RIN3_ARATH
ID RIN3_ARATH Reviewed; 577 AA.
AC Q8W4Q5; Q9FGM8;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=E3 ubiquitin protein ligase RIN3;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase RIN3 {ECO:0000305};
DE AltName: Full=RPM1-interacting protein 3;
GN Name=RIN3; OrderedLocusNames=At5g51450; ORFNames=MFG13.16;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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, SUBCELLULAR LOCATION, INTERACTION WITH RPM1, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=16212605; DOI=10.1111/j.1365-313x.2005.02525.x;
RA Kawasaki T., Nam J., Boyes D.C., Holt B.F. III, Hubert D.A., Wiig A.,
RA Dangl J.L.;
RT "A duplicated pair of Arabidopsis RING-finger E3 ligases contribute to the
RT RPM1- and RPS2-mediated hypersensitive response.";
RL Plant J. 44:258-270(2005).
CC -!- FUNCTION: E3 ubiquitin protein ligase that acts as positive regulator
CC of RPM1- and RPS2-dependent hypersensitive response (HR), in
CC association with RIN2. Probably not required for RPM1 degradation
CC during HR. {ECO:0000269|PubMed:16212605}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts (via C-terminus) with RPM1 (via N-terminus).
CC {ECO:0000269|PubMed:16212605}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16212605}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:16212605}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8W4Q5-1; Sequence=Displayed;
CC -!- INDUCTION: Repressed upon infection with the P.syringae avirulent
CC DC3000 strain containing avrRpm1 (at protein level).
CC {ECO:0000269|PubMed:16212605}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:16212605}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09756.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB025621; BAB09756.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96082.1; -; Genomic_DNA.
DR EMBL; AY062101; AAL32977.1; -; mRNA.
DR RefSeq; NP_568760.1; NM_124524.2. [Q8W4Q5-1]
DR AlphaFoldDB; Q8W4Q5; -.
DR SMR; Q8W4Q5; -.
DR BioGRID; 20464; 3.
DR STRING; 3702.AT5G51450.2; -.
DR PaxDb; Q8W4Q5; -.
DR ProteomicsDB; 237005; -. [Q8W4Q5-1]
DR EnsemblPlants; AT5G51450.1; AT5G51450.1; AT5G51450. [Q8W4Q5-1]
DR GeneID; 835219; -.
DR Gramene; AT5G51450.1; AT5G51450.1; AT5G51450. [Q8W4Q5-1]
DR KEGG; ath:AT5G51450; -.
DR Araport; AT5G51450; -.
DR eggNOG; KOG0802; Eukaryota.
DR HOGENOM; CLU_029305_1_0_1; -.
DR InParanoid; Q8W4Q5; -.
DR OMA; FLYIWWL; -.
DR PhylomeDB; Q8W4Q5; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8W4Q5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8W4Q5; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR GO; GO:0034052; P:positive regulation of plant-type hypersensitive response; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd14422; CUE_RIN3_plant; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR035667; RIN3_plant_CUE.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF02845; CUE; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00546; CUE; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS51140; CUE; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hypersensitive response; Membrane; Metal-binding;
KW Plant defense; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..577
FT /note="E3 ubiquitin protein ligase RIN3"
FT /id="PRO_0000395754"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 537..577
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT ZN_FING 337..379
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT CONFLICT 218
FT /note="D -> E (in Ref. 3; AAL32977)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 577 AA; 64518 MW; 3B3B1B1A8D405B78 CRC64;
MGITYLHISV ATTALSFVGL QVWTELSLDR LRADGIITKN ISLGNSENTL ELLLSSHTTI
ALLASFVLNI YILLVLSLKT LFFGDLYAIE TRKLVERLAN YIIYKGTFLP FVVPRTVFQG
VLWTIWLTVL CTLKMFQALA RDRLDRLNAS PSSTPWTYFR VYSALFMVLS TDLCWIKLSL
MIYNTVGSSV YLLLLFEPCG IAFETLQALL IHGFQLLDMW INHLAVKNSD CQRSKFYDSM
TAGSLLEWKG LLNRNLGFFL DMATLVMALG HYLHIWWLHG MAFHLVDAVL FLNIRALLSS
ILKRIKGYIK LRVALGALHA ALLDATSEEL RDYDDECAIC REPMAKAKRL HCNHLFHLGC
LRSWLDQGLN EVYSCPTCRK PLFVGRTESE ANPSRGEVSS DEHLARQFER QNNSVHALTT
GMFPTETPNF TESDPWRNSE VDPSWLQTWS DQGVDVVGSS AGSRSVGLGQ VQLMMRHLAS
VGEGSAQTTL DDASWGLWPM NPSQASTSST YVPPGAGGRT GGLHLRTVSR AANNMASILA
MAETVREVLP HVPDEIIFQD LQRTNSVSVT VNNLLQM
