Phosphothreonine Ref.13
Modified residue2161Phosphoserine Ref.13 Ref.15 Ref.18 Ref.21
Glycosylation9381N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis3011S → F in eli1-1; reduced cellulose synthesis and aberrant deposition of lignin. Ref.14
Mutagenesis5221A → V in eli1-2; reduced cellulose synthesis and aberrant deposition of lignin.
Mutagenesis6171G → E in cev1; reduced amount of crystalline cellulose in roots. Ref.7 Ref.9 Ref.10
Mutagenesis9421T → I in ixr1-2; confers resistance to the herbicides isoxaben and thiazolidinones. Ref.8
Mutagenesis9981G → D in ixr1-1; confers resistance to the herbicides isoxaben and thiazolidinones. Ref.8
Mutagenesis10561P → S in rsw5; reduction of cellulose synthesis, and temperature sensitive. Ref.16
Sequence conflict3771S → F in AAC39336. Ref.1
Sequence conflict4791R → G in AAC39336. Ref.1
Sequence conflict8581P → L in AAC39336. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q941L0 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: 3AA4714CE3C4D581

FASTA1,065119,683
        10         20         30         40         50         60 
MESEGETAGK PMKNIVPQTC QICSDNVGKT VDGDRFVACD ICSFPVCRPC YEYERKDGNQ 

        70         80         90        100        110        120 
SCPQCKTRYK RLKGSPAIPG DKDEDGLADE GTVEFNYPQK EKISERMLGW HLTRGKGEEM 

       130        140        150        160        170        180 
GEPQYDKEVS HNHLPRLTSR QDTSGEFSAA SPERLSVSST IAGGKRLPYS SDVNQSPNRR 

       190        200        210        220        230        240 
IVDPVGLGNV AWKERVDGWK MKQEKNTGPV STQAASERGG VDIDASTDIL ADEALLNDEA 

       250        260        270        280        290        300 
RQPLSRKVSI PSSRINPYRM VIMLRLVILC LFLHYRITNP VPNAFALWLV SVICEIWFAL 

       310        320        330        340        350        360 
SWILDQFPKW FPVNRETYLD RLALRYDREG EPSQLAAVDI FVSTVDPLKE PPLVTANTVL 

       370        380        390        400        410        420 
SILAVDYPVD KVSCYVSDDG AAMLSFESLA ETSEFARKWV PFCKKYSIEP RAPEWYFAAK 

       430        440        450        460        470        480 
IDYLKDKVQT SFVKDRRAMK REYEEFKIRI NALVSKALKC PEEGWVMQDG TPWPGNNTRD 

       490        500        510        520        530        540 
HPGMIQVFLG QNGGLDAEGN ELPRLVYVSR EKRPGFQHHK KAGAMNALVR VSAVLTNGPF 

       550        560        570        580        590        600 
ILNLDCDHYI NNSKALREAM CFLMDPNLGK QVCYVQFPQR FDGIDKNDRY ANRNTVFFDI 

       610        620        630        640        650        660 
NLRGLDGIQG PVYVGTGCVF NRTALYGYEP PIKVKHKKPS LLSKLCGGSR KKNSKAKKES 

       670        680        690        700        710        720 
DKKKSGRHTD STVPVFNLDD IEEGVEGAGF DDEKALLMSQ MSLEKRFGQS AVFVASTLME 

       730        740        750        760        770        780 
NGGVPPSATP ENLLKEAIHV ISCGYEDKSD WGMEIGWIYG SVTEDILTGF KMHARGWRSI 

       790        800        810        820        830        840 
YCMPKLPAFK GSAPINLSDR LNQVLRWALG SVEILFSRHC PIWYGYNGRL KFLERFAYVN 

       850        860        870        880        890        900 
TTIYPITSIP LLMYCTLPAV CLFTNQFIIP QISNIASIWF LSLFLSIFAT GILEMRWSGV 

       910        920        930        940        950        960 
GIDEWWRNEQ FWVIGGVSAH LFAVFQGILK VLAGIDTNFT VTSKASDEDG DFAELYLFKW 

       970        980        990       1000       1010       1020 
TTLLIPPTTL LIVNLVGVVA GVSYAINSGY QSWGPLFGKL FFAFWVIVHL YPFLKGLMGR 

      1030       1040       1050       1060 
QNRTPTIVVV WSVLLASIFS LLWVRIDPFT SRVTGPDILE CGINC 

« Hide

References

« Hide 'large scale' references
[1]"Molecular analysis of cellulose biosynthesis in Arabidopsis."
Arioli T., Peng L., Betzner A.S., Burn J., Wittke W., Herth W., Camilleri C., Hoefte H., Plazinski J., Birch R., Cork A., Glover J., Redmond J., Williamson R.E.
Science 279:717-720(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence features of the regions of 1,011,550 bp covered by seventeen P1 and TAC clones."
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H., Miyajima N., Tabata S.
DNA Res. 6:183-195(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 635-1065.
Strain: cv. Columbia.
[6]"Higher plant cellulose synthases."
Richmond T.
Genome Biol. 1:REVIEWS3001.1-REVIEWS3001.6(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[7]"The Arabidopsis mutant cev1 has constitutively active jasmonate and ethylene signal pathways and enhanced resistance to pathogens."
Ellis C., Turner J.G.
Plant Cell 13:1025-1033(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLY-617, DISRUPTION PHENOTYPE.
[8]"Modifications of cellulose synthase confer resistance to isoxaben and thiazolidinone herbicides in Arabidopsis Ixr1 mutants."
Scheible W.-R., Eshed R., Richmond T., Delmer D., Somerville C.
Proc. Natl. Acad. Sci. U.S.A. 98:10079-10084(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, MUTAGENESIS OF THR-942 AND GLY-998.
[9]"Constitutive activation of jasmonate signaling in an Arabidopsis mutant correlates with enhanced resistance to Erysiphe cichoracearum, Pseudomonas syringae, and Myzus persicae."
Ellis C., Karafyllidis I., Turner J.G.
Mol. Plant Microbe Interact. 15:1025-1030(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-617.
[10]"The Arabidopsis mutant cev1 links cell wall signaling to jasmonate and ethylene responses."
Ellis C., Karafyllidis I., Wasternack C., Turner J.G.
Plant Cell 14:1557-1566(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF GLY-617.
[11]"Functional analysis of the cellulose synthase genes CesA1, CesA2, and CesA3 in Arabidopsis."
Burn J.E., Hocart C.H., Birch R.J., Cork A.C., Williamson R.E.
Plant Physiol. 129:797-807(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[12]"Genetic complexity of cellulose synthase A gene function in Arabidopsis embryogenesis."
Beeckman T., Przemeck G.K.H., Stamatiou G., Lau R., Terryn N., De Rycke R., Inze D., Berleth T.
Plant Physiol. 130:1883-1893(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[13]"Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry."
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.
Mol. Cell. Proteomics 2:1234-1243(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; THR-212 AND SER-216, MASS SPECTROMETRY.
Strain: cv. La-0.
[14]"Reduced cellulose synthesis invokes lignification and defense responses in Arabidopsis thaliana."
Cano-Delgado A., Penfield S., Smith C., Catley M., Bevan M.
Plant J. 34:351-362(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF SER-301.
[15]"Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database."
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.
Plant Cell 16:2394-2405(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-151; SER-211 AND SER-216, MASS SPECTROMETRY.
[16]"Chimeric proteins suggest that the catalytic and/or C-terminal domains give CesA1 and CesA3 access to their specific sites in the cellulose synthase of primary walls."
Wang J., Howles P.A., Cork A.H., Birch R.J., Williamson R.E.
Plant Physiol. 142:685-695(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF PRO-1056.
[17]"Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis."
Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M., Menke F.L.H.
Mol. Cell. Proteomics 6:1198-1214(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, MASS SPECTROMETRY.
Strain: cv. Columbia.
[18]"Identification of cellulose synthase AtCesA7 (IRX3) in vivo phosphorylation sites -- a potential role in regulating protein degradation."
Taylor N.G.
Plant Mol. Biol. 64:161-171(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-3; SER-151; SER-211 AND SER-216, MASS SPECTROMETRY.
[19]"Genetic evidence for three unique components in primary cell-wall cellulose synthase complexes in Arabidopsis."
Persson S., Paredez A., Carroll A., Palsdottir H., Doblin M., Poindexter P., Khitrov N., Auer M., Somerville C.R.
Proc. Natl. Acad. Sci. U.S.A. 104:15566-15571(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[20]"Organization of cellulose synthase complexes involved in primary cell wall synthesis in Arabidopsis thaliana."
Desprez T., Juraniec M., Crowell E.F., Jouy H., Pochylova Z., Parcy F., Hoefte H., Gonneau M., Vernhettes S.
Proc. Natl. Acad. Sci. U.S.A. 104:15572-15577(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CESA1 AND CESA6.
[21]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-143; SER-151; SER-176; SER-211 AND SER-216, MASS SPECTROMETRY.
Strain: cv. Columbia.
Tissue: Seedling.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF027174 mRNA. Translation: AAC39336.1.
AB018111 Genomic DNA. Translation: BAB09693.1.
CP002688 Genomic DNA. Translation: AED90836.1.
AY045960 mRNA. Translation: AAK76634.2.
BT002335 mRNA. Translation: AAN86168.1.
AK230097 mRNA. Translation: BAF01916.1.
IPIIPI00528019.
PIRT52054.
RefSeqNP_196136.1. NM_120599.3.
UniGeneAt.24338.

3D structure databases

ProteinModelPortalQ941L0.
SMRQ941L0. Positions 3-78, 519-577.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-46437N.
IntActQ941L0. 1 interaction.
STRING3702.AT5G05170.1-P.

Protein family/group databases

CAZyGT2. Glycosyltransferase Family 2.

Proteomic databases

PaxDbQ941L0.
PRIDEQ941L0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G05170.1; AT5G05170.1; AT5G05170.
GeneID830399.
KEGGath:AT5G05170.

Organism-specific databases

GeneFarm5086. 484.
TAIRAt5g05170.

Phylogenomic databases

eggNOGCOG1215.
HOGENOMHOG000241942.
InParanoidQ941L0.
KOK10999.
OMAGNIGKRA.
PhylomeDBQ941L0.
ProtClustDBPLN02638.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-2362.
UniPathwayUPA00695.

Gene expression databases

GenevestigatorQ941L0.
GermOnlineAT5G05170. Arabidopsis thaliana.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR005150. Cellulose_synth.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF03552. Cellulose_synt. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS00518. ZF_RING_1. False negative.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCESA3_ARATH
AccessionPrimary (citable) accession number: Q941L0
Secondary accession number(s): O48948, Q0WLU1, Q9FHK6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: May 1, 2013
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families