RFP1_SCHPO
ID RFP1_SCHPO Reviewed; 254 AA.
AC O13826;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=E3 ubiquitin-protein ligase complex slx8-rfp subunit rfp1;
DE EC=2.3.2.27;
DE AltName: Full=Meiotically up-regulated gene 140 protein;
DE AltName: Full=RING finger protein 1;
DE AltName: Full=RING-type E3 ubiquitin transferase rfp1 {ECO:0000305};
GN Name=rfp1; Synonyms=mug140; ORFNames=SPAC19A8.10;
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 FUNCTION IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
RN [3]
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 [4]
RP FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, IDENTIFICATION IN A E3
RP UBIQUITIN-PROTEIN LIGASE COMPLEX WITH RFP2 AND SLX8, INTERACTION WITH SLX8;
RP NSE5 AND RAD60, 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 [5]
RP FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, INTERACTION WITH PMT3, AND
RP 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 [6]
RP FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, AND INTERACTION WITH CHK1.
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. Has a role in
CC meiosis. {ECO:0000269|PubMed:16303567, ECO:0000269|PubMed:17502373,
CC ECO:0000269|PubMed:17762864, 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, chk1, nse5, pmt3 and rad60.
CC {ECO:0000269|PubMed:17502373, ECO:0000269|PubMed:17762864,
CC ECO:0000269|PubMed:17762865}.
CC -!- INTERACTION:
CC O13826; P34208: chk1; NbExp=3; IntAct=EBI-3647269, EBI-768535;
CC O13826; O13351: pmt3; NbExp=5; IntAct=EBI-3647269, EBI-966336;
CC O13826; P87176: slx8; NbExp=5; IntAct=EBI-3647269, 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; CAB11646.1; -; Genomic_DNA.
DR PIR; T37951; T37951.
DR RefSeq; NP_593782.1; NM_001019211.2.
DR AlphaFoldDB; O13826; -.
DR BioGRID; 278999; 18.
DR IntAct; O13826; 10.
DR MINT; O13826; -.
DR STRING; 4896.SPAC19A8.10.1; -.
DR PaxDb; O13826; -.
DR EnsemblFungi; SPAC19A8.10.1; SPAC19A8.10.1:pep; SPAC19A8.10.
DR GeneID; 2542542; -.
DR KEGG; spo:SPAC19A8.10; -.
DR PomBase; SPAC19A8.10; rfp1.
DR VEuPathDB; FungiDB:SPAC19A8.10; -.
DR eggNOG; ENOG502SDJU; Eukaryota.
DR HOGENOM; CLU_043321_1_0_1; -.
DR InParanoid; O13826; -.
DR OMA; PRCHEEL; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O13826; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR GO; GO:0033768; C:SUMO-targeted ubiquitin ligase complex; IPI:PomBase.
DR GO; GO:0003677; F:DNA binding; IDA:PomBase.
DR GO; GO:0140082; F:SUMO-ubiquitin ligase activity; IDA:PomBase.
DR GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
DR GO; GO:0006281; P:DNA repair; IGI:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC: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; IPR038886; E3_SLX5/Rfp1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR28042; PTHR28042; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Meiosis; Metal-binding; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..254
FT /note="E3 ubiquitin-protein ligase complex slx8-rfp subunit
FT rfp1"
FT /id="PRO_0000056333"
FT ZN_FING 189..238
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 254 AA; 28903 MW; E47B9E2B35E573DA CRC64;
MQFNGSNGID ESSVIDLTRS PSPPVETSIS STNIIDLDAI PDDSFPSSPV LSPRRRRMNR
RRNERSRNFP SNHLSYLEDM IYLGPQVSTR RSSSRRDLMG MIARTFPEFS SVNSLSPSLF
QLIVNRMRFD AIHPEWTNGS DDEYFSNHFE ESYDDFTSSL ENIKQSYKPP GPPKSGFTRS
FNNDTLMVCP RCQEPLGTSK SKEKSALWAT KCGHVYCGSC AKVLKTSKRS QSKCLVNDCG
RYLNTKNAMW ELFY
