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AIG2A_ARATH
ID   AIG2A_ARATH             Reviewed;         170 AA.
AC   P54121;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Protein AIG2 A {ECO:0000305};
DE            EC=2.3.2.- {ECO:0000305};
DE   AltName: Full=Avirulence-induced gene 2 protein {ECO:0000303|PubMed:8742710};
DE   AltName: Full=Avirulence-induced gene 2 protein A {ECO:0000305};
DE   AltName: Full=AvrRpt2-induced gene 2 {ECO:0000303|PubMed:8742710};
DE   AltName: Full=Protein AIG2 {ECO:0000303|PubMed:8742710};
DE   AltName: Full=Putative gamma-glutamylcyclotransferase {ECO:0000250|UniProtKB:O75223};
GN   Name=AIG2A {ECO:0000305}; Synonyms=AIG2 {ECO:0000303|PubMed:8742710};
GN   OrderedLocusNames=At3g28930 {ECO:0000312|Araport:AT3G28930};
GN   ORFNames=K5K13.3 {ECO:0000312|EMBL:BAA95744.1}, K5K13_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 [MRNA], AND INDUCTION.
RC   STRAIN=cv. Columbia;
RX   PubMed=8742710; DOI=10.2307/3870267;
RA   Reuber T.L., Ausubel F.M.;
RT   "Isolation of Arabidopsis genes that differentiate between resistance
RT   responses mediated by the RPS2 and RPM1 disease resistance genes.";
RL   Plant Cell 8:241-249(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(2000).
RN   [3]
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   [4]
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   [5]
RP   GENE FAMILY.
RX   PubMed=18214976; DOI=10.1002/prot.21936;
RA   de la Cruz N.B., Peterson F.C., Volkman B.F.;
RT   "Solution structure of At3g28950 from Arabidopsis thaliana.";
RL   Proteins 71:546-551(2008).
CC   -!- FUNCTION: Putative gamma-glutamylcyclotransferase.
CC       {ECO:0000250|UniProtKB:O75223}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000305|PubMed:18214976}.
CC   -!- DEVELOPMENTAL STAGE: Peak of expression around the time of early
CC       inflorescence. {ECO:0000305|PubMed:18214976}.
CC   -!- INDUCTION: Up-regulated early after infection with P.syringae carrying
CC       avrRpt2 (PubMed:8742710). Expressed constitutively (PubMed:18214976).
CC       {ECO:0000269|PubMed:8742710, ECO:0000305|PubMed:18214976}.
CC   -!- SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family.
CC       {ECO:0000305}.
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DR   EMBL; U40857; AAC49283.1; -; mRNA.
DR   EMBL; AB025615; BAA95744.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77510.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM64138.1; -; Genomic_DNA.
DR   EMBL; AF372890; AAK49606.1; -; mRNA.
DR   EMBL; AY057725; AAL15355.1; -; mRNA.
DR   RefSeq; NP_001326185.1; NM_001338977.1.
DR   RefSeq; NP_189535.1; NM_113814.5.
DR   AlphaFoldDB; P54121; -.
DR   SMR; P54121; -.
DR   BioGRID; 7858; 1.
DR   STRING; 3702.AT3G28930.1; -.
DR   iPTMnet; P54121; -.
DR   PaxDb; P54121; -.
DR   PRIDE; P54121; -.
DR   ProteomicsDB; 245009; -.
DR   DNASU; 822529; -.
DR   EnsemblPlants; AT3G28930.1; AT3G28930.1; AT3G28930.
DR   EnsemblPlants; AT3G28930.3; AT3G28930.3; AT3G28930.
DR   GeneID; 822529; -.
DR   Gramene; AT3G28930.1; AT3G28930.1; AT3G28930.
DR   Gramene; AT3G28930.3; AT3G28930.3; AT3G28930.
DR   KEGG; ath:AT3G28930; -.
DR   Araport; AT3G28930; -.
DR   TAIR; locus:2086987; AT3G28930.
DR   eggNOG; ENOG502S7T1; Eukaryota.
DR   HOGENOM; CLU_093936_0_0_1; -.
DR   InParanoid; P54121; -.
DR   OMA; ECVPVMV; -.
DR   OrthoDB; 1307538at2759; -.
DR   PhylomeDB; P54121; -.
DR   PRO; PR:P54121; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; P54121; baseline and differential.
DR   Genevisible; P54121; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009617; P:response to bacterium; IEP:TAIR.
DR   CDD; cd06661; GGCT_like; 1.
DR   InterPro; IPR045038; AIG2-like.
DR   InterPro; IPR009288; AIG2-like_dom.
DR   InterPro; IPR013024; GGCT-like.
DR   InterPro; IPR036568; GGCT-like_sf.
DR   PANTHER; PTHR31544; PTHR31544; 1.
DR   Pfam; PF06094; GGACT; 1.
DR   SUPFAM; SSF110857; SSF110857; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..170
FT                   /note="Protein AIG2 A"
FT                   /id="PRO_0000064512"
FT   REGION          147..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        83
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O75223"
FT   BINDING         15..20
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O75223"
SQ   SEQUENCE   170 AA;  19445 MW;  A4C4F6417143AE30 CRC64;
     MTSSDQSPSH DVFVYGSFQE PAVVNLILEC APVMVSAQLH GYHLYRLKGR LHPCISPSDN
     GLINGKILTG LTDSQLESLD MIEGTEYVRK TVEVVLTDTL EKKQVETIVW ANKDDPNMYG
     EWDFEEWKRL HMEKFIEAAT KFMEWKKNPN GRSREEFEKF VQDDSSPASA
 
 
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