POF3_SCHPO
ID POF3_SCHPO Reviewed; 577 AA.
AC O74991;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=F-box/TPR repeat protein pof3;
GN Name=pof3; ORFNames=SPCC338.16;
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 [GENOMIC DNA], FUNCTION, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=11809834; DOI=10.1091/mbc.01-07-0333;
RA Katayama S., Kitamura K., Lehmann A., Nikaido O., Toda T.;
RT "Fission yeast F-box protein Pof3 is required for genome integrity and
RT telomere function.";
RL Mol. Biol. Cell 13:211-224(2002).
RN [2]
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 [3]
RP INTERACTION WITH SKP1.
RX PubMed=15147268; DOI=10.1111/j.1356-9597.2004.00730.x;
RA Lehmann A., Katayama S., Harrison C., Dhut S., Kitamura K., McDonald N.,
RA Toda T.;
RT "Molecular interactions of fission yeast Skp1 and its role in the DNA
RT damage checkpoint.";
RL Genes Cells 9:367-382(2004).
RN [4]
RP INTERACTION WITH MCL1.
RX PubMed=16997270; DOI=10.1016/j.bbrc.2006.09.024;
RA Mamnun Y.M., Katayama S., Toda T.;
RT "Fission yeast Mcl1 interacts with SCF(Pof3) and is required for centromere
RT formation.";
RL Biochem. Biophys. Res. Commun. 350:125-130(2006).
RN [5]
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).
CC -!- FUNCTION: Has a role in substrate recognition in the Skp1-Cullin-
CC 1/Cdc53-F-box (SCF) ubiquitin ligase complex. Required for the
CC maintenance of telomere length and transcriptional silencing at the
CC telomere. Also required for chromosome segregation.
CC {ECO:0000269|PubMed:11809834}.
CC -!- SUBUNIT: A part of the E3 ubiquitin ligase Skp1-Cullin-1-F-box (SCF)
CC complex. Interacts with cul1, mcl1 and skp1.
CC {ECO:0000269|PubMed:11809834, ECO:0000269|PubMed:15147268,
CC ECO:0000269|PubMed:16997270}.
CC -!- INTERACTION:
CC O74991; O13790: cul1; NbExp=2; IntAct=EBI-1153554, EBI-1154807;
CC O74991; Q9C107: mcl1; NbExp=2; IntAct=EBI-1153554, EBI-1203666;
CC O74991; Q9Y709: skp1; NbExp=3; IntAct=EBI-1153554, EBI-1172248;
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Nucleus.
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DR EMBL; AB032411; BAA84529.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA19347.1; -; Genomic_DNA.
DR PIR; T41727; T41727.
DR RefSeq; NP_588152.1; NM_001023141.2.
DR AlphaFoldDB; O74991; -.
DR BioGRID; 276089; 95.
DR IntAct; O74991; 4.
DR STRING; 4896.SPCC338.16.1; -.
DR MaxQB; O74991; -.
DR PaxDb; O74991; -.
DR EnsemblFungi; SPCC338.16.1; SPCC338.16.1:pep; SPCC338.16.
DR GeneID; 2539527; -.
DR KEGG; spo:SPCC338.16; -.
DR PomBase; SPCC338.16; pof3.
DR VEuPathDB; FungiDB:SPCC338.16; -.
DR eggNOG; ENOG502SA77; Eukaryota.
DR HOGENOM; CLU_472639_0_0_1; -.
DR InParanoid; O74991; -.
DR OMA; GIYKYGM; -.
DR PhylomeDB; O74991; -.
DR PRO; PR:O74991; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:PomBase.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISM:PomBase.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:PomBase.
DR GO; GO:1903464; P:negative regulation of mitotic cell cycle DNA replication; IMP:PomBase.
DR GO; GO:0061806; P:regulation of DNA recombination at centromere; IMP:PomBase.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IMP:PomBase.
DR GO; GO:0000723; P:telomere maintenance; IMP:PomBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:PomBase.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00646; F-box; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Mitochondrion; Nucleus; Reference proteome; Repeat; TPR repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..577
FT /note="F-box/TPR repeat protein pof3"
FT /id="PRO_0000106362"
FT REPEAT 6..39
FT /note="TPR 1"
FT REPEAT 41..74
FT /note="TPR 2"
FT REPEAT 76..108
FT /note="TPR 3"
FT DOMAIN 138..180
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
SQ SEQUENCE 577 AA; 66239 MW; 507D7901C1980D3F CRC64;
MNNYQVKAIK EKTQQYLSKR KFEDALTFIT KTIEQEPNPT IDLFELRAQV YEKSGQYSQA
ELDAKRMIHL NARNARGYLR LGKLLQLDGF DKKADQLYTQ GLRMVHKMDP LRPVLKKVSQ
RLNERILRTR PVLDLFRILP REVLLCILQQ LNFKSIVQCM QVCKHWRDCI KKEPSLFCCL
DFSCASPRSV NSRDRNVMAV ARYSVYSKDN IQEVIGLEKL GILTPTKALL RSVKSLKVYK
TISPLHTQST DKLYTIWTPF SELHYFYCAT PITFSIASKI LSCCKKLKQV ELVDLIPDLI
FDSMDWDKLF NAESVPLALK SLTFIRNQKF PFHHKEQQFL KDLLSASPYL EYLEASYQSD
LVAAIKKYKI NLRSLIIIDE GVSNTVKDLA FLPQSLTTLI VKPCNPASTI LCPYLFPTNV
RMESLINLEL FLYLRLSQND IDNVVKFLTS CYKLKKLVLH DSLALAPHFF EIFASLPELE
HLEIPDNVAL QNKHAIHITD CCPNLKYVNF SNSISLDGSG FIAVLRGLKE LKRIDIINCD
SVSRDAIDWA RSKGMQVTVA SSLPNSQPLG TKKIRLI
