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Database: UniProt
Entry: RFP1_SCHPO
LinkDB: RFP1_SCHPO
Original site: 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   18-SEP-2019, entry version 122.
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;
OC   Schizosaccharomycetaceae; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., 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.,
RA   San-Segundo P., Smith G.R., Moreno S.;
RT   "A large-scale screen in S. pombe identifies seven novel genes
RT   required for 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
RT   fission 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
RP   SLX8; 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.,
RA   Tainer J.A., 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,
RP   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   [6]
RP   FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, AND INTERACTION WITH
RP   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
CC       stability where it acts in the cellular response to DNA damage.
CC       Has a role in meiosis. {ECO:0000269|PubMed:16303567,
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-
CC         cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
CC         conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
CC         protein]-L-lysine.; EC=2.3.2.27;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Part of an E3 ubiquitin complex including rfp1, rfp2 and
CC       slx8. 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       P34208:chk1; NbExp=3; IntAct=EBI-3647269, EBI-768535;
CC       O13351:pmt3; NbExp=5; IntAct=EBI-3647269, EBI-966336;
CC       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}.
DR   EMBL; CU329670; CAB11646.1; -; Genomic_DNA.
DR   PIR; T37951; T37951.
DR   RefSeq; NP_593782.1; NM_001019211.2.
DR   SMR; O13826; -.
DR   BioGrid; 278999; 17.
DR   IntAct; O13826; 10.
DR   MINT; O13826; -.
DR   STRING; 4896.SPAC19A8.10.1; -.
DR   PaxDb; O13826; -.
DR   PRIDE; O13826; -.
DR   EnsemblFungi; SPAC19A8.10.1; SPAC19A8.10.1:pep; SPAC19A8.10.
DR   GeneID; 2542542; -.
DR   KEGG; spo:SPAC19A8.10; -.
DR   EuPathDB; FungiDB:SPAC19A8.10; -.
DR   PomBase; SPAC19A8.10; rfp1.
DR   InParanoid; O13826; -.
DR   OMA; PRCHEEL; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:O13826; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000790; C:nuclear 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:0033234; P:negative regulation of protein sumoylation; IMP:PomBase.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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   Complete proteome; Meiosis; Metal-binding; Nucleus;
KW   Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    254       E3 ubiquitin-protein ligase complex slx8-
FT                                rfp subunit rfp1.
FT                                /FTId=PRO_0000056333.
FT   ZN_FING     189    238       RING-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00175}.
FT   COMPBIAS     54     57       Poly-Arg.
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
//
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