AIGLB_ARATH
ID AIGLB_ARATH Reviewed; 172 AA.
AC Q9FIX1;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=AIG2-like protein B {ECO:0000305};
DE EC=2.3.2.- {ECO:0000305};
DE AltName: Full=Avirulence-induced gene 2-like protein B {ECO:0000305};
DE AltName: Full=Putative gamma-glutamylcyclotransferase {ECO:0000250|UniProtKB:O75223};
GN Name=AIG2LB {ECO:0000305};
GN OrderedLocusNames=At5g39730 {ECO:0000312|Araport:AT5G39730};
GN ORFNames=MKM21.4 {ECO:0000312|EMBL:BAB11379.1};
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=15060130; DOI=10.1074/mcp.m400001-mcp200;
RA Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
RA Garin J., Barbier-Brygoo H., Ephritikhine G.;
RT "Identification of new intrinsic proteins in Arabidopsis plasma membrane
RT proteome.";
RL Mol. Cell. Proteomics 3:675-691(2004).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130}.
CC -!- TISSUE SPECIFICITY: Expressed in flowerss, leaves, stems, seeds and
CC roots. {ECO:0000305|PubMed:18214976}.
CC -!- DEVELOPMENTAL STAGE: Constitutive expression with an increase during
CC flowering. {ECO:0000305|PubMed:18214976}.
CC -!- INDUCTION: Expressed constitutively. {ECO:0000305|PubMed:18214976}.
CC -!- SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family.
CC {ECO:0000305}.
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DR EMBL; AB016876; BAB11379.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94468.1; -; Genomic_DNA.
DR EMBL; AY035142; AAK59646.1; -; mRNA.
DR EMBL; AY059076; AAL15182.1; -; mRNA.
DR EMBL; AY081320; AAL91209.1; -; mRNA.
DR EMBL; AY114688; AAM48007.1; -; mRNA.
DR RefSeq; NP_198789.1; NM_123335.4.
DR AlphaFoldDB; Q9FIX1; -.
DR SMR; Q9FIX1; -.
DR IntAct; Q9FIX1; 7.
DR STRING; 3702.AT5G39730.1; -.
DR iPTMnet; Q9FIX1; -.
DR PaxDb; Q9FIX1; -.
DR PRIDE; Q9FIX1; -.
DR ProteomicsDB; 244890; -.
DR EnsemblPlants; AT5G39730.1; AT5G39730.1; AT5G39730.
DR GeneID; 833969; -.
DR Gramene; AT5G39730.1; AT5G39730.1; AT5G39730.
DR KEGG; ath:AT5G39730; -.
DR Araport; AT5G39730; -.
DR TAIR; locus:2167032; AT5G39730.
DR eggNOG; ENOG502SWGU; Eukaryota.
DR HOGENOM; CLU_093936_0_0_1; -.
DR InParanoid; Q9FIX1; -.
DR OMA; KRLHMKK; -.
DR OrthoDB; 1307538at2759; -.
DR PhylomeDB; Q9FIX1; -.
DR PRO; PR:Q9FIX1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIX1; baseline and differential.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Acyltransferase; Cell membrane; Membrane; Reference proteome; Transferase.
FT CHAIN 1..172
FT /note="AIG2-like protein B"
FT /id="PRO_0000438022"
FT REGION 146..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..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 172 AA; 20018 MW; 9FCECF6520D2946D CRC64;
MSSSDSPQLH NIFVYGSFQE PDIIHVMLNR IPEIVSATLP GFKRFRLKGR LYPCIIPSEN
GEVHGKVLMG LTNDELENVD WVEGNEYERV FVEVVRKDNS EKMRVETYPW INKNDPDIGG
EWDFEEWKRL HMKTFIEAFT EIMERKRNPQ GKGRDDFSNV LKEEDPANAP SS
