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POF11_SCHPO
ID   POF11_SCHPO             Reviewed;         506 AA.
AC   Q09855; Q9P7V1;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=F-box/WD repeat-containing protein pof11;
DE   AltName: Full=Meiotically up-regulated gene 156 protein;
GN   Name=pof11; Synonyms=mug156; ORFNames=SPAC29E6.01, SPAC30.05;
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].
RA   Harrison C.L., Toda T.;
RT   "Systematic genome-wide analysis of F-box protein-encoding genes in fission
RT   yeast.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
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   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   [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 meiosis. {ECO:0000269|PubMed:16303567}.
CC   -!- SUBUNIT: Interacts with skp1. {ECO:0000269|PubMed:15147268}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
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DR   EMBL; AB061694; BAB55543.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB66464.1; -; Genomic_DNA.
DR   EMBL; Z66525; CAA91423.1; -; Genomic_DNA.
DR   PIR; T38502; S62507.
DR   PIR; T50211; T50211.
DR   RefSeq; NP_594559.1; NM_001019988.2.
DR   AlphaFoldDB; Q09855; -.
DR   SMR; Q09855; -.
DR   BioGRID; 278202; 11.
DR   IntAct; Q09855; 1.
DR   STRING; 4896.SPAC29E6.01.1; -.
DR   PaxDb; Q09855; -.
DR   PRIDE; Q09855; -.
DR   EnsemblFungi; SPAC29E6.01.1; SPAC29E6.01.1:pep; SPAC29E6.01.
DR   GeneID; 2541707; -.
DR   KEGG; spo:SPAC29E6.01; -.
DR   PomBase; SPAC29E6.01; pof11.
DR   VEuPathDB; FungiDB:SPAC29E6.01; -.
DR   eggNOG; KOG0281; Eukaryota.
DR   HOGENOM; CLU_000288_103_6_1; -.
DR   InParanoid; Q09855; -.
DR   OMA; ENNWRMG; -.
DR   PhylomeDB; Q09855; -.
DR   Reactome; R-SPO-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR   Reactome; R-SPO-8951664; Neddylation.
DR   Reactome; R-SPO-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR   Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:Q09855; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; ISM:PomBase.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; ISM:PomBase.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISM:PomBase.
DR   Gene3D; 2.130.10.10; -; 2.
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; 6.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00256; FBOX; 1.
DR   SMART; SM00320; WD40; 8.
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; Meiosis; Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..506
FT                   /note="F-box/WD repeat-containing protein pof11"
FT                   /id="PRO_0000051138"
FT   DOMAIN          70..116
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   REPEAT          219..256
FT                   /note="WD 1"
FT   REPEAT          259..298
FT                   /note="WD 2"
FT   REPEAT          301..338
FT                   /note="WD 3"
FT   REPEAT          345..386
FT                   /note="WD 4"
FT   REPEAT          388..426
FT                   /note="WD 5"
FT   REPEAT          427..464
FT                   /note="WD 6"
FT   REPEAT          468..505
FT                   /note="WD 7"
SQ   SEQUENCE   506 AA;  58257 MW;  CEF34D4EFFBC2E10 CRC64;
     MNQDDNGKNV VSKVSDLTSC SDFSTSSPVP CLNPLSHENN RIDLIRDLLA SLSKEGVVAV
     YNHVRSLLFT DFTEVFPEEV SLRVFSYLDQ LDLCKCKLMS KRWKRLLEDP GIWKALYMQK
     GWFVNENVLN EFEAWRRTHK FPQPRFENFL KQQNIIGPYG TMFLPQQFIF DSNGRPLLNW
     SYLYKEHAHL DSNWRHGRFL VSTFNNPSIR FPADQDFRAT LDSVYCVQYD DEIMVSGSKD
     RTVSVWDVNS RFILYKLYGH SGSVLCLDFC RRRNLLVSGS SDSTIIIWDW QNRRPLKVYF
     GHTDNVLGVV VSENYIISSS RDHTARVWRL DATSPAEACM HVLRGHLASV NSVQYSSKTG
     LIVTASSDRT LRTWDITTGH CIRIIHAHQR GIACAQYNGK FIVSGSSDLT IRIFEASSGK
     LLRMLQGHED LIRTVRFNDE KIVSGGYDGT VRIWNFNTGE QHCVLHNSRN SRVFGLQFDH
     RRIIACTHSS EILVWNFDDG LDCTFF
 
 
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