ID   RKP_ARATH               Reviewed;        1280 AA.
AC   Q9SIZ8;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=E3 ubiquitin-protein ligase RKP;
DE            Short=AtKPC1;
DE            EC=2.3.2.27;
DE   AltName: Full=Protein RELATED TO KPC1;
DE   AltName: Full=RING-type E3 ubiquitin transferase RKP {ECO:0000305};
GN   Name=RKP; Synonyms=KPC1; OrderedLocusNames=At2g22010; ORFNames=F7D8.33;
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;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18005227; DOI=10.1111/j.1365-313x.2007.03370.x;
RA   Ren H., Santner A., del Pozo J.C., Murray J.A., Estelle M.;
RT   "Degradation of the cyclin-dependent kinase inhibitor KRP1 is regulated by
RT   two different ubiquitin E3 ligases.";
RL   Plant J. 53:705-716(2008).
RN   [5]
RP   FUNCTION, INDUCTION BY BEET SEVERE CURLY TOP VIRUS C4, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=19000158; DOI=10.1111/j.1365-313x.2008.03737.x;
RA   Lai J., Chen H., Teng K., Zhao Q., Zhang Z., Li Y., Liang L., Xia R.,
RA   Wu Y., Guo H., Xie Q.;
RT   "RKP, a RING finger E3 ligase induced by BSCTV C4 protein, affects
RT   geminivirus infection by regulation of the plant cell cycle.";
RL   Plant J. 57:905-917(2009).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that promotes the ubiquitination
CC       and proteasomal degradation of KRP1 and KRP2.
CC       {ECO:0000269|PubMed:18005227, ECO:0000269|PubMed:19000158}.
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
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=Q9SIZ8-1; Sequence=Displayed;
CC   -!- INDUCTION: Induced by the beet severe curly top virus (BSCTV) C4
CC       protein and by BSCTV infection. {ECO:0000269|PubMed:19000158}.
CC   -!- DISRUPTION PHENOTYPE: No defects in growth and development, but reduced
CC       susceptibility to beet severe curly top virus infection.
CC       {ECO:0000269|PubMed:18005227, ECO:0000269|PubMed:19000158}.
CC   -!- MISCELLANEOUS: Favors geminivirus replication by up-regulating the host
CC       cell cycle.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD20418.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AK230019; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AC007019; AAD20418.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC07251.1; -; Genomic_DNA.
DR   EMBL; AK230019; -; NOT_ANNOTATED_CDS; mRNA.
DR   PIR; H84607; H84607.
DR   RefSeq; NP_850020.1; NM_179689.3. [Q9SIZ8-1]
DR   AlphaFoldDB; Q9SIZ8; -.
DR   SMR; Q9SIZ8; -.
DR   BioGRID; 2090; 6.
DR   STRING; 3702.AT2G22010.2; -.
DR   iPTMnet; Q9SIZ8; -.
DR   PaxDb; Q9SIZ8; -.
DR   ProteomicsDB; 234814; -. [Q9SIZ8-1]
DR   EnsemblPlants; AT2G22010.1; AT2G22010.1; AT2G22010. [Q9SIZ8-1]
DR   GeneID; 816737; -.
DR   Gramene; AT2G22010.1; AT2G22010.1; AT2G22010. [Q9SIZ8-1]
DR   KEGG; ath:AT2G22010; -.
DR   Araport; AT2G22010; -.
DR   eggNOG; KOG2242; Eukaryota.
DR   eggNOG; KOG4692; Eukaryota.
DR   InParanoid; Q9SIZ8; -.
DR   PRO; PR:Q9SIZ8; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SIZ8; baseline and differential.
DR   Genevisible; Q9SIZ8; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR   GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:InterPro.
DR   GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR   GO; GO:0030163; P:protein catabolic process; IMP:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd12882; SPRY_RNF123; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR045737; RKP_N.
DR   InterPro; IPR045129; RNF123/RSPRY1-like.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR035773; SPRY_RNF123.
DR   InterPro; IPR019474; Ub_conjug_fac_E4_core.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13363; PTHR13363; 1.
DR   Pfam; PF19322; RKP_N; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF10408; Ufd2P_core; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Membrane; Metal-binding; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..1280
FT                   /note="E3 ubiquitin-protein ligase RKP"
FT                   /id="PRO_0000395752"
FT   TRANSMEM        551..571
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        834..854
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          82..269
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   ZN_FING         1217..1252
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          669..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        704..718
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1280 AA;  144499 MW;  87F1522A36A2A9C5 CRC64;
     MAEDSLRVGM ISSGLAVLLN GEDAKENSSK ARIVPHFDYS GHRPLERTIE FIFGLAEKSV
     GPLDGQVDSS LIRAVIKNQF SKLHGDLDVS VSQREGISVV HHGVGPPIVG LEEFSICGDI
     RIVKPPLVLE SLALFSSARA NACIWKGKWM YEVALETSGI QQLGWATLAC PFTDQKGVGD
     ADDSYAFDGR RVSKWNKEAE PYGQSWVAGD VIGCCIDLNC DEIYFYRNGV SLGAAFTGIR
     KLGPGFGYYP AISLSQGERC ELNFGAYPFK YPVDGFQPLQ EAPTRFSFAT ELLRCFSRLL
     DRPDRSLADT LSRLRRFASV EELFCPVSSA ICDEFFYILE QDPLLAEYLG RGAFLSFLLE
     TFRTQAPHDS SSLDKVLDVF LEFPQSHLIF EHVVNALACG CKTATLILTE CPYSGPYPYL
     ALACHLFKRE ELMVQWWRSL HFEFLFEGFL SCRSSNKHDL QHLMPVVWWP GSSEDISYES
     SMGFTISALS EAINKIEEKQ RNLCLLVIQF IPPVSPPQLP GSAFRGFLQN LLLKNRGADR
     TLAPSGVTRN SVLVSLFSVI LHFLSEGFAM LKSSEAVHHN VGFLHRGGQQ KFPLSLFLKN
     DPHRADITRL GGLFSHISKS YPTDDQEEEI MRWEEGCMDD EQNRVTHATE QKPCCCLAYD
     TDLTKSLKDR GKNTAQSSRG RCSSIPERSS HVAAECSAGS FSEEIDDKPS TSNQSDPDFG
     YRPVRFMRTA LQESRISSAI LSEEELLDAL LLLYHIAVAP NFKQASYYMS HQSQSISLLE
     ETDKQIRERA SCDQIKRLKE ARNNYKEDVM DCVRHSAWFR ISLFSRWKQR GMYALCMWVV
     QLLLVLSKMD SVFVYIPEFY LESLVDCFHV LRKSDPPFVP STTFIKQGLS SFITFVVTHF
     NDSRISNTDL KDLLLQSISV LVQYKEYLEA FENNEAATRH MPAALLAAFD NRSWIPVTNI
     FLRLCKGSGF SSLKNGESSF SSTVFQALLR DACINDGELL STFLNRLFNT LSWTITEFSV
     SVREMQEKYQ VMEFQQRKCC VIFELSSNLA RVLEFCTYAM PQAFLAGTDT NLRRLTELIL
     FILNHMTSAV DDEFFDLSLR RQGQPSEKVS RGILLAPLVG IILNLLEASE DSKPKQQHDV
     IGLFASMDCP DTVYYGFQYL LEYNWDGCVS GDDAYVKKLG QLENFLSHLI NRASSQEPER
     KEESFNKDTT DIEDNTCCIC YAGEANAMIA PCSHRSCYGC ITRHLLNCQR CFFCNATVID
     VIRDKEEEEE EDDDGHKRST