TAR2_ORYSJ
ID TAR2_ORYSJ Reviewed; 507 AA.
AC Q5VQG8; Q0JQC9;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Tryptophan aminotransferase-related protein 2 {ECO:0000303|PubMed:22582989};
DE Short=OsTAR2 {ECO:0000303|PubMed:22582989};
DE EC=2.6.1.27 {ECO:0000305};
DE AltName: Full=Protein FISH BONE {ECO:0000303|PubMed:24654985};
GN Name=TAR2 {ECO:0000303|PubMed:22582989};
GN Synonyms=FIB {ECO:0000303|PubMed:24654985},
GN TAA1 {ECO:0000303|PubMed:29740464};
GN OrderedLocusNames=Os01g0169800 {ECO:0000312|EMBL:BAS70606.1},
GN LOC_Os01g07500 {ECO:0000305};
GN ORFNames=OJ1276_B06.34 {ECO:0000312|EMBL:BAD68317.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=22582989; DOI=10.1111/j.1399-3054.2012.01649.x;
RA Abu-Zaitoon Y.M., Bennett K., Normanly J., Nonhebel H.M.;
RT "A large increase in IAA during development of rice grains correlates with
RT the expression of tryptophan aminotransferase OsTAR1 and a grain-specific
RT YUCCA.";
RL Physiol. Plantarum 146:487-499(2012).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF GLY-475.
RX PubMed=24654985; DOI=10.1111/tpj.12517;
RA Yoshikawa T., Ito M., Sumikura T., Nakayama A., Nishimura T., Kitano H.,
RA Yamaguchi I., Koshiba T., Hibara K., Nagato Y., Itoh J.;
RT "The rice FISH BONE gene encodes a tryptophan aminotransferase, which
RT affects pleiotropic auxin-related processes.";
RL Plant J. 78:927-936(2014).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29740464; DOI=10.3389/fpls.2018.00523;
RA Zhang T., Li R., Xing J., Yan L., Wang R., Zhao Y.;
RT "The YUCCA-auxin-WOX11 module controls crown root development in rice.";
RL Front. Plant Sci. 9:523-523(2018).
CC -!- FUNCTION: Probable tryptophan aminotransferase involved in auxin (IAA)
CC biosynthesis (PubMed:24654985, PubMed:29740464). Required for auxin
CC production to initiate multiple change in growth in response to
CC environmental and developmental cues (PubMed:24654985,
CC PubMed:29740464). Functions upstream of YUCCA1 in auxin biosynthesis
CC (PubMed:29740464). Required for polar auxin transport
CC (PubMed:24654985). {ECO:0000269|PubMed:24654985,
CC ECO:0000269|PubMed:29740464}.
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 Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q9S7N2};
CC -!- PATHWAY: Plant hormone metabolism; auxin biosynthesis. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:24654985}.
CC -!- DEVELOPMENTAL STAGE: Expressed in developing grain from 1 to 21 days
CC after pollination. {ECO:0000269|PubMed:22582989}.
CC -!- DISRUPTION PHENOTYPE: Strong dwarf phenotype and pleiotropic
CC developmental defects affecting all organs (PubMed:29740464). Reduced
CC endogenous levels of auxin (PubMed:29740464).
CC {ECO:0000269|PubMed:29740464}.
CC -!- SIMILARITY: Belongs to the alliinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF04049.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB243735; BAI63217.1; -; mRNA.
DR EMBL; AP003339; BAD68317.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF04049.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014957; BAS70606.1; -; Genomic_DNA.
DR RefSeq; XP_015648041.1; XM_015792555.1.
DR RefSeq; XP_015648050.1; XM_015792564.1.
DR AlphaFoldDB; Q5VQG8; -.
DR SMR; Q5VQG8; -.
DR STRING; 4530.OS01T0169800-01; -.
DR PaxDb; Q5VQG8; -.
DR PRIDE; Q5VQG8; -.
DR EnsemblPlants; Os01t0169800-01; Os01t0169800-01; Os01g0169800.
DR GeneID; 4325198; -.
DR Gramene; Os01t0169800-01; Os01t0169800-01; Os01g0169800.
DR KEGG; osa:4325198; -.
DR eggNOG; ENOG502QPYC; Eukaryota.
DR HOGENOM; CLU_036760_0_0_1; -.
DR InParanoid; Q5VQG8; -.
DR OrthoDB; 457006at2759; -.
DR PlantReactome; R-OSA-1119330; Alanine biosynthesis II.
DR PlantReactome; R-OSA-1119486; IAA biosynthesis I.
DR UniPathway; UPA00151; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:InterPro.
DR GO; GO:0050362; F:L-tryptophan:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0009851; P:auxin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR Gene3D; 2.10.25.30; -; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 Pfam; PF04864; Alliinase_C; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Auxin biosynthesis; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..507
FT /note="Tryptophan aminotransferase-related protein 2"
FT /id="PRO_0000444624"
FT REGION 91..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 169
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT BINDING 211..212
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT BINDING 282
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT BINDING 304..307
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT BINDING 327..330
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT BINDING 338
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9S7N2"
FT MOD_RES 330
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255"
FT MUTAGEN 475
FT /note="G->R: In fib-1; strong dwarf phenotype and
FT pleiotropic developmental defects affecting all organs.
FT Reduced endogenous levels of auxin."
FT /evidence="ECO:0000269|PubMed:24654985"
SQ SEQUENCE 507 AA; 55260 MW; 5293C30719FE9691 CRC64;
MAALRVGTRA VEGRFQASNG GGGGGGGMAP SSRLVAAHRE AKPRSSHSAA PWKLPRRRAG
AMPLWRVAVF ASVALNVATL ALLLHHYATS PPPHHHHHDA GLATRSSDAA VHRRARTASS
MAPSTGKPAV TTDSVINLDH GDPTMFEEFW RETGDAAEVV IPGWQTMSYF SDVTNVCWFL
EPELDRQVRR LHRVVGNAAV DGYHVLVGTG STQLFMAALY ALAPDAAAAA AGEPISVVST
APYYSSYPAV TDFLRSGLFR WAGDADAFKG DSYIELVCSP NNPDGAIREA VLDPKTGNGR
TVHDLAYYWP QYTPITKRAS HDIMLFTVSK STGHAGTRIG WALVKDRAIA RKMTKFVELN
TIGVSKDSQM RAAKVLAAVS DGYERRPEQT KETMTTPLRL FDFGRRKMVE RWSMLRAAAA
ASGIFSLPEE TSGFCNFTKE TAATNPAFAW LRCDREDVED CAGFLRGHKI LTRSGAQFGA
DARYVRVSML DRDDAFDIFI NRLSSLK
