SRO1_ARATH
ID SRO1_ARATH Reviewed; 568 AA.
AC O82289; Q940B2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Probable inactive poly [ADP-ribose] polymerase SRO1;
DE AltName: Full=Protein SIMILAR TO RCD ONE 1;
GN Name=SRO1; Synonyms=CEO2; OrderedLocusNames=At2g35510; ORFNames=T32F12.11;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 FUNCTION, INTERACTION WITH DREB2A; DREB2B; DREB2C AND NAC082, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19548978; DOI=10.1111/j.1365-313x.2009.03951.x;
RA Jaspers P., Blomster T., Brosche M., Salojaervi J., Ahlfors R.,
RA Vainonen J.P., Reddy R.A., Immink R., Angenent G., Turck F., Overmyer K.,
RA Kangasjaervi J.;
RT "Unequally redundant RCD1 and SRO1 mediate stress and developmental
RT responses and interact with transcription factors.";
RL Plant J. 60:268-279(2009).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19625634; DOI=10.1104/pp.109.142786;
RA Teotia S., Lamb R.S.;
RT "The paralogous genes RADICAL-INDUCED CELL DEATH1 and SIMILAR TO RCD ONE1
RT have partially redundant functions during Arabidopsis development.";
RL Plant Physiol. 151:180-198(2009).
RN [6]
RP INDUCTION.
RX PubMed=20226034; DOI=10.1186/1471-2164-11-170;
RA Jaspers P., Overmyer K., Wrzaczek M., Vainonen J.P., Blomster T.,
RA Salojaervi J., Reddy R.A., Kangasjaervi J.;
RT "The RST and PARP-like domain containing SRO protein family: analysis of
RT protein structure, function and conservation in land plants.";
RL BMC Genomics 11:170-170(2010).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=20009514; DOI=10.4161/psb.5.2.10400;
RA Teotia S., Muthuswamy S., Lamb R.S.;
RT "Radical-induced cell death1 and similar to RCD one1 and the stress-induced
RT morphogenetic response.";
RL Plant Signal. Behav. 5:143-145(2010).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21172813; DOI=10.1093/jxb/erq363;
RA Teotia S., Lamb R.S.;
RT "RCD1 and SRO1 are necessary to maintain meristematic fate in Arabidopsis
RT thaliana.";
RL J. Exp. Bot. 62:1271-1284(2011).
CC -!- FUNCTION: Probable inactive ADP-ribosyltransferase that functions with
CC RCD1 to regulate oxidative stress, hormonal and developmental
CC responses. May regulate some stress-responsive genes. Seems to play a
CC smaller developmental role than R. {ECO:0000269|PubMed:19548978,
CC ECO:0000269|PubMed:19625634, ECO:0000269|PubMed:21172813}.
CC -!- SUBUNIT: Interacts with DREB2A, DREB2B, DREB2C and NAC082.
CC {ECO:0000269|PubMed:19548978}.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:19548978}.
CC Note=Speckle-like pattern.
CC -!- TISSUE SPECIFICITY: Expressed in young developing tissues, such as
CC young leaves and flowers and root tips. In mature plants, expressed in
CC vasculature of leaves and roots. {ECO:0000269|PubMed:19548978,
CC ECO:0000269|PubMed:19625634, ECO:0000269|PubMed:21172813}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryo proper at the globular
CC stage. Expressed in the embryo until the torpedo stage, after which
CC expression within the procambial strands becomes pronounced.
CC {ECO:0000269|PubMed:21172813}.
CC -!- INDUCTION: By salt stress. {ECO:0000269|PubMed:20226034}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC condition. {ECO:0000269|PubMed:19548978, ECO:0000269|PubMed:20009514,
CC ECO:0000269|PubMed:21172813}.
CC -!- CAUTION: Lacks the conserved catalytic triad His-Tyr-Glu of the active
CC site. {ECO:0000305}.
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DR EMBL; AC005314; AAC36170.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09115.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61534.1; -; Genomic_DNA.
DR EMBL; AY056136; AAL07215.1; -; mRNA.
DR EMBL; AY150402; AAN12947.1; -; mRNA.
DR PIR; E84769; E84769.
DR RefSeq; NP_001323747.1; NM_001336558.1.
DR RefSeq; NP_565806.1; NM_129103.5.
DR AlphaFoldDB; O82289; -.
DR SMR; O82289; -.
DR BioGRID; 3462; 5.
DR IntAct; O82289; 5.
DR STRING; 3702.AT2G35510.1; -.
DR PaxDb; O82289; -.
DR PRIDE; O82289; -.
DR ProteomicsDB; 226713; -.
DR EnsemblPlants; AT2G35510.1; AT2G35510.1; AT2G35510.
DR EnsemblPlants; AT2G35510.3; AT2G35510.3; AT2G35510.
DR GeneID; 818116; -.
DR Gramene; AT2G35510.1; AT2G35510.1; AT2G35510.
DR Gramene; AT2G35510.3; AT2G35510.3; AT2G35510.
DR KEGG; ath:AT2G35510; -.
DR Araport; AT2G35510; -.
DR TAIR; locus:2062471; AT2G35510.
DR eggNOG; ENOG502QZEX; Eukaryota.
DR HOGENOM; CLU_027033_1_0_1; -.
DR InParanoid; O82289; -.
DR OMA; ESNCRSH; -.
DR OrthoDB; 458629at2759; -.
DR PhylomeDB; O82289; -.
DR PRO; PR:O82289; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82289; baseline and differential.
DR Genevisible; O82289; AT.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:InterPro.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0010102; P:lateral root morphogenesis; IMP:TAIR.
DR GO; GO:0048573; P:photoperiodism, flowering; IMP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR044964; RCD1/SRO1-5.
DR InterPro; IPR022003; RST.
DR InterPro; IPR004170; WWE-dom.
DR PANTHER; PTHR32263; PTHR32263; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF12174; RST; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS51879; RST; 1.
DR PROSITE; PS50918; WWE; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Nucleus; Reference proteome; Stress response.
FT CHAIN 1..568
FT /note="Probable inactive poly [ADP-ribose] polymerase SRO1"
FT /id="PRO_0000410419"
FT DOMAIN 77..152
FT /note="WWE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT DOMAIN 245..463
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT DOMAIN 497..568
FT /note="RST"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01227"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 409
FT /note="E -> K (in Ref. 3; AAL07215)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 568 AA; 64137 MW; B46C7E81FF72B6F5 CRC64;
MEAKIVKVSD SSYKDGLGKK RKHPGNYTPY DSGRSYAKLQ WVLSPNSSTQ KLEKRRNLDG
ENKVIVSENH VEKSLVRYFS YYKKTGVPKR VMFHENGEWI DLPDHILCDI RNDLEAKRAT
IEFNWCGRHF LLDFLHMYRL DLETGVKTQL AWIDIAGKCF FPETFDTLER DGCHHIRGED
PEQHDQREIK LHIEIDVNSG ELPRLNLNVV TDESGDNMDD FQAVQRSSNG PNDEASEDSC
SRELDDAVEK WDKTETDRFS GVKPAEEELD KDAVKQMFAL GAATLGHVES LDVYQFSSEI
AKARLSLFQK QADITKKHRG DANIRYAWVP AKKEVLSAVM MHGLGVGGAF IKKSMYGVGV
HAANCPYFSA RYCDIDDNGV RHMVLCRVIM GNMEPLRGDN TQYFTGGEEY DNGVDDVESP
KHYLIWNMNM NTHIYPEFVV SFKLSIPNAE GNILPTTQSR HESSGLTLEG PKGSPSNEPG
RVSNGGSGSE KNSSSSRRPR SPIMPFPLLF KAISSKIARK DMDLIIAGYQ ELREKKVSRK
EFYKTLSMIV GDDDLLISTI TGLQRSLG
