POP1_SCHPO
ID POP1_SCHPO Reviewed; 775 AA.
AC P87060; Q9P7P3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 173.
DE RecName: Full=WD repeat-containing protein pop1;
DE AltName: Full=WD repeat-containing protein ste16;
GN Name=pop1; Synonyms=ste16; ORFNames=SPBC1718.01, SPBC2G2.18;
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 [GENOMIC DNA], FUNCTION, AND INTERACTION WITH CDC18.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9203581; DOI=10.1101/gad.11.12.1548;
RA Kominami K., Toda T.;
RT "Fission yeast WD-repeat protein pop1 regulates genome ploidy through
RT ubiquitin-proteasome-mediated degradation of the CDK inhibitor Rum1 and the
RT S-phase initiator Cdc18.";
RL Genes Dev. 11:1548-1560(1997).
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 SUBUNIT.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9990507; DOI=10.1046/j.1365-2443.1998.00225.x;
RA Kominami K., Ochotorena I., Toda T.;
RT "Two F-box/WD-repeat proteins Pop1 and Pop2 form hetero- and homo-complexes
RT together with cullin-1 in fission yeast SCF (Skip-cullin-1-F-box) ubiquitin
RT ligase.";
RL Genes Cells 3:721-735(1998).
RN [4]
RP FUNCTION.
RX PubMed=9472077; DOI=10.1007/s002940050305;
RA Maekawa H., Kitamura K., Shimoda C.;
RT "The Ste16 WD-repeat protein regulates cell-cycle progression under
RT starvation through the Rum1 protein in Schizosaccharomyces pombe.";
RL Curr. Genet. 33:29-37(1998).
RN [5]
RP INTERACTION WITH POP2 AND CDC18.
RX PubMed=10209119; DOI=10.1016/s0960-9822(99)80165-1;
RA Wolf D.A., McKeon F., Jackson P.K.;
RT "F-box/WD-repeat proteins pop1p and Sud1p/Pop2p form complexes that bind
RT and direct the proteolysis of cdc18p.";
RL Curr. Biol. 9:373-376(1999).
RN [6]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=12167173; DOI=10.1186/1471-2091-3-22;
RA Seibert V., Prohl C., Schoultz I., Rhee E., Lopez R., Abderazzaq K.,
RA Zhou C., Wolf D.A.;
RT "Combinatorial diversity of fission yeast SCF ubiquitin ligases by
RT homo- and heterooligomeric assemblies of the F-box proteins Pop1p and
RT Pop2p.";
RL BMC Biochem. 3:22-22(2002).
RN [7]
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 [8]
RP FUNCTION, AND INTERACTION WITH CIG2.
RX PubMed=14970237; DOI=10.1074/jbc.m311060200;
RA Yamano H., Kominami K., Harrison C., Kitamura K., Katayama S., Dhut S.,
RA Hunt T., Toda T.;
RT "Requirement of the SCFPop1/Pop2 ubiquitin ligase for degradation of the
RT fission yeast S phase cyclin Cig2.";
RL J. Biol. Chem. 279:18974-18980(2004).
RN [9]
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: Involved in maintenance of ploidy through proteasome
CC dependent degradation of CDK inhibitor rum1 and S-phase initiator
CC cdc18. Functions as a recognition factor for rum1 and cdc18, which are
CC subsequently ubiquitinated and targeted to the 26S proteasome for
CC degradation. Together with pop2, required for cig2 instability during
CC G2 and M phase and cig2 degradation in exponentially growing cells.
CC Regulates cell-cycle progression under starvation through the rum1
CC protein. {ECO:0000269|PubMed:12167173, ECO:0000269|PubMed:14970237,
CC ECO:0000269|PubMed:9203581, ECO:0000269|PubMed:9472077}.
CC -!- SUBUNIT: Homodimer and heterodimer with pop2. Binds to cdc18,
CC phosphorylated cig2, cul1, pip1 and skp1. {ECO:0000269|PubMed:12167173,
CC ECO:0000269|PubMed:9990507}.
CC -!- INTERACTION:
CC P87060; P41411: cdc18; NbExp=3; IntAct=EBI-1185389, EBI-1207853;
CC P87060; P36630: cig2; NbExp=4; IntAct=EBI-1185389, EBI-1149212;
CC P87060; O14170: pop2; NbExp=12; IntAct=EBI-1185389, EBI-1185414;
CC P87060; Q9Y709: skp1; NbExp=2; IntAct=EBI-1185389, EBI-1172248;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12167173,
CC ECO:0000269|PubMed:16823372}.
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DR EMBL; Y08391; CAA69671.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB75991.1; -; Genomic_DNA.
DR PIR; T45136; T45136.
DR PIR; T50329; T50329.
DR RefSeq; XP_001713146.1; XM_001713094.2.
DR AlphaFoldDB; P87060; -.
DR SMR; P87060; -.
DR BioGRID; 277039; 13.
DR IntAct; P87060; 7.
DR STRING; 4896.SPBC1718.01.1; -.
DR MaxQB; P87060; -.
DR PaxDb; P87060; -.
DR PRIDE; P87060; -.
DR EnsemblFungi; SPBC1718.01.1; SPBC1718.01.1:pep; SPBC1718.01.
DR PomBase; SPBC1718.01; pop1.
DR VEuPathDB; FungiDB:SPBC1718.01; -.
DR eggNOG; KOG0274; Eukaryota.
DR HOGENOM; CLU_000288_103_3_1; -.
DR InParanoid; P87060; -.
DR OMA; CLQHDDE; -.
DR PhylomeDB; P87060; -.
DR PRO; PR:P87060; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0043224; C:nuclear SCF ubiquitin ligase complex; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:PomBase.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IMP:PomBase.
DR GO; GO:0000747; P:conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISO:PomBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:PomBase.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; Repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..775
FT /note="WD repeat-containing protein pop1"
FT /id="PRO_0000051139"
FT DOMAIN 298..345
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 444..472
FT /note="WD 1"
FT REPEAT 484..538
FT /note="WD 2"
FT REPEAT 575..603
FT /note="WD 3"
FT REPEAT 615..645
FT /note="WD 4"
FT REPEAT 657..687
FT /note="WD 5"
SQ SEQUENCE 775 AA; 87817 MW; B06EDBA46553EEC1 CRC64;
MNEKKKDSLS VLDSNEFFGE TTMVSPSIDV SSSPRPNVER FSPCSTKKDL LEGNNIMTRI
PEELSRVSLQ FDSKGSQQSM IFTNNRCLSD KENLENLQNL LYLHCDLNRP HLSCELPSEH
REKCLKRRNS SLSSNLHANK RFLFNSQSDG NKKNETFPST NYSNVFYPNN CDSKEVASET
TFSLDAPNNS VNYSYFSPNL LGNDSKTRQS FPPHSSSSSH NSLHEPVIYD FSSENPSIHP
SNHLSSQKNA VLKLAQLISS FEKLPESVRQ YLLFHLLSRC GKHAVQNIHK ILLPIFQKNF
LTGFPAEITN LVLTHLDAPS LCAVSQVSHH WYKLVSSNEE LWKSLFLKDG FFWDSIDSKI
RTMCLEQSLS ACAIMKRVYF RHFNLRERWL HAPEKIKRCS FPIHGVRLIT KLQFDDDKII
VSTCSPRINI YDTKTGVLIR SLEEHEGDVW TFEYVGDTLV TGSTDRTVRV WDLRTGECKQ
VFYGHTSTIR CIKIVQGNQS TTDTDDVEKE NRPASNDANS MPPYIISSSR DCTIRLWSLP
CLDDPPFVNV NENPDQNNDF TSATTNPFYI RTLRGHTDSV REVACLGDLI VSASYDGTLR
VWKASTGVCL HVLRGHVGRV YSVTINPSRQ QCISAGTDAK IRIWNLESGE LLQTLHGHSN
LVSQVTFNQN ILVSASAPPD TSLRVWDLNT GSCRDILKCP LGHIFFQHDE SKVVSGSHST
LQLWDIRSGK LVRDLLTDLD IIWQVAYNEN VCVAAVLRNN RFWIEVLEFG STKSS
