ID   TAR2_ARATH              Reviewed;         440 AA.
AC   Q94A02; Q9SB62;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 129.
DE   RecName: Full=Tryptophan aminotransferase-related protein 2;
DE            EC=2.6.1.27;
DE            EC=2.6.1.99;
GN   Name=TAR2; OrderedLocusNames=At4g24670; ORFNames=F22K18.130;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   INDUCTION BY ETHYLENE, GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=18394997; DOI=10.1016/j.cell.2008.01.047;
RA   Stepanova A.N., Robertson-Hoyt J., Yun J., Benavente L.M., Xie D.Y.,
RA   Dolezal K., Schlereth A., Juergens G., Alonso J.M.;
RT   "TAA1-mediated auxin biosynthesis is essential for hormone crosstalk and
RT   plant development.";
RL   Cell 133:177-191(2008).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=18394996; DOI=10.1016/j.cell.2008.01.049;
RA   Tao Y., Ferrer J.L., Ljung K., Pojer F., Hong F., Long J.A., Li L.,
RA   Moreno J.E., Bowman M.E., Ivans L.J., Cheng Y., Lim J., Zhao Y.,
RA   Ballare C.L., Sandberg G., Noel J.P., Chory J.;
RT   "Rapid synthesis of auxin via a new tryptophan-dependent pathway is
RT   required for shade avoidance in plants.";
RL   Cell 133:164-176(2008).
RN   [6]
RP   ACTIVITY REGULATION.
RX   PubMed=22108404; DOI=10.1105/tpc.111.089029;
RA   He W., Brumos J., Li H., Ji Y., Ke M., Gong X., Zeng Q., Li W., Zhang X.,
RA   An F., Wen X., Li P., Chu J., Sun X., Yan C., Yan N., Xie D.Y., Raikhel N.,
RA   Yang Z., Stepanova A.N., Alonso J.M., Guo H.;
RT   "A small-molecule screen identifies L-kynurenine as a competitive inhibitor
RT   of TAA1/TAR activity in ethylene-directed auxin biosynthesis and root
RT   growth in Arabidopsis.";
RL   Plant Cell 23:3944-3960(2011).
CC   -!- FUNCTION: Involved in auxin production. Both TAA1 and TAR2 are required
CC       for maintaining proper auxin levels in roots, while TAA1, TAR1 and TAR2
CC       are required for proper embryo patterning. Involved in the maintenance
CC       of the root stem cell niches. {ECO:0000269|PubMed:18394997}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-tryptophan = indole-3-pyruvate + L-
CC         glutamate; Xref=Rhea:RHEA:14093, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:17640, ChEBI:CHEBI:29985, ChEBI:CHEBI:57912; EC=2.6.1.27;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tryptophan + pyruvate = indole-3-pyruvate + L-alanine;
CC         Xref=Rhea:RHEA:27586, ChEBI:CHEBI:15361, ChEBI:CHEBI:17640,
CC         ChEBI:CHEBI:57912, ChEBI:CHEBI:57972; EC=2.6.1.99;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:Q9S7N2};
CC   -!- ACTIVITY REGULATION: Inhibited by L-kynurenine.
CC       {ECO:0000269|PubMed:22108404}.
CC   -!- PATHWAY: Plant hormone metabolism; auxin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons and in the apical
CC       parts of hypocotyls. In roots, restricted to the provasculature of
CC       meristematic regions. Detected on the inner side of the apical hooks.
CC       {ECO:0000269|PubMed:18394997}.
CC   -!- DEVELOPMENTAL STAGE: In early-stage flowers, expressed in all floral
CC       organs. Becomes later restricted to the gynoecia, preferentially to the
CC       outer cell layers that give rise to the valves. No expression in
CC       flowers at anthesis. {ECO:0000269|PubMed:18394997}.
CC   -!- INDUCTION: Up-regulated by ethylene. {ECO:0000269|PubMed:18394997}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC       {ECO:0000269|PubMed:18394997}.
CC   -!- SIMILARITY: Belongs to the alliinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA22996.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79377.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL035356; CAA22996.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161561; CAB79377.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE84940.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84941.1; -; Genomic_DNA.
DR   EMBL; AY050779; AAK92714.1; -; mRNA.
DR   EMBL; AY091455; AAM14394.1; -; mRNA.
DR   PIR; T05567; T05567.
DR   RefSeq; NP_567706.1; NM_118600.2.
DR   RefSeq; NP_974608.1; NM_202879.2.
DR   AlphaFoldDB; Q94A02; -.
DR   SMR; Q94A02; -.
DR   STRING; 3702.Q94A02; -.
DR   PaxDb; 3702-AT4G24670-2; -.
DR   ProteomicsDB; 234258; -.
DR   EnsemblPlants; AT4G24670.1; AT4G24670.1; AT4G24670.
DR   EnsemblPlants; AT4G24670.2; AT4G24670.2; AT4G24670.
DR   GeneID; 828569; -.
DR   Gramene; AT4G24670.1; AT4G24670.1; AT4G24670.
DR   Gramene; AT4G24670.2; AT4G24670.2; AT4G24670.
DR   KEGG; ath:AT4G24670; -.
DR   Araport; AT4G24670; -.
DR   TAIR; AT4G24670; TAR2.
DR   eggNOG; ENOG502QPYC; Eukaryota.
DR   HOGENOM; CLU_036760_1_0_1; -.
DR   InParanoid; Q94A02; -.
DR   OMA; HNILTRG; -.
DR   OrthoDB; 1275724at2759; -.
DR   PhylomeDB; Q94A02; -.
DR   UniPathway; UPA00151; -.
DR   PRO; PR:Q94A02; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q94A02; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
DR   GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:InterPro.
DR   GO; GO:0050362; F:L-tryptophan:2-oxoglutarate aminotransferase activity; ISS:TAIR.
DR   GO; GO:0080097; F:L-tryptophan:pyruvate aminotransferase activity; ISS:TAIR.
DR   GO; GO:0043562; P:cellular response to nitrogen levels; IMP:TAIR.
DR   GO; GO:0048825; P:cotyledon development; IGI:TAIR.
DR   GO; GO:0010588; P:cotyledon vascular tissue pattern formation; IGI:TAIR.
DR   GO; GO:0042742; P:defense response to bacterium; IGI:TAIR.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IGI:TAIR.
DR   GO; GO:0009908; P:flower development; IGI:TAIR.
DR   GO; GO:0048467; P:gynoecium development; IGI:TAIR.
DR   GO; GO:0009684; P:indoleacetic acid biosynthetic process; IGI:TAIR.
DR   GO; GO:0048527; P:lateral root development; IMP:TAIR.
DR   GO; GO:0010078; P:maintenance of root meristem identity; IGI:TAIR.
DR   GO; GO:0010087; P:phloem or xylem histogenesis; IGI:TAIR.
DR   GO; GO:0009958; P:positive gravitropism; IGI:TAIR.
DR   GO; GO:0080022; P:primary root development; IGI:TAIR.
DR   GO; GO:0009723; P:response to ethylene; IGI:TAIR.
DR   GO; GO:0048367; P:shoot system development; IGI:TAIR.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 2.10.25.30; EGF-like, alliinase; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR006948; Alliinase_C.
DR   InterPro; IPR037029; Alliinase_N_sf.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43795; BIFUNCTIONAL ASPARTATE AMINOTRANSFERASE AND GLUTAMATE/ASPARTATE-PREPHENATE AMINOTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR43795:SF123; TRYPTOPHAN AMINOTRANSFERASE-RELATED PROTEIN 2; 1.
DR   Pfam; PF04864; Alliinase_C; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   Genevisible; Q94A02; AT.
PE   2: Evidence at transcript level;
KW   Aminotransferase; Auxin biosynthesis; Membrane; Pyridoxal phosphate;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..440
FT                   /note="Tryptophan aminotransferase-related protein 2"
FT                   /id="PRO_0000411675"
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         112
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT   BINDING         154..155
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT   BINDING         222
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT   BINDING         242..245
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT   BINDING         265..268
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT   BINDING         276
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT   MOD_RES         268
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   440 AA;  50007 MW;  1FED7264F48B1D87 CRC64;
     MGQIPRFLSW RNMLVLSLAI NFSLILKILK GDRERGDSWD RTAYVSIWPV VSTTASESSS
     LSSASCNYSK IEEDDDRIIN LKFGDPTVYE RYWQENGEVT TMVIPGWQSL SYFSDENNLC
     WFLEPELAKE IVRVHKVVGN AVTQDRFIVV GTGSTQLYQA ALYALSPHDD SGPINVVSAT
     PYYSTYPLIT DCLKSGLYRW GGDAKTYKED GPYIELVTSP NNPDGFLRES VVNSTEGILI
     HDLAYYWPQY TPITSPADHD VMLFTASKST GHAGIRIGWA LVKDRETARK MIEYIELNTI
     GVSKDSQLRV AKVLKVVSDS CGNVTGKSFF DHSYDAMYER WKLLKQAAKD TKRFSVPDFV
     SQRCNFFGRV FEPQPAFAWF KCEEGIVDCE KFLREEKKIL TKSGKYFGDE LSNVRISMLD
     RDTNFNIFLH RITSSFNSTL
//