RFP2_SCHPO
ID RFP2_SCHPO Reviewed; 205 AA.
AC Q9UT72;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=E3 ubiquitin-protein ligase complex slx8-rfp subunit rfp2;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 2;
DE AltName: Full=RING-type E3 ubiquitin transferase rfp2 {ECO:0000305};
GN Name=rfp2; ORFNames=SPAC343.18;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, IDENTIFICATION IN A E3
RP UBIQUITIN-PROTEIN LIGASE COMPLEX WITH RFP1 AND SLX8, INTERACTION WITH SLX8,
RP AND SUBCELLULAR LOCATION.
RX PubMed=17762865; DOI=10.1038/sj.emboj.7601838;
RA Prudden J., Pebernard S., Raffa G., Slavin D.A., Perry J.J.P., Tainer J.A.,
RA McGowan C.H., Boddy M.N.;
RT "SUMO-targeted ubiquitin ligases in genome stability.";
RL EMBO J. 26:4089-4101(2007).
RN [4]
RP FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, AND SUBCELLULAR LOCATION.
RX PubMed=17762864; DOI=10.1038/sj.emboj.7601839;
RA Sun H., Leverson J.D., Hunter T.;
RT "Conserved function of RNF4 family proteins in eukaryotes: targeting a
RT ubiquitin ligase to SUMOylated proteins.";
RL EMBO J. 26:4102-4112(2007).
RN [5]
RP FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS.
RX PubMed=17502373; DOI=10.1074/jbc.m702652200;
RA Kosoy A., Calonge T.M., Outwin E.A., O'Connell M.J.;
RT "Fission yeast Rnf4 homologs are required for DNA repair.";
RL J. Biol. Chem. 282:20388-20394(2007).
CC -!- FUNCTION: Mediates ubiquitination and subsequent
CC desumoylation/degradation of sumoylated proteins and proteins
CC containing SUMO-like domains. Involved in maintaining genome stability
CC where it acts in the cellular response to DNA damage.
CC {ECO:0000269|PubMed:17502373, ECO:0000269|PubMed:17762864,
CC ECO:0000269|PubMed:17762865}.
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: Part of an E3 ubiquitin complex including rfp1, rfp2 and slx8.
CC Interacts with slx8. {ECO:0000269|PubMed:17762865}.
CC -!- INTERACTION:
CC Q9UT72; P87176: slx8; NbExp=3; IntAct=EBI-7587772, EBI-7588105;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372,
CC ECO:0000269|PubMed:17762864, ECO:0000269|PubMed:17762865}.
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DR EMBL; CU329670; CAB52281.1; -; Genomic_DNA.
DR PIR; T38667; T38667.
DR RefSeq; NP_593439.1; NM_001018872.2.
DR AlphaFoldDB; Q9UT72; -.
DR SMR; Q9UT72; -.
DR BioGRID; 279621; 19.
DR ELM; Q9UT72; -.
DR IntAct; Q9UT72; 4.
DR MINT; Q9UT72; -.
DR STRING; 4896.SPAC343.18.1; -.
DR PaxDb; Q9UT72; -.
DR EnsemblFungi; SPAC343.18.1; SPAC343.18.1:pep; SPAC343.18.
DR GeneID; 2543192; -.
DR KEGG; spo:SPAC343.18; -.
DR PomBase; SPAC343.18; rfp2.
DR VEuPathDB; FungiDB:SPAC343.18; -.
DR eggNOG; KOG0320; Eukaryota.
DR HOGENOM; CLU_1422181_0_0_1; -.
DR InParanoid; Q9UT72; -.
DR OMA; SIFASKC; -.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9UT72; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0033768; C:SUMO-targeted ubiquitin ligase complex; IPI:PomBase.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0006281; P:DNA repair; IGI:PomBase.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0120290; P:stalled replication fork localization to nuclear periphery; IMP:PomBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:PomBase.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF00097; zf-C3HC4; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..205
FT /note="E3 ubiquitin-protein ligase complex slx8-rfp subunit
FT rfp2"
FT /id="PRO_0000358873"
FT ZN_FING 147..190
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 205 AA; 23060 MW; C4BF42106B1F55AF CRC64;
MNLHGLELPG RDQRLSPEVI DLTEDIEDDG ADVSEVTLLD LTRIPEFQPR RRIRTSRNHL
DANLSNVPTI NSIPSPVTRP PVAVGGGIFY GARRTRNRSQ TQRRTLLENG FRNSRKKAQD
SSNSIAERVS PPPGFCYDVH PHNNIACAKC GNELVSDEKK SIFAAKCGHL FCSTCAKELR
KKTVPCPVQH CRKRITKKFI FPLYL
