POF14_SCHPO
ID POF14_SCHPO Reviewed; 431 AA.
AC Q10223;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=F-box protein pof14;
GN Name=pof14; ORFNames=SPAC13D6.01;
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 [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 [2]
RP FUNCTION, INTERACTION WITH CUL1; ERG9 AND SKP1, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RX PubMed=17016471; DOI=10.1038/sj.emboj.7601329;
RA Tafforeau L., Le Blastier S., Bamps S., Dewez M., Vandenhaute J.,
RA Hermand D.;
RT "Repression of ergosterol level during oxidative stress by fission yeast F-
RT box protein Pof14 independently of SCF.";
RL EMBO J. 25:4547-4556(2006).
RN [3]
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: Expression is induced during oxidative stress. Plays an
CC essential, SCF-independent, role in the stress response to hydrogen
CC peroxide for survival, by negatively regulating ergosterol synthesis
CC via direct binding to the squalene synthase erg9.
CC {ECO:0000269|PubMed:17016471}.
CC -!- SUBUNIT: Component of the E3 ubiquitin ligase Skp1-Cullin-1-F-box (SCF)
CC complex. Interacts with skp1, cul1 and erg9.
CC {ECO:0000269|PubMed:17016471}.
CC -!- INTERACTION:
CC Q10223; P36596: erg9; NbExp=5; IntAct=EBI-1793014, EBI-1794119;
CC Q10223; Q9Y709: skp1; NbExp=5; IntAct=EBI-1793014, EBI-1172248;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Endoplasmic reticulum.
CC Note=Associated with vesicle-like and endoplasmic reticulum (excluding
CC a nuclear rim) structures.
CC -!- INDUCTION: Expression is induced during oxidative stress.
CC {ECO:0000269|PubMed:17016471}.
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DR EMBL; CU329670; CAA93541.1; -; Genomic_DNA.
DR PIR; T37621; T37621.
DR RefSeq; NP_593679.1; NM_001019111.2.
DR AlphaFoldDB; Q10223; -.
DR BioGRID; 279262; 21.
DR IntAct; Q10223; 6.
DR MINT; Q10223; -.
DR STRING; 4896.SPAC13D6.01.1; -.
DR MaxQB; Q10223; -.
DR PaxDb; Q10223; -.
DR PRIDE; Q10223; -.
DR EnsemblFungi; SPAC13D6.01.1; SPAC13D6.01.1:pep; SPAC13D6.01.
DR GeneID; 2542815; -.
DR KEGG; spo:SPAC13D6.01; -.
DR PomBase; SPAC13D6.01; pof14.
DR VEuPathDB; FungiDB:SPAC13D6.01; -.
DR HOGENOM; CLU_694751_0_0_1; -.
DR OMA; WLSEHVQ; -.
DR PRO; PR:Q10223; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:PomBase.
DR GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:PomBase.
DR GO; GO:0032443; P:regulation of ergosterol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IPI:PomBase.
DR InterPro; IPR001810; F-box_dom.
DR Pfam; PF13013; F-box-like_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..431
FT /note="F-box protein pof14"
FT /id="PRO_0000116488"
FT DOMAIN 172..186
FT /note="F-box; atypical"
SQ SEQUENCE 431 AA; 49624 MW; 132FB0919646AC9F CRC64;
MLQFSFQNCK THTCYMNTSV NEHLDQDESF LRILIDTRKK IRSSYFKPQT FDEFVHCLAR
VRAMKRLVSI CSNFDEEDNW NGVWNTLVVD GDSHASAMID YEGLLDKCSL SRNLLELIND
YAEYTTQVLP FRKIPSSDNL DSSLNLTVAS PKSNLYYRYS SESPKYAKIL DCPDEILQLI
FSYCYDASYI EKLPFAFSYR KQRHTLIHDL PNTCLRFKKI LSPRNVSFWK RLLKVHKKNP
NSAVTCSESI NTSAVAKFTD IPTIIPIFLD PSYQSYAAKT IHSDTSSLAS SIIQTGDGTQ
SCDESTYIEL ACNLVGRCVL CNRIPKLTKF KDCITSFYRP SVATNICDQC LEAIIDFYEP
VSRYKFDVMK DRLGVGYISR PGQKFPSWLS EHVQLARDEE KAFKSIYHSQ GEFARSLFRL
FRAQLAELCE Q
