POF2_SCHPO
ID POF2_SCHPO Reviewed; 463 AA.
AC O74783;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=SCF E3 ubiquitin ligase complex F-box protein pof2;
DE AltName: Full=F-box and leucine-rich repeat protein pof2;
DE AltName: Full=F-box/LRR-repeat protein pof2;
DE Short=F-box protein pof2;
GN Name=pof2; ORFNames=SPBC25B2.11;
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 (JUN-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 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 substrate recognition in ubiquitin-dependent
CC degradation. {ECO:0000250}.
CC -!- SUBUNIT: Part of a SCF E3 ubiquitin ligase complex (By similarity).
CC Interacts with skp1. {ECO:0000250, ECO:0000269|PubMed:15147268}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB062778; BAB60689.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA21269.1; -; Genomic_DNA.
DR PIR; T39987; T39987.
DR RefSeq; NP_596079.1; NM_001021991.2.
DR AlphaFoldDB; O74783; -.
DR SMR; O74783; -.
DR BioGRID; 276884; 29.
DR IntAct; O74783; 1.
DR STRING; 4896.SPBC25B2.11.1; -.
DR PaxDb; O74783; -.
DR EnsemblFungi; SPBC25B2.11.1; SPBC25B2.11.1:pep; SPBC25B2.11.
DR GeneID; 2540355; -.
DR KEGG; spo:SPBC25B2.11; -.
DR PomBase; SPBC25B2.11; pof2.
DR VEuPathDB; FungiDB:SPBC25B2.11; -.
DR eggNOG; KOG1947; Eukaryota.
DR HOGENOM; CLU_010840_2_1_1; -.
DR InParanoid; O74783; -.
DR OMA; LCNRIRY; -.
DR PhylomeDB; O74783; -.
DR Reactome; R-SPO-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-SPO-8949613; Cristae formation.
DR PRO; PR:O74783; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
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; ISO:PomBase.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF13516; LRR_6; 2.
DR SMART; SM00367; LRR_CC; 8.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Leucine-rich repeat; Mitochondrion; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..463
FT /note="SCF E3 ubiquitin ligase complex F-box protein pof2"
FT /id="PRO_0000119972"
FT DOMAIN 1..42
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 145..170
FT /note="LRR 1"
FT REPEAT 171..196
FT /note="LRR 2"
FT REPEAT 198..220
FT /note="LRR 3"
FT REPEAT 225..247
FT /note="LRR 4"
FT REPEAT 249..271
FT /note="LRR 5"
FT REPEAT 278..299
FT /note="LRR 6"
FT REPEAT 304..326
FT /note="LRR 7"
FT REPEAT 328..353
FT /note="LRR 8"
FT REPEAT 354..378
FT /note="LRR 9"
FT REPEAT 380..405
FT /note="LRR 10"
SQ SEQUENCE 463 AA; 52360 MW; 07435B3C28BB2073 CRC64;
MRVPNEVCFN ILSYLEADEL RCKSTVCTSW RNFIIPTLWE KVVFQNEAQL NNFFDTLQYS
KDVSYYFRYL RKLNCSRVRK FLTDKHLMLM TLATGISRLN LSGCTRISEP LIGKLLYQNL
NLVTINFSNI FSLPANILEY ISDNCPNLKA LNIGNCGLVE DTGMVQIIKR CPYLNRLIIP
NCRKLTDVSL QILSEKEDLI ELDISGCEGF HNADTLSRLV SRNRGLKELS MDGCTELSHF
ITFLNLNCEL DAMRALSLNN LPDLKDSDIE LITCKFSKLN SLFLSKCIGL TDSSLLSLTK
LSQSLTTLHL GHCYEITDIG VQCLLKSCKN ITYIDFGGCL RLSDIAVSAI AKLPYLQRVG
LVKCICLTDL SVILLSGSFS RNLERVHLSY CIGLTAKSVS YLMYNCKTLK HLSVTGINSI
LCTELRSFSR PIPDGINPSQ VPVFCAFTKV EIDLFREFIR NRI