AZG1_ARATH
ID AZG1_ARATH Reviewed; 579 AA.
AC Q9SRK7; Q0WUT2; Q8LDL2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Adenine/guanine permease AZG1;
DE AltName: Full=AzgA-homolog protein;
DE AltName: Full=Protein AZAGUANINE RESISTANT 1;
DE Short=AtAzg1;
GN Name=AZG1; OrderedLocusNames=At3g10960; ORFNames=F9F8.22;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 32-579.
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 [6]
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 but
CC not to other toxic nucleobase analogs. Deficiency in the uptake of
CC adenine and guanine. {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}.
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DR EMBL; AC009991; AAF01525.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74982.1; -; Genomic_DNA.
DR EMBL; AY093125; AAM13124.1; -; mRNA.
DR EMBL; BT010556; AAQ65179.1; -; mRNA.
DR EMBL; AY085941; AAM63152.1; -; mRNA.
DR EMBL; AK227056; BAE99116.1; -; mRNA.
DR RefSeq; NP_566384.1; NM_111933.3.
DR AlphaFoldDB; Q9SRK7; -.
DR BioGRID; 5601; 6.
DR IntAct; Q9SRK7; 3.
DR STRING; 3702.AT3G10960.1; -.
DR TCDB; 2.A.40.7.3; the nucleobase/ascorbate transporter (nat) or nucleobase:cation symporter-2 (ncs2) family.
DR iPTMnet; Q9SRK7; -.
DR PaxDb; Q9SRK7; -.
DR PRIDE; Q9SRK7; -.
DR ProteomicsDB; 240947; -.
DR EnsemblPlants; AT3G10960.1; AT3G10960.1; AT3G10960.
DR GeneID; 820267; -.
DR Gramene; AT3G10960.1; AT3G10960.1; AT3G10960.
DR KEGG; ath:AT3G10960; -.
DR Araport; AT3G10960; -.
DR TAIR; locus:2085517; AT3G10960.
DR eggNOG; ENOG502QQ5E; Eukaryota.
DR HOGENOM; CLU_024508_3_2_1; -.
DR InParanoid; Q9SRK7; -.
DR OMA; YVDIIDC; -.
DR OrthoDB; 996173at2759; -.
DR PhylomeDB; Q9SRK7; -.
DR PRO; PR:Q9SRK7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SRK7; baseline and differential.
DR Genevisible; Q9SRK7; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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:0005345; F:purine nucleobase transmembrane transporter activity; IMP:TAIR.
DR GO; GO:0015853; P:adenine 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; IPR006043; NCS2.
DR PANTHER; PTHR43337; PTHR43337; 1.
DR Pfam; PF00860; Xan_ur_permease; 2.
PE 2: Evidence at transcript level;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..579
FT /note="Adenine/guanine permease AZG1"
FT /id="PRO_0000379905"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 480..500
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 514..534
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 26
FT /note="T -> S (in Ref. 4; AAM63152)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="R -> G (in Ref. 5; BAE99116)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 61669 MW; 153B0DCF2A095355 CRC64;
MEQQQQQQLP STTTRPKPKL LNRLNTYVGS SRVGKRFKLA ERNSTFTTEL RAGTATFLTM
AYILAVNASI LSDSGGTCSV SDCIPLCSNP AIEPSQCTGP GLRLIQPDVS CKFNPVNPGY
AACVEEIRKD LIVATVAASL IGCVIMGLMA NLPLALAPGM GTNAYFAYTV VGFHGSGSIS
YRTALAAVFI EGLIFLFISA IGFRAKLAKL VPKPVRISSS AGIGLFLAFI GLQNNQGIGL
VGYSPSTLVT LAACPASSRI SLAPVITSAN GTVSLLAGGS VSGDIMCIHG RMESPTFWLG
IVGFVIIAYC LVKNVKGAMI YGIVFVTAVS WFRNTEVTAF PNTSAGDAAH DYFKKIVDVH
VIKHTAGALS FSGINKGHFW EALVTFLYVD ILDTTGTLYS MARFAGFVDE KGDFAGQYFA
FMSDASAIVI GSLLGTSPVT VFIESSTGIR EGGRTGLTAI TVAVYFLLAM FFTPLLASIP
AWAVGPPLIL VGVMMMKSVT EIDWEDMREA IPAFVTMILM PLTYSVAYGL IGGIGSYVVL
HLWDWGEEGL VKLGFLKRKV KEEDNNNGVV KASEIDTTV
