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Q94A02 (TAR2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 77. 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:
Tryptophan aminotransferase-related protein 2

EC=2.6.1.27
EC=2.6.1.99
Gene names
Name:TAR2
Ordered Locus Names:At4g24670
ORF Names:F22K18.130
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in auxin production. Both TAA1 and TAR2 are required for maintaining proper auxin levels in roots, while TAA1, TAR1 and TAR2 are required for proper embryo patterning. Involved in the maintenance of the root stem cell niches. Ref.4

Catalytic activity

L-tryptophan + 2-oxoglutarate = (indol-3-yl)pyruvate + L-glutamate.

L-tryptophan + pyruvate = indole-3-pyruvate + L-alanine.

Cofactor

Pyridoxal phosphate By similarity.

Enzyme regulation

Inhibited by L-kynurenine. Ref.6

Pathway

Plant hormone metabolism; auxin biosynthesis.

Subcellular location

Membrane; Single-pass membrane protein Potential.

Tissue specificity

Expressed in roots, cotyledons and in the apical parts of hypocotyls. In roots, restricted to the provasculature of meristematic regions. Detected on the inner side of the apical hooks. Ref.4

Developmental stage

In early-stage flowers, expressed in all floral organs. Becomes later restricted to the gynoecia, preferentially to the outer cell layers that give rise to the valves. No expression in flowers at anthesis. Ref.4

Induction

Up-regulated by ethylene. Ref.4 Ref.6

Disruption phenotype

No visible phenotype. Ref.4

Sequence similarities

Belongs to the alliinase family.

Sequence caution

The sequence CAA22996.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB79377.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processAuxin biosynthesis
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcotyledon development

Inferred from genetic interaction Ref.4. Source: TAIR

cotyledon vascular tissue pattern formation

Inferred from genetic interaction Ref.4. Source: TAIR

defense response to bacterium

Inferred from genetic interaction PubMed 22181713. Source: TAIR

embryo development ending in seed dormancy

Inferred from genetic interaction Ref.4. Source: TAIR

flower development

Inferred from genetic interaction Ref.4. Source: TAIR

gynoecium development

Inferred from genetic interaction Ref.4. Source: TAIR

indoleacetic acid biosynthetic process

Inferred from genetic interaction Ref.4. Source: TAIR

maintenance of root meristem identity

Inferred from genetic interaction Ref.4. Source: TAIR

phloem or xylem histogenesis

Inferred from genetic interaction Ref.4. Source: TAIR

positive gravitropism

Inferred from genetic interaction Ref.4. Source: TAIR

primary root development

Inferred from genetic interaction Ref.4. Source: TAIR

response to ethylene

Inferred from genetic interaction Ref.4. Source: TAIR

shoot system development

Inferred from genetic interaction Ref.4. Source: TAIR

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionL-tryptophan:2-oxoglutarate aminotransferase activity

Inferred from sequence or structural similarity Ref.4. Source: TAIR

L-tryptophan:pyruvate aminotransferase activity

Inferred from sequence or structural similarity Ref.4. Source: TAIR

carbon-sulfur lyase activity

Inferred from electronic annotation. Source: InterPro

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 440440Tryptophan aminotransferase-related protein 2
PRO_0000411675

Regions

Transmembrane7 – 2620Helical; Potential
Region154 – 1552Pyridoxal phosphate binding By similarity
Region242 – 2454Pyridoxal phosphate binding By similarity
Region265 – 2684Pyridoxal phosphate binding By similarity

Sites

Binding site1121Pyridoxal phosphate By similarity
Binding site2221Pyridoxal phosphate By similarity
Binding site2421Pyridoxal phosphate By similarity
Binding site2761Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2681N6-(pyridoxal phosphate)lysine Potential

Sequences

Sequence LengthMass (Da)Tools
Q94A02 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 1FED7264F48B1D87

FASTA44050,007
        10         20         30         40         50         60 
MGQIPRFLSW RNMLVLSLAI NFSLILKILK GDRERGDSWD RTAYVSIWPV VSTTASESSS 

        70         80         90        100        110        120 
LSSASCNYSK IEEDDDRIIN LKFGDPTVYE RYWQENGEVT TMVIPGWQSL SYFSDENNLC 

       130        140        150        160        170        180 
WFLEPELAKE IVRVHKVVGN AVTQDRFIVV GTGSTQLYQA ALYALSPHDD SGPINVVSAT 

       190        200        210        220        230        240 
PYYSTYPLIT DCLKSGLYRW GGDAKTYKED GPYIELVTSP NNPDGFLRES VVNSTEGILI 

       250        260        270        280        290        300 
HDLAYYWPQY TPITSPADHD VMLFTASKST GHAGIRIGWA LVKDRETARK MIEYIELNTI 

       310        320        330        340        350        360 
GVSKDSQLRV AKVLKVVSDS CGNVTGKSFF DHSYDAMYER WKLLKQAAKD TKRFSVPDFV 

       370        380        390        400        410        420 
SQRCNFFGRV FEPQPAFAWF KCEEGIVDCE KFLREEKKIL TKSGKYFGDE LSNVRISMLD 

       430        440 
RDTNFNIFLH RITSSFNSTL 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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.
[4]"TAA1-mediated auxin biosynthesis is essential for hormone crosstalk and plant development."
Stepanova A.N., Robertson-Hoyt J., Yun J., Benavente L.M., Xie D.Y., Dolezal K., Schlereth A., Juergens G., Alonso J.M.
Cell 133:177-191(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION BY ETHYLENE, GENE FAMILY, NOMENCLATURE.
[5]"Rapid synthesis of auxin via a new tryptophan-dependent pathway is required for shade avoidance in plants."
Tao Y., Ferrer J.L., Ljung K., Pojer F., Hong F., Long J.A., Li L., Moreno J.E., Bowman M.E., Ivans L.J., Cheng Y., Lim J., Zhao Y., Ballare C.L., Sandberg G., Noel J.P., Chory J.
Cell 133:164-176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[6]"A small-molecule screen identifies L-kynurenine as a competitive inhibitor of TAA1/TAR activity in ethylene-directed auxin biosynthesis and root growth in Arabidopsis."
He W., Brumos J., Li H., Ji Y., Ke M., Gong X., Zeng Q., Li W., Zhang X., An F., Wen X., Li P., Chu J., Sun X., Yan C., Yan N., Xie D.Y., Raikhel N. expand/collapse author list , Yang Z., Stepanova A.N., Alonso J.M., Guo H.
Plant Cell 23:3944-3960(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL035356 Genomic DNA. Translation: CAA22996.1. Sequence problems.
AL161561 Genomic DNA. Translation: CAB79377.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84940.1.
CP002687 Genomic DNA. Translation: AEE84941.1.
AY050779 mRNA. Translation: AAK92714.1.
AY091455 mRNA. Translation: AAM14394.1.
PIRT05567.
RefSeqNP_567706.1. NM_118600.1.
NP_974608.1. NM_202879.1.
UniGeneAt.26567.

3D structure databases

ProteinModelPortalQ94A02.
SMRQ94A02. Positions 76-434.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G24670.2-P.

Proteomic databases

PaxDbQ94A02.
PRIDEQ94A02.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G24670.1; AT4G24670.1; AT4G24670.
AT4G24670.2; AT4G24670.2; AT4G24670.
GeneID828569.
KEGGath:AT4G24670.

Organism-specific databases

TAIRAT4G24670.

Phylogenomic databases

eggNOGNOG331832.
HOGENOMHOG000237549.
InParanoidQ94A02.
KOK16903.
OMAGWQSMSY.
PhylomeDBQ94A02.

Enzyme and pathway databases

BioCycARA:GQT-2242-MONOMER.
UniPathwayUPA00151.

Gene expression databases

GenevestigatorQ94A02.

Family and domain databases

Gene3D2.10.25.30. 1 hit.
3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR006948. Alliinase_C.
IPR006947. EGF_alliinase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF04864. Alliinase_C. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTAR2_ARATH
AccessionPrimary (citable) accession number: Q94A02
Secondary accession number(s): Q9SB62
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: December 1, 2001
Last modified: June 11, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names