ID POF10_SCHPO Reviewed; 662 AA.
AC Q9P7W4;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 154.
DE RecName: Full=F-box/WD repeat-containing protein pof10;
DE AltName: Full=Skp1-binding protein 2;
GN Name=pof10; Synonyms=sbp2; ORFNames=SPBC1703.06;
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], INTERACTION WITH SKP1, AND SUBCELLULAR
RP LOCATION.
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 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: Probably recognizes and binds to some phosphorylated proteins
CC and promotes their ubiquitination and degradation.
CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex (By
CC similarity). Interacts with skp1. {ECO:0000250,
CC ECO:0000269|PubMed:11820777, ECO:0000269|PubMed:15147268}.
CC -!- INTERACTION:
CC Q9P7W4; Q9Y709: skp1; NbExp=5; IntAct=EBI-908406, EBI-1172248;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11820777,
CC ECO:0000269|PubMed:16823372}.
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DR EMBL; AB061725; BAB55636.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB66450.1; -; Genomic_DNA.
DR PIR; T50319; T50319.
DR RefSeq; NP_596201.1; NM_001022120.2.
DR AlphaFoldDB; Q9P7W4; -.
DR SMR; Q9P7W4; -.
DR BioGRID; 276318; 19.
DR IntAct; Q9P7W4; 1.
DR MINT; Q9P7W4; -.
DR STRING; 284812.Q9P7W4; -.
DR MaxQB; Q9P7W4; -.
DR PaxDb; 4896-SPBC1703-06-1; -.
DR EnsemblFungi; SPBC1703.06.1; SPBC1703.06.1:pep; SPBC1703.06.
DR GeneID; 2539767; -.
DR KEGG; spo:SPBC1703.06; -.
DR PomBase; SPBC1703.06; pof10.
DR VEuPathDB; FungiDB:SPBC1703.06; -.
DR eggNOG; KOG0274; Eukaryota.
DR HOGENOM; CLU_414556_0_0_1; -.
DR InParanoid; Q9P7W4; -.
DR OMA; NTHAMCA; -.
DR PhylomeDB; Q9P7W4; -.
DR Reactome; R-SPO-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-SPO-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-SPO-5689603; UCH proteinases.
DR Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR PRO; PR:Q9P7W4; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISM:PomBase.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISM:PomBase.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:PomBase.
DR CDD; cd09917; F-box_SF; 1.
DR Gene3D; 1.20.1280.50; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR10223; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 4; 1.
DR PANTHER; PTHR10223:SF0; 26S PROTEASOME NON-ATPASE REGULATORY SUBUNIT 4; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF81383; F-box domain; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS50330; UIM; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Repeat; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..662
FT /note="F-box/WD repeat-containing protein pof10"
FT /id="PRO_0000051137"
FT DOMAIN 28..74
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 215..260
FT /note="WD 1"
FT REPEAT 263..302
FT /note="WD 2"
FT REPEAT 429..468
FT /note="WD 3"
FT DOMAIN 581..600
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 646..662
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 74205 MW; 44061C20A61F602C CRC64;
MKSEPTSLDF TSSNLRRMNR DHSSNNTNRT VLNLPKEILI IIFSFLDPRS LLSAQCTCKY
WKKLLSDDLS WRTAFFHHFA GDQSQIFSPL GNGTWRQEYL LRSTITRAYE KGKGQTVQYD
CRVGQLTNLY YDFSSGRLYS GNWLTGTISV SDPTTGKVER SLLHASTDGS FTHGLSTMTL
GKQIFGFGFM DGRVGVILMS RQAETPRKFR YCLDSHADSV TCIDALTGDL PPTGEIGMVT
GSDDGSVHCW DVKTGVSLQS FQFRSSQILS LCFRPKYKML LVDTFNYELN SYQLYLIPGY
ARSRKNEQPI LLSSRKCVLT DEEEPPCLMT ADCCAGVAFL SRGAPKNCIC RVSFKEFLEK
NDNVGVQTSS IPLNGKPTSI SLDTNDRVLS KSTPGRGARL LAVGDENGLV YVVNTRTEDP
NKAILRTITA YSNFPITDIY LNEVAMVVGS ASGYCGVYDT VTGNFLKKIA SARNAARREP
INCILLDSNP LSLKGVITMS KHVKSWSYTI PKPFVNKRSK VLPLRPSVTH DNLSKSSDYS
KNEVEREIML GLDQIAQERR EKMEARQKFE QHFGEGLVGL SEEEIIAYVT MLSQEEEAKR
MVQLSMDVDK IEEDFKENDE QATSSLNALS SNHEPPQEQA NVAELNEQEQ IELAMRLSLM
EM
//
