SRO5_ARATH
ID SRO5_ARATH Reviewed; 309 AA.
AC Q9FJJ3; F4K6I7; Q8LCY5;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable inactive poly [ADP-ribose] polymerase SRO5;
DE AltName: Full=Protein SIMILAR TO RCD ONE 5;
GN Name=SRO5; OrderedLocusNames=At5g62520; ORFNames=K19B1.13;
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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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] (ISOFORM 1).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP SUBCELLULAR LOCATION, SUBUNIT, AND 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).
CC -!- FUNCTION: Probable inactive ADP-ribosyltransferase that may be involved
CC in stress and developmental responses. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with dehydration-responsive DREB2 proteins and a
CC number of transcription factors belonging to several protein families.
CC {ECO:0000269|PubMed:20226034}.
CC -!- INTERACTION:
CC Q9FJJ3; O80575: At2g44050; NbExp=3; IntAct=EBI-4434999, EBI-4473692;
CC Q9FJJ3; Q38830: IAA12; NbExp=3; IntAct=EBI-4434999, EBI-617608;
CC Q9FJJ3; Q9FLR1: MYB29; NbExp=3; IntAct=EBI-4434999, EBI-15410392;
CC Q9FJJ3; O23160: MYB73; NbExp=3; IntAct=EBI-4434999, EBI-25506855;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:20226034}.
CC Note=Speckle-like pattern.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FJJ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FJJ3-2; Sequence=VSP_041442, VSP_041443;
CC -!- INDUCTION: By salt stress and light. {ECO:0000269|PubMed:20226034}.
CC -!- CAUTION: Lacks the conserved catalytic triad His-Tyr-Glu of the active
CC site. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX831989; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AB015469; BAB11502.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97617.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97618.1; -; Genomic_DNA.
DR EMBL; AF446893; AAL38626.1; -; mRNA.
DR EMBL; AY052687; AAK96591.1; -; mRNA.
DR EMBL; BX831989; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY086327; AAM64396.1; -; mRNA.
DR RefSeq; NP_201058.1; NM_125646.3. [Q9FJJ3-1]
DR RefSeq; NP_974981.1; NM_203252.1. [Q9FJJ3-2]
DR AlphaFoldDB; Q9FJJ3; -.
DR SMR; Q9FJJ3; -.
DR BioGRID; 21616; 4.
DR IntAct; Q9FJJ3; 6.
DR STRING; 3702.AT5G62520.1; -.
DR PaxDb; Q9FJJ3; -.
DR PRIDE; Q9FJJ3; -.
DR EnsemblPlants; AT5G62520.1; AT5G62520.1; AT5G62520. [Q9FJJ3-1]
DR EnsemblPlants; AT5G62520.2; AT5G62520.2; AT5G62520. [Q9FJJ3-2]
DR GeneID; 836372; -.
DR Gramene; AT5G62520.1; AT5G62520.1; AT5G62520. [Q9FJJ3-1]
DR Gramene; AT5G62520.2; AT5G62520.2; AT5G62520. [Q9FJJ3-2]
DR KEGG; ath:AT5G62520; -.
DR Araport; AT5G62520; -.
DR TAIR; locus:2154084; AT5G62520.
DR eggNOG; ENOG502QTKK; Eukaryota.
DR HOGENOM; CLU_062533_0_0_1; -.
DR InParanoid; Q9FJJ3; -.
DR OMA; HMNSYVF; -.
DR OrthoDB; 948541at2759; -.
DR PhylomeDB; Q9FJJ3; -.
DR PRO; PR:Q9FJJ3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJJ3; baseline and differential.
DR Genevisible; Q9FJJ3; AT.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:InterPro.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR044964; RCD1/SRO1-5.
DR InterPro; IPR022003; RST.
DR PANTHER; PTHR32263; PTHR32263; 1.
DR Pfam; PF12174; RST; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS51879; RST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Nucleus; Reference proteome;
KW Stress response.
FT CHAIN 1..309
FT /note="Probable inactive poly [ADP-ribose] polymerase SRO5"
FT /id="PRO_0000410423"
FT DOMAIN 28..255
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT DOMAIN 238..309
FT /note="RST"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01227"
FT VAR_SEQ 236..241
FT /note="SPKRLR -> KQNQNL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_041442"
FT VAR_SEQ 242..309
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_041443"
FT CONFLICT 56
FT /note="Y -> F (in Ref. 5; AAM64396)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="D -> H (in Ref. 5; AAM64396)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="P -> L (in Ref. 5; AAM64396)"
FT /evidence="ECO:0000305"
FT CONFLICT 253
FT /note="A -> T (in Ref. 5; AAM64396)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 34623 MW; 9A55475A239E2968 CRC64;
MDYVRTQVEA VFDDSEQDGS TISESGSCDS SSDRSFADEL GLMELLEGDK AHDLIYRNCK
SGLGDQCQIL SVLRNGFRNV GSRAKLKTFQ VFQEAVQMKH GGDGGAKVKY GWCSVSKHEL
KTIFEYGFSE PLRNDGSFGR GLYLSPDNSP LDCLKDSASE SEDGMRFLLL CRVLLGKSEI
VPQGSTRSCP SSPEFDSGVD DLVSTKKYIV WSTHMNTHVL PEFLVCIKAP FNLTRSPKRL
RSPWMAFPVL IKALSKFLPP SQILVIQKHY KDQQNRRITR SELIQRVRSI TGDKLLVHII
KACGHKVQH
