POF1_SCHPO
ID POF1_SCHPO Reviewed; 605 AA.
AC P87053;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=F-box/WD repeat-containing protein pof1;
DE AltName: Full=Skp1-binding protein 1;
GN Name=pof1; Synonyms=sbp1; ORFNames=SPAC57A10.05c;
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].
RX PubMed=11820777; DOI=10.1006/bbrc.2002.6344;
RA Ikebe C., Kominami K., Toda T., Nakayama K.;
RT "Isolation and characterization of a novel F-box protein Pof10 in fission
RT yeast.";
RL Biochem. Biophys. Res. Commun. 290:1399-1407(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 FUNCTION, SUBUNIT, AND MUTAGENESIS OF PHE-109; SER-118; LYS-246 AND
RP SER-566.
RX PubMed=15660136; DOI=10.1038/sj.emboj.7600536;
RA Harrison C., Katayama S., Dhut S., Chen D., Jones N., Bahler J., Toda T.;
RT "SCF(Pof1)-ubiquitin and its target Zip1 transcription factor mediate
RT cadmium response in fission yeast.";
RL EMBO J. 24:599-610(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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229 AND SER-232, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Probably recognizes and binds to some phosphorylated proteins
CC and promotes their ubiquitination and degradation. Required for the
CC inactivation of zip1 via ubiquitination. {ECO:0000269|PubMed:15660136}.
CC -!- SUBUNIT: A part of the E3 ubiquitin ligase Skp1-Cullin-1-F-box (SCF)
CC complex. Interacts with cul1, skp1 and phosphorylated zip1.
CC {ECO:0000269|PubMed:15147268, ECO:0000269|PubMed:15660136}.
CC -!- INTERACTION:
CC P87053; Q9Y709: skp1; NbExp=2; IntAct=EBI-1185435, EBI-1172248;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
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DR EMBL; AB032410; BAA84528.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB08168.1; -; Genomic_DNA.
DR PIR; T38932; T38932.
DR RefSeq; NP_593310.1; NM_001018741.2.
DR AlphaFoldDB; P87053; -.
DR SMR; P87053; -.
DR BioGRID; 279356; 6.
DR IntAct; P87053; 3.
DR STRING; 4896.SPAC57A10.05c.1; -.
DR iPTMnet; P87053; -.
DR MaxQB; P87053; -.
DR PaxDb; P87053; -.
DR PRIDE; P87053; -.
DR EnsemblFungi; SPAC57A10.05c.1; SPAC57A10.05c.1:pep; SPAC57A10.05c.
DR GeneID; 2542914; -.
DR KEGG; spo:SPAC57A10.05c; -.
DR PomBase; SPAC57A10.05c; pof1.
DR VEuPathDB; FungiDB:SPAC57A10.05c; -.
DR eggNOG; KOG0274; Eukaryota.
DR HOGENOM; CLU_000288_103_1_1; -.
DR InParanoid; P87053; -.
DR OMA; KMCEQHI; -.
DR PhylomeDB; P87053; -.
DR PRO; PR:P87053; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:PomBase.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IPI:PomBase.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IC: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; 7.
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; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation pathway; WD repeat.
FT CHAIN 1..605
FT /note="F-box/WD repeat-containing protein pof1"
FT /id="PRO_0000051136"
FT DOMAIN 107..153
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 271..299
FT /note="WD 1"
FT REPEAT 311..339
FT /note="WD 2"
FT REPEAT 350..379
FT /note="WD 3"
FT REPEAT 390..420
FT /note="WD 4"
FT REPEAT 432..460
FT /note="WD 5"
FT REPEAT 472..500
FT /note="WD 6"
FT REPEAT 510..538
FT /note="WD 7"
FT REGION 195..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 109
FT /note="F->S: Temperature sensitive induction of early
FT growth arrest and small cell size; when associated with P-
FT 118."
FT /evidence="ECO:0000269|PubMed:15660136"
FT MUTAGEN 118
FT /note="S->P: Temperature sensitive induction of early
FT growth arrest and small cell size; when associated with S-
FT 109."
FT /evidence="ECO:0000269|PubMed:15660136"
FT MUTAGEN 246
FT /note="K->E: Temperature sensitive induction of early
FT growth arrest and small cell size; when associated with G-
FT 566."
FT /evidence="ECO:0000269|PubMed:15660136"
FT MUTAGEN 566
FT /note="S->G: Temperature sensitive induction of early
FT growth arrest and small cell size; when associated with E-
FT 246."
FT /evidence="ECO:0000269|PubMed:15660136"
SQ SEQUENCE 605 AA; 67111 MW; 7118C9379EC5C1F0 CRC64;
MTTGYESVPT SEPSDNLAPR AELWQRHLLE KKEGDQSISV SAFNISSMHN ELSGLSEKSR
QRVEAVWAAF SEASCSERKL ALQGILNNCS SSLLSFASST LDSLVRLDFL SLLPVEISFR
ILSFLDARSL CQAAQVSKHW KELADDDVIW HRMCEQHINR KCEKCGWGLP LLERNTLYAA
KASIQKRYER LTKRGVDQAH ESSPVKKAKL DDYPTSSNEE TISSVKPPSP NSDSKFFLPF
KTRPWKEVYA ERCRVECNWR HGRCRQVVLS GHSDGVMCLQ LVRNILASGS YDATIRLWNL
ATFQQVALLE GHSSGVTCLQ FDQCKLISGS MDKTIRIWNY RTSECISILH GHTDSVLCLT
FDSTLLVSGS ADCTVKLWHF SGGKRITLRG HTGPVNSVRI IRDRGLVLSG SDDSTIKIWS
LETNTCLHTF SAHIGPVQSL ALADSRLFSC SLDGTIKQWD IEKKKCVHTL FGHIEGVWEI
AADHLRLISG AHDGVVKVWE ACECVHTLKN HSEPVTSVAL GDCEVVSGSE DGKIYLWLFN
NAPNESPVST QSVPISSLNG QRSNSSVQRA LSSVPNYSSS LSNISTRNLN IPPSNANNDD
VSIQS
