SRG1_ARATH
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 03-AUG-2022, entry version 126.
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}.
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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.AT1G17020.1; -.
DR PaxDb; Q39224; -.
DR PRIDE; Q39224; -.
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; locus:2020407; AT1G17020.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_0_1; -.
DR InParanoid; Q39224; -.
DR OMA; FHTSKHD; -.
DR OrthoDB; 1005149at2759; -.
DR PhylomeDB; Q39224; -.
DR BioCyc; ARA:AT1G17020-MON; -.
DR PRO; PR:Q39224; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q39224; baseline and differential.
DR Genevisible; Q39224; AT.
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 Gene3D; 2.60.120.330; -; 1.
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 Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
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
