SR1P1_ARATH
ID SR1P1_ARATH Reviewed; 604 AA.
AC Q66GP0; F4K3Q2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=BTB/POZ domain-containing protein SR1IP1 {ECO:0000305};
DE AltName: Full=Protein ATSR1-INTERACTION PROTEIN 1 {ECO:0000303|PubMed:24528504};
GN Name=SR1IP1 {ECO:0000303|PubMed:24528504};
GN OrderedLocusNames=At5g67385 {ECO:0000312|EMBL:AED98336.1};
GN ORFNames=K8K14 {ECO:0000312|EMBL:AB007645};
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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].
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 DOMAIN BTB.
RX PubMed=15749712; DOI=10.1074/jbc.m413247200;
RA Gingerich D.J., Gagne J.M., Salter D.W., Hellmann H., Estelle M., Ma L.,
RA Vierstra R.D.;
RT "Cullins 3a and 3b assemble with members of the broad
RT complex/tramtrack/bric-a-brac (BTB) protein family to form essential
RT ubiquitin-protein ligases (E3s) in Arabidopsis.";
RL J. Biol. Chem. 280:18810-18821(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP FUNCTION, INTERACTION WITH CAMTA3 AND CUL3A, AND DISRUPTION PHENOTYPE.
RX PubMed=24528504; DOI=10.1111/tpj.12473;
RA Zhang L., Du L., Shen C., Yang Y., Poovaiah B.W.;
RT "Regulation of plant immunity through ubiquitin-mediated modulation of
RT Ca(2+) -calmodulin-AtSR1/CAMTA3 signaling.";
RL Plant J. 78:269-281(2014).
CC -!- FUNCTION: Acts as a substrate-specific adapter of an E3 ubiquitin-
CC protein ligase complex (CUL3-RBX1-BTB) which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins (Probable). Involved in disease resistance. Acts as a
CC substrate adapter that recruits CAMTA3/SR1 for ubiquitination and
CC degradation during pathogen infection. Acts as positive regulator of
CC plant defense by removing the defense suppressor CAMTA3/SR1
CC (PubMed:24528504). {ECO:0000269|PubMed:24528504,
CC ECO:0000305|PubMed:24528504}.
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with CAMTA3 and CUL3A.
CC {ECO:0000269|PubMed:24528504}.
CC -!- DOMAIN: The BTB/POZ domain mediates the interaction with some component
CC of ubiquitin ligase complexes. {ECO:0000269|PubMed:15749712}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants exhibit enhanced susceptibility to the
CC bacterial virulent pathogen Pseudomonas syringae pv tomato strain
CC DC3000. {ECO:0000269|PubMed:24528504}.
CC -!- SIMILARITY: Belongs to the NPH3 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00982}.
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DR EMBL; AB007645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED98336.1; -; Genomic_DNA.
DR EMBL; BT015362; AAU05485.1; -; mRNA.
DR EMBL; BT015895; AAU95431.1; -; mRNA.
DR EMBL; BX829802; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_680473.2; NM_148168.4.
DR AlphaFoldDB; Q66GP0; -.
DR SMR; Q66GP0; -.
DR BioGRID; 22116; 3.
DR IntAct; Q66GP0; 1.
DR STRING; 3702.AT5G67385.1; -.
DR iPTMnet; Q66GP0; -.
DR PaxDb; Q66GP0; -.
DR PRIDE; Q66GP0; -.
DR ProteomicsDB; 226764; -.
DR EnsemblPlants; AT5G67385.1; AT5G67385.1; AT5G67385.
DR GeneID; 836874; -.
DR Gramene; AT5G67385.1; AT5G67385.1; AT5G67385.
DR KEGG; ath:AT5G67385; -.
DR Araport; AT5G67385; -.
DR TAIR; locus:504954965; AT5G67385.
DR eggNOG; ENOG502QUFV; Eukaryota.
DR HOGENOM; CLU_005994_6_0_1; -.
DR InParanoid; Q66GP0; -.
DR OrthoDB; 298243at2759; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q66GP0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q66GP0; baseline and differential.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009904; P:chloroplast accumulation movement; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR043454; NPH3/RPT2-like.
DR InterPro; IPR027356; NPH3_dom.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR32370; PTHR32370; 1.
DR Pfam; PF03000; NPH3; 1.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS51649; NPH3; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Phosphoprotein; Plant defense; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..604
FT /note="BTB/POZ domain-containing protein SR1IP1"
FT /id="PRO_0000409588"
FT DOMAIN 27..96
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT DOMAIN 201..474
FT /note="NPH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00982"
FT REGION 478..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 500..541
FT /evidence="ECO:0000255"
FT COMPBIAS 541..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 415
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9FMF5"
FT CONFLICT 247
FT /note="L -> S (in Ref. 3; AAU05485/AAU95431)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="D -> N (in Ref. 4; BX829802)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 604 AA; 67559 MW; 7DBC3E7923FCDA63 CRC64;
MSAKKKDLLS SAMKRTSEWI SSQEVSSDVT VHVGEASFSL HKFPLMSKCG FIKKLVSESS
KDSDSTVIKI PDIPGGSEAF ELAAKFCYGI NFDMSTENIA MLRCAAEYLE MTEEHSVENL
VVRAEAYLNE VALKSLSSSI TVLHKSEKLL PIAERVKLVS RCIDAIAYMT CQESHFCSPS
SSNSGNNEVV VQQQSKQPVV DWWAEDLTVL RIDSFQRVLI AMMARGFKQY GLGPVLMLYA
QKSLRGLEIF GKGMKKIEPK QEHEKRVILE TIVSLLPREK NAMSVSFLSM LLRAAIFLET
TVACRLDLEN RMGLQLGQAV LDDLLIPSYS FTGDHSMFDT DTVQRILMNY LEFEVEGVRL
SNNGVDLAGD MERVGKLLEN YMAEIASDRN VSLQKFIGLA ELIPEQSRVT EDGMYRAVDI
YLKAHPNMSD VERKKVCSLM DCQKLSREAC AHAAQNDRLP VQTIVQVLYY EQQRLRGEVT
NDSDSPAPPP PQPAAVLPPK LSSYTDELSK LKRENQDLKL ELLKMKMKLK EFEKESEKKT
SSSTISTNPS SPISTASTGK PPLPRKSFIN SVSKKLGKLN PFSITPYNGR GRTKPPKDRR
HSIS
