GT121_ARATH
ID GT121_ARATH Reviewed; 395 AA.
AC Q8H0Z4; Q9M9Q1;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Putative glutamine amidotransferase GAT1_2.1 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000305};
DE AltName: Full=Class I glutamine amidotransferase {ECO:0000303|PubMed:22885937};
DE AltName: Full=GAT1_2 domain-containing protein 1 {ECO:0000305};
GN Name=GAT1_2.1 {ECO:0000303|PubMed:22885937};
GN Synonyms=GAT {ECO:0000303|PubMed:22885937};
GN OrderedLocusNames=At1g15040 {ECO:0000312|Araport:AT1G15040};
GN ORFNames=T15D22.12 {ECO:0000312|EMBL:AAF31027.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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] (ISOFORMS 1 AND 2).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22885937; DOI=10.1104/pp.112.199364;
RA Zhu H., Kranz R.G.;
RT "A nitrogen-regulated glutamine amidotransferase (GAT1_2.1) represses shoot
RT branching in Arabidopsis.";
RL Plant Physiol. 160:1770-1780(2012).
CC -!- FUNCTION: Putative glutamine amidotransferase that represses shoot
CC branching. May act as a factor that links nitrogen stress response and
CC branching control. May activate strigolactones by amidation, or
CC represent a new pathway for repression of shoot branching.
CC {ECO:0000269|PubMed:22885937}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8H0Z4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8H0Z4-2; Sequence=VSP_059214, VSP_059215;
CC -!- INDUCTION: Induced by phosphate starvation. Highly repressed following
CC nitrogen deprivation. {ECO:0000269|PubMed:22885937}.
CC -!- DISRUPTION PHENOTYPE: Enhanced shoot branching phenotype.
CC {ECO:0000269|PubMed:22885937}.
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DR EMBL; AC012189; AAF31027.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29258.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29259.1; -; Genomic_DNA.
DR EMBL; AF332456; AAG48819.1; -; mRNA.
DR EMBL; BT001098; AAN64162.1; -; mRNA.
DR EMBL; AK175150; BAD42913.1; -; mRNA.
DR EMBL; AK175288; BAD43051.1; -; mRNA.
DR EMBL; AK176685; BAD44448.1; -; mRNA.
DR PIR; A86284; A86284.
DR RefSeq; NP_172958.2; NM_101374.3. [Q8H0Z4-2]
DR RefSeq; NP_850943.1; NM_180612.4. [Q8H0Z4-1]
DR AlphaFoldDB; Q8H0Z4; -.
DR SMR; Q8H0Z4; -.
DR STRING; 3702.AT1G15040.1; -.
DR MEROPS; C26.A08; -.
DR iPTMnet; Q8H0Z4; -.
DR PaxDb; Q8H0Z4; -.
DR PRIDE; Q8H0Z4; -.
DR ProteomicsDB; 248522; -. [Q8H0Z4-1]
DR DNASU; 838069; -.
DR EnsemblPlants; AT1G15040.1; AT1G15040.1; AT1G15040. [Q8H0Z4-1]
DR EnsemblPlants; AT1G15040.2; AT1G15040.2; AT1G15040. [Q8H0Z4-2]
DR GeneID; 838069; -.
DR Gramene; AT1G15040.1; AT1G15040.1; AT1G15040. [Q8H0Z4-1]
DR Gramene; AT1G15040.2; AT1G15040.2; AT1G15040. [Q8H0Z4-2]
DR KEGG; ath:AT1G15040; -.
DR Araport; AT1G15040; -.
DR TAIR; locus:2196174; AT1G15040.
DR eggNOG; ENOG502QR1H; Eukaryota.
DR InParanoid; Q8H0Z4; -.
DR OMA; NGTKMEM; -.
DR OrthoDB; 690917at2759; -.
DR PhylomeDB; Q8H0Z4; -.
DR PRO; PR:Q8H0Z4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8H0Z4; baseline and differential.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:2000032; P:regulation of secondary shoot formation; IMP:TAIR.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR011697; Peptidase_C26.
DR InterPro; IPR044668; PuuD-like.
DR PANTHER; PTHR43235; PTHR43235; 1.
DR Pfam; PF07722; Peptidase_C26; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Glutamine amidotransferase; Reference proteome;
KW Stress response; Transferase.
FT CHAIN 1..395
FT /note="Putative glutamine amidotransferase GAT1_2.1"
FT /id="PRO_0000442222"
FT DOMAIN 45..280
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 134
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT VAR_SEQ 308..333
FT /note="ANTVLSKQQENRLKQMGATVRNSCVY -> VRDSFVLHTYRLYVLPLNIGFS
FT DMAE (in isoform 2)"
FT /id="VSP_059214"
FT VAR_SEQ 334..395
FT /note="Missing (in isoform 2)"
FT /id="VSP_059215"
SQ SEQUENCE 395 AA; 45363 MW; 4324DB87B9532219 CRC64;
MVVANDLSSK ILPRVLIVSR RTLRKNKYVD FVGEYHLDLI VSSGAVPVIV PRVNGIHSML
QSFEPIHGVL LCEGEDVDPS LYADDELSDL SPEDMEEIKK AHAEDMTIDR EKDSIELTLA
RLCLERNIPF LGICRGSQIL NVAAGGTLYQ DIDKELGTTM TTTNHIDYDN YDGHRHEARI
VEETPLHKLF EEMEIMVNSY HHQGVKRLAQ RFVPMAYAPD GLIEGFYDPN RYDPKEGQFL
MGLQFHPERM RLPGSDEFDY PGCALVYQEF VKAVIAFQKK QVNATQVEMK RKTTTLVKSF
SQAEFLEANT VLSKQQENRL KQMGATVRNS CVYMKRMKMK EEQERAMDKL SAERLSDMLS
FHHMMARLCS NAIKRKLLEP EHTDRTIESS FFLNY
