RIN2_ARATH
ID RIN2_ARATH Reviewed; 578 AA.
AC Q8VYC8; A6XER5; Q9SB40;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=E3 ubiquitin protein ligase RIN2;
DE EC=2.3.2.27;
DE AltName: Full=AMF receptor-like protein 1A;
DE AltName: Full=RING-type E3 ubiquitin transferase RIN2 {ECO:0000305};
DE AltName: Full=RPM1-interacting protein 2;
GN Name=RIN2; Synonyms=AMFR-1A; OrderedLocusNames=At4g25230;
GN ORFNames=F24A6.70;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 NUCLEOTIDE SEQUENCE [MRNA] OF 314-577.
RC STRAIN=cv. Columbia;
RA Fu H.;
RT "Functional differentiation of ubiquitin-interacting factors from
RT Arabidopsis.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RPM1, INDUCTION,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-337.
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 RIN3. 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 -!- INDUCTION: Repressed upon infection with the P.syringae avirulent
CC DC3000 strains containing avrRpm1 or avrRpt2 (at protein level).
CC {ECO:0000269|PubMed:16212605}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:16212605}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA23064.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81334.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035396; CAA23064.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161563; CAB81334.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85028.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85029.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66650.1; -; Genomic_DNA.
DR EMBL; AY072178; AAL60000.1; -; mRNA.
DR EMBL; DQ677669; ABG85249.1; -; mRNA.
DR RefSeq; NP_001328533.1; NM_001341724.1.
DR RefSeq; NP_194253.2; NM_118655.4.
DR RefSeq; NP_849552.1; NM_179221.2.
DR AlphaFoldDB; Q8VYC8; -.
DR SMR; Q8VYC8; -.
DR BioGRID; 13913; 4.
DR STRING; 3702.AT4G25230.1; -.
DR PaxDb; Q8VYC8; -.
DR PRIDE; Q8VYC8; -.
DR ProteomicsDB; 236866; -.
DR EnsemblPlants; AT4G25230.1; AT4G25230.1; AT4G25230.
DR EnsemblPlants; AT4G25230.2; AT4G25230.2; AT4G25230.
DR EnsemblPlants; AT4G25230.3; AT4G25230.3; AT4G25230.
DR GeneID; 828626; -.
DR Gramene; AT4G25230.1; AT4G25230.1; AT4G25230.
DR Gramene; AT4G25230.2; AT4G25230.2; AT4G25230.
DR Gramene; AT4G25230.3; AT4G25230.3; AT4G25230.
DR KEGG; ath:AT4G25230; -.
DR Araport; AT4G25230; -.
DR TAIR; locus:2122674; AT4G25230.
DR eggNOG; KOG0802; Eukaryota.
DR HOGENOM; CLU_029305_1_0_1; -.
DR InParanoid; Q8VYC8; -.
DR OMA; NPADAVW; -.
DR OrthoDB; 897451at2759; -.
DR PhylomeDB; Q8VYC8; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8VYC8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8VYC8; baseline and differential.
DR Genevisible; Q8VYC8; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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:0004842; F:ubiquitin-protein transferase activity; IDA:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR GO; GO:0034052; P:positive regulation of plant-type hypersensitive response; IGI:TAIR.
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; SM00184; RING; 1.
DR PROSITE; PS51140; CUE; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Hypersensitive response; Membrane; Metal-binding; Plant defense;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..578
FT /note="E3 ubiquitin protein ligase RIN2"
FT /id="PRO_0000395753"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 538..578
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 REGION 504..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 337
FT /note="C->A: Loss of E3 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:16212605"
SQ SEQUENCE 578 AA; 64564 MW; 13593FF338CE73C1 CRC64;
MGIKYLPVSV ASTALSFVGL QVWTELSLDR LRADGLIAKN ISLGDSEHAL ELLLGSYFTI
ALLTNFVLNV YILLVLSLKT LFFGDLYDVE TKKLVERLAN YIIYKGTFLP LVIPPTIFQG
VLWTVWLTVL CTLKMFQALA RDRLERLNAS PSSTPWTYFR VYSVLFLVLS VDMFWIKLSL
MTYNTIGSAV YLLLLFEPCS IAFETLQALL IHGFQLLDMW INHLAVKNSD CQRSKFIDSM
TAGSLLEWKG LLNRNLGFFL DMATLVMALG HYLHIWWLHG IAFHLVDAVL FLNIRALLSA
ILKRIKGYIK LRIALGALHA ALPDATSEEL RAYDDECAIC REPMAKAKRL HCNHLFHLGC
LRSWLDQGLN EVYSCPTCRK PLFVGRTENE VNPRTVEVSS DEQLARQLER QNNPVHALAT
GLFPAEVPDS VENDTSRNLG LDPSWLQTWS SQGSDVAGPS TTSRTVGLGR VQMMMRHLAS
VGESYAQTAL DDAAWSLWPM NPSQASTSST TVPPGNGGRT GGLHLRTVSN TTNESLTNIL
AMAETVREVM PHVPDEIIFQ DLQRTNSVAV TVNNLLQM
