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Protein

Tryptophan aminotransferase-related protein 2

Gene

TAR2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

Enzyme regulationi

Inhibited by L-kynurenine.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei112 – 1121Pyridoxal phosphateBy similarity
Binding sitei222 – 2221Pyridoxal phosphateBy similarity
Binding sitei242 – 2421Pyridoxal phosphateBy similarity
Binding sitei276 – 2761Pyridoxal phosphateBy similarity

GO - Molecular functioni

  1. carbon-sulfur lyase activity Source: InterPro
  2. L-tryptophan:2-oxoglutarate aminotransferase activity Source: TAIR
  3. L-tryptophan:pyruvate aminotransferase activity Source: TAIR
  4. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. auxin biosynthetic process Source: UniProtKB-UniPathway
  2. cellular response to nitrogen levels Source: TAIR
  3. defense response to bacterium Source: TAIR
  4. flower development Source: TAIR
  5. gynoecium development Source: TAIR
  6. lateral root development Source: TAIR
  7. maintenance of root meristem identity Source: TAIR
  8. phloem or xylem histogenesis Source: TAIR
  9. positive gravitropism Source: TAIR
  10. response to ethylene Source: TAIR
  11. shoot system development Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Auxin biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciARA:GQT-2242-MONOMER.
UniPathwayiUPA00151.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophan aminotransferase-related protein 2 (EC:2.6.1.27, EC:2.6.1.99)
Gene namesi
Name:TAR2
Ordered Locus Names:At4g24670
ORF Names:F22K18.130
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G24670.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei7 – 2620HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: TAIR
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Disruption phenotypei

No visible phenotype.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 440440Tryptophan aminotransferase-related protein 2PRO_0000411675Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei268 – 2681N6-(pyridoxal phosphate)lysineSequence Analysis

Proteomic databases

PaxDbiQ94A02.
PRIDEiQ94A02.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

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.1 Publication

Inductioni

Up-regulated by ethylene.1 Publication

Gene expression databases

GenevestigatoriQ94A02.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G24670.2-P.

Structurei

3D structure databases

ProteinModelPortaliQ94A02.
SMRiQ94A02. Positions 76-434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni154 – 1552Pyridoxal phosphate bindingBy similarity
Regioni242 – 2454Pyridoxal phosphate bindingBy similarity
Regioni265 – 2684Pyridoxal phosphate bindingBy similarity

Sequence similaritiesi

Belongs to the alliinase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG331832.
HOGENOMiHOG000237549.
InParanoidiQ94A02.
KOiK16903.
OMAiMIEYIEL.
PhylomeDBiQ94A02.

Family and domain databases

Gene3Di2.10.25.30. 1 hit.
3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR006948. Alliinase_C.
IPR006947. EGF_alliinase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF04864. Alliinase_C. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

Q94A02-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQIPRFLSW RNMLVLSLAI NFSLILKILK GDRERGDSWD RTAYVSIWPV
60 70 80 90 100
VSTTASESSS LSSASCNYSK IEEDDDRIIN LKFGDPTVYE RYWQENGEVT
110 120 130 140 150
TMVIPGWQSL SYFSDENNLC WFLEPELAKE IVRVHKVVGN AVTQDRFIVV
160 170 180 190 200
GTGSTQLYQA ALYALSPHDD SGPINVVSAT PYYSTYPLIT DCLKSGLYRW
210 220 230 240 250
GGDAKTYKED GPYIELVTSP NNPDGFLRES VVNSTEGILI HDLAYYWPQY
260 270 280 290 300
TPITSPADHD VMLFTASKST GHAGIRIGWA LVKDRETARK MIEYIELNTI
310 320 330 340 350
GVSKDSQLRV AKVLKVVSDS CGNVTGKSFF DHSYDAMYER WKLLKQAAKD
360 370 380 390 400
TKRFSVPDFV SQRCNFFGRV FEPQPAFAWF KCEEGIVDCE KFLREEKKIL
410 420 430 440
TKSGKYFGDE LSNVRISMLD RDTNFNIFLH RITSSFNSTL
Length:440
Mass (Da):50,007
Last modified:December 1, 2001 - v1
Checksum:i1FED7264F48B1D87
GO

Sequence cautioni

The sequence CAA22996.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB79377.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiT05567.
RefSeqiNP_567706.1. NM_118600.1.
NP_974608.1. NM_202879.1.
UniGeneiAt.26567.

Genome annotation databases

EnsemblPlantsiAT4G24670.1; AT4G24670.1; AT4G24670.
AT4G24670.2; AT4G24670.2; AT4G24670.
GeneIDi828569.
KEGGiath:AT4G24670.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiT05567.
RefSeqiNP_567706.1. NM_118600.1.
NP_974608.1. NM_202879.1.
UniGeneiAt.26567.

3D structure databases

ProteinModelPortaliQ94A02.
SMRiQ94A02. Positions 76-434.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G24670.2-P.

Proteomic databases

PaxDbiQ94A02.
PRIDEiQ94A02.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G24670.1; AT4G24670.1; AT4G24670.
AT4G24670.2; AT4G24670.2; AT4G24670.
GeneIDi828569.
KEGGiath:AT4G24670.

Organism-specific databases

TAIRiAT4G24670.

Phylogenomic databases

eggNOGiNOG331832.
HOGENOMiHOG000237549.
InParanoidiQ94A02.
KOiK16903.
OMAiMIEYIEL.
PhylomeDBiQ94A02.

Enzyme and pathway databases

UniPathwayiUPA00151.
BioCyciARA:GQT-2242-MONOMER.

Gene expression databases

GenevestigatoriQ94A02.

Family and domain databases

Gene3Di2.10.25.30. 1 hit.
3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR006948. Alliinase_C.
IPR006947. EGF_alliinase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF04864. Alliinase_C. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-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.
    , 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(2002) [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(2007) [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(2007) [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.
    , Yang Z., Stepanova A.N., Alonso J.M., Guo H.
    Plant Cell 23:3944-3960(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.

Entry informationi

Entry nameiTAR2_ARATH
AccessioniPrimary (citable) accession number: Q94A02
Secondary accession number(s): Q9SB62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: December 1, 2001
Last modified: April 1, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.