ID SRG1_ARATH Reviewed; 358 AA. AC Q39224; DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 132. DE RecName: Full=Protein SRG1; DE Short=AtSRG1; DE AltName: Full=Protein SENESCENCE-RELATED GENE 1; GN Name=SRG1; OrderedLocusNames=At1g17020; ORFNames=F20D23.28, F6I1.30; 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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=cv. C24; RX PubMed=9414552; DOI=10.1104/pp.115.4.1385; RA Callard D., Mazzolini L.; RT "Identification of proliferation-induced genes in Arabidopsis thaliana. RT Characterization of a new member of the highly evolutionarily conserved RT histone H2A.F/Z variant subfamily."; RL Plant Physiol. 115:1385-1395(1997). RN [2] 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 [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 INDUCTION BY VIRUS INFECTION. RX PubMed=12535341; DOI=10.1046/j.1365-313x.2003.01625.x; RA Whitham S.A., Quan S., Chang H.S., Cooper B., Estes B., Zhu T., Wang X., RA Hou Y.M.; RT "Diverse RNA viruses elicit the expression of common sets of genes in RT susceptible Arabidopsis thaliana plants."; RL Plant J. 33:271-283(2003). CC -!- TISSUE SPECIFICITY: Low expression in roots and leaves. CC {ECO:0000269|PubMed:9414552}. CC -!- DEVELOPMENTAL STAGE: Highly induced during normal senescence. CC {ECO:0000269|PubMed:9414552}. CC -!- INDUCTION: By virus infection. {ECO:0000269|PubMed:12535341}. CC -!- MISCELLANEOUS: Unlike the homologous protein NCS1 of Coptis japonica, CC SRG1 has no norcoclaurine synthase activity. CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X79052; CAA55654.1; -; mRNA. DR EMBL; AC007651; AAD50032.1; -; Genomic_DNA. DR EMBL; CP002684; AEE29531.1; -; Genomic_DNA. DR EMBL; AY048302; AAK82564.1; -; mRNA. DR EMBL; AY139794; AAM98100.1; -; mRNA. DR PIR; S44261; S44261. DR RefSeq; NP_173145.1; NM_101562.4. DR AlphaFoldDB; Q39224; -. DR SMR; Q39224; -. DR STRING; 3702.Q39224; -. DR PaxDb; 3702-AT1G17020-1; -. DR ProteomicsDB; 226728; -. DR EnsemblPlants; AT1G17020.1; AT1G17020.1; AT1G17020. DR GeneID; 838272; -. DR Gramene; AT1G17020.1; AT1G17020.1; AT1G17020. DR KEGG; ath:AT1G17020; -. DR Araport; AT1G17020; -. DR TAIR; AT1G17020; SRG1. DR eggNOG; KOG0143; Eukaryota. DR HOGENOM; CLU_010119_16_0_1; -. DR InParanoid; Q39224; -. DR OMA; FHTSKHD; -. DR OrthoDB; 1057251at2759; -. DR PhylomeDB; Q39224; -. DR BioCyc; ARA:AT1G17020-MONOMER; -. DR PRO; PR:Q39224; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q39224; baseline and differential. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; ISS:TAIR. DR GO; GO:0010150; P:leaf senescence; IEP:TAIR. DR InterPro; IPR026992; DIOX_N. DR InterPro; IPR044861; IPNS-like_FE2OG_OXY. DR InterPro; IPR027443; IPNS-like_sf. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR PANTHER; PTHR47991:SF224; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1. DR PANTHER; PTHR47991; OXOGLUTARATE/IRON-DEPENDENT DIOXYGENASE; 1. DR Pfam; PF03171; 2OG-FeII_Oxy; 1. DR Pfam; PF14226; DIOX_N; 1. DR SUPFAM; SSF51197; Clavaminate synthase-like; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. DR Genevisible; Q39224; AT. PE 2: Evidence at transcript level; KW Iron; Metal-binding; Oxidoreductase; Reference proteome. FT CHAIN 1..358 FT /note="Protein SRG1" FT /id="PRO_0000358940" FT DOMAIN 209..309 FT /note="Fe2OG dioxygenase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT BINDING 233 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT BINDING 235 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT BINDING 290 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" SQ SEQUENCE 358 AA; 41039 MW; DFEEF51DE9FB69E1 CRC64; MEAKGAAQWS SILVPSVQEM VKEKTITTVP PRYVRSDQDK TEVDDDFDVK IEIPIIDMKR LCSSTTMDSE VEKLDFACKE WGFFQLVNHG IDSSFLDKVK SEIQDFFNLP MEEKKKFWQR PDEIEGFGQA FVVSEDQKLD WADLFFHTVQ PVELRKPHLF PKLPLPFRDT LEMYSSEVQS VAKILIAKMA RALEIKPEEL EKLFDDVDSV QSMRMNYYPP CPQPDQVIGL TPHSDSVGLT VLMQVNDVEG LQIKKDGKWV PVKPLPNAFI VNIGDVLEII TNGTYRSIEH RGVVNSEKER LSIATFHNVG MYKEVGPAKS LVERQKVARF KRLTMKEYND GLFSRTLDGK AYLDALRI //