AZG2_ARATH
ID AZG2_ARATH Reviewed; 530 AA.
AC Q84MA8; Q9FGR5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Adenine/guanine permease AZG2;
DE AltName: Full=AzgA-homolog protein;
DE AltName: Full=Protein AZAGUANINE RESISTANT 2;
DE Short=AtAzg2;
GN Name=AZG2; OrderedLocusNames=At5g50300; ORFNames=K6A12.16;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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].
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].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19121308; DOI=10.1016/j.febslet.2008.12.048;
RA Mansfield T.A., Schultes N.P., Mourad G.S.;
RT "AtAzg1 and AtAzg2 comprise a novel family of purine transporters in
RT Arabidopsis.";
RL FEBS Lett. 583:481-486(2009).
CC -!- FUNCTION: Transports natural purines (adenine and guanine) as well as
CC purine analogs. Confers sensitivity to 8-azaadenine and 8-azaguanine
CC (8-azg). {ECO:0000269|PubMed:19121308}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Resistance to 8-azaadenine and 8-azaguanine, and,
CC to a lower extent, to 5-fluorouracil, but not to other toxic nucleobase
CC analogs. Deficiency in the uptake of adenine and guanine.
CC {ECO:0000269|PubMed:19121308}.
CC -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2) (TC
CC 2.A.40) family. Azg-like subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09401.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB024031; BAB09401.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95923.1; -; Genomic_DNA.
DR EMBL; BT006441; AAP21249.1; -; mRNA.
DR EMBL; AK227445; BAE99448.1; -; mRNA.
DR RefSeq; NP_001332453.1; NM_001344886.1.
DR RefSeq; NP_199841.2; NM_124409.4.
DR AlphaFoldDB; Q84MA8; -.
DR STRING; 3702.AT5G50300.1; -.
DR PaxDb; Q84MA8; -.
DR PRIDE; Q84MA8; -.
DR EnsemblPlants; AT5G50300.1; AT5G50300.1; AT5G50300.
DR GeneID; 835095; -.
DR Gramene; AT5G50300.1; AT5G50300.1; AT5G50300.
DR KEGG; ath:AT5G50300; -.
DR Araport; AT5G50300; -.
DR TAIR; locus:2157752; AT5G50300.
DR eggNOG; ENOG502QQ5E; Eukaryota.
DR HOGENOM; CLU_024508_3_1_1; -.
DR InParanoid; Q84MA8; -.
DR OMA; RKGSYFF; -.
DR OrthoDB; 996173at2759; -.
DR PhylomeDB; Q84MA8; -.
DR PRO; PR:Q84MA8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84MA8; baseline and differential.
DR Genevisible; Q84MA8; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0000295; F:adenine nucleotide transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0001409; F:guanine nucleotide transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0005345; F:purine nucleobase transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0051503; P:adenine nucleotide transport; IMP:UniProtKB.
DR GO; GO:0015853; P:adenine transport; IMP:UniProtKB.
DR GO; GO:1903790; P:guanine nucleotide transmembrane transport; IMP:UniProtKB.
DR GO; GO:0015854; P:guanine transport; IMP:UniProtKB.
DR GO; GO:0006863; P:purine nucleobase transport; IMP:TAIR.
DR InterPro; IPR045018; Azg-like.
DR InterPro; IPR029950; AZG2.
DR InterPro; IPR006043; NCS2.
DR PANTHER; PTHR43337; PTHR43337; 1.
DR PANTHER; PTHR43337:SF13; PTHR43337:SF13; 1.
DR Pfam; PF00860; Xan_ur_permease; 1.
PE 2: Evidence at transcript level;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..530
FT /note="Adenine/guanine permease AZG2"
FT /id="PRO_0000379906"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..504
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 530 AA; 56277 MW; 2B7C37AC661BCA37 CRC64;
MGREKTLCKS WSDMKKHLND TVSKSFIGRF FKLEARKTTF TTELRAATAT FLTMAYIITV
NANILADSGA TCSINDCSTV ASSSPPGPEC VLGSNPGYEQ CISRVKKDLV VATSLSAMVG
SLAMGLLANL PFGLAPGMGA NAYIAYNVVG FRGSGSISYH TAMAIVLLEG CAFLAVSALG
LRGKLARLIP QTVRLACAVG IGMFIAFVGL QMNQGIGLVG PDKSTLVTLT ACAETDPVTG
ACLGGKMKSP TFWLAVVGFL ITSFGLMKNV KGSMIYGIVF VTAISWIRGT QVTIFPHTPL
GDSNYNYFTK IVDFHKIQST LGAISFTEFR KSEVWVAFAT LFYVDLLGTT GVLYTMAEIG
GFVEDGKFEG EYAAYLVDAG SSVVGSALGV TTTATFVESS AGLKEGGKTG LTAVIVGLYF
LASMFFTPLV TNVPRWAVGP SLVMVGVMMM GVVKDIRWGE TKEAVTAFVT ILLMPLTYSI
ANGIIAGIGI YLALSMYDVV LGVAKWLNGV RKRVMREHNQ VSSVATVEIV
