POP2_SCHPO
ID POP2_SCHPO Reviewed; 703 AA.
AC O14170;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=WD repeat-containing protein pop2;
DE AltName: Full=Proteolysis factor sud1;
GN Name=pop2; Synonyms=sud1; ORFNames=SPAC4D7.03;
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 [MRNA], AND INTERACTION WITH POP1 AND CDC18.
RC STRAIN=972 / ATCC 24843;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INTERACTION WITH CDC18.
RX PubMed=9653157; DOI=10.1073/pnas.95.14.8159;
RA Jallepalli P.V., Tien D., Kelly T.J.;
RT "sud1+ targets cyclin-dependent kinase-phosphorylated Cdc18 and Rum1
RT proteins for degradation and stops unwanted diploidization in fission
RT yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8159-8164(1998).
RN [3]
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 [4]
RP FUNCTION, AND 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 [5]
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 [6]
RP FUNCTION.
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).
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 pop1, required for cig2 instability during
CC G2 and M phase and cig2 degradation in exponentially growing cells.
CC {ECO:0000269|PubMed:12167173, ECO:0000269|PubMed:14970237,
CC ECO:0000269|PubMed:9653157, ECO:0000269|PubMed:9990507}.
CC -!- SUBUNIT: Homodimer and heterodimer with pop1. Binds to cul1, pip1 and
CC phosphorylated cdc18. {ECO:0000269|PubMed:12167173,
CC ECO:0000269|PubMed:9990507}.
CC -!- INTERACTION:
CC O14170; P41411: cdc18; NbExp=3; IntAct=EBI-1185414, EBI-1207853;
CC O14170; O13790: cul1; NbExp=3; IntAct=EBI-1185414, EBI-1154807;
CC O14170; P87060: pop1; NbExp=12; IntAct=EBI-1185414, EBI-1185389;
CC O14170; Q9Y709: skp1; NbExp=3; IntAct=EBI-1185414, EBI-1172248;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12167173}. Nucleus
CC {ECO:0000269|PubMed:12167173}.
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DR EMBL; AF038867; AAB95480.1; -; mRNA.
DR EMBL; AF064515; AAC39496.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11275.1; -; Genomic_DNA.
DR PIR; T43557; T43557.
DR RefSeq; NP_594956.1; NM_001020387.2.
DR AlphaFoldDB; O14170; -.
DR SMR; O14170; -.
DR BioGRID; 279932; 73.
DR IntAct; O14170; 6.
DR MINT; O14170; -.
DR STRING; 4896.SPAC4D7.03.1; -.
DR MaxQB; O14170; -.
DR PaxDb; O14170; -.
DR PRIDE; O14170; -.
DR EnsemblFungi; SPAC4D7.03.1; SPAC4D7.03.1:pep; SPAC4D7.03.
DR GeneID; 2543514; -.
DR KEGG; spo:SPAC4D7.03; -.
DR PomBase; SPAC4D7.03; pop2.
DR VEuPathDB; FungiDB:SPAC4D7.03; -.
DR eggNOG; KOG0274; Eukaryota.
DR HOGENOM; CLU_000288_103_3_1; -.
DR InParanoid; O14170; -.
DR OMA; HTGGVWT; -.
DR PhylomeDB; O14170; -.
DR PRO; PR:O14170; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043224; C:nuclear SCF ubiquitin ligase complex; ISO:PomBase.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IPI:PomBase.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:PomBase.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IBA:GO_Central.
DR GO; GO:1903467; P:negative regulation of mitotic DNA replication initiation; IMP:PomBase.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISO: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; PF00646; F-box; 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; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Repeat; Ubl conjugation pathway;
KW WD repeat.
FT CHAIN 1..703
FT /note="WD repeat-containing protein pop2"
FT /id="PRO_0000051140"
FT DOMAIN 236..283
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 389..417
FT /note="WD 1"
FT REPEAT 429..473
FT /note="WD 2"
FT REPEAT 505..533
FT /note="WD 3"
FT REPEAT 545..575
FT /note="WD 4"
FT REPEAT 587..615
FT /note="WD 5"
FT REPEAT 625..654
FT /note="WD 6"
FT REGION 1..170
FT /note="Interaction with pop1"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 703 AA; 79605 MW; 0336A0568C152396 CRC64;
MSLSRCPTDN SSSRINSSVP LINSSSPATP PESFDPQVFP SSLIHGDNLL PQDDQIASDP
RSESNSCNGN TSSSLPCTDS YQYPLKHSCT PSFLRKFNES IENVSYKCLD HSPPDSVPGD
FSISLVPQRN FLYSHSSLPP KIISIDRNNR IKLDNSISSN SDNFPPSPKV DTSNTVSPGS
KPISEDLEDL NLQSIVQTFE DLPEGIQSYA FFQLLRSCNR QSMRLLLNEC EPLLKKDILS
NLPFSIVQSI LLNLDIHSFL SCRLVSPTWN RILDVHTSYW KHMFSLFGFQ INENDWKYAN
PNLNRPPFLH NDQISDDYFP EIFKRHFLNR KRWLFPSIPP SHLSFPIHVP NFMITSLLLH
KDRIITTSGS GTIQIHNAIT GVLEARLEGH KEGVWAVKIH ENTLVSGSID KTVRVWNIEK
AKCTHIFRGH ISIIRCLEIL VPSRLIRHGV EIVEPDQPYI VSGSRDHTLR VWKLPKNTDP
PYLPDNTNSI DRWEKNPYFV HTLIGHTDSV RTISGYGDIL VSGSYDSSIR IWRVSTGECL
YHLRGHSLRI YSVLYEPERN ICISGSMDKS IRVWDLSTGT CKYVLEGHDA FVTLLNVFQN
RLISGSADST IRIWDLNTGK PLMVLPSNSG YISSFVSDEH KIISGNDGSV KLWDVRTGKL
LRFLLTDLTK IWHVDFDAMR CVAAVQRDDQ AYLEVINFSG SRP
