UVI31_SCHPO
ID UVI31_SCHPO Reviewed; 102 AA.
AC Q12238;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=UV-induced protein uvi31 {ECO:0000303|PubMed:12521307, ECO:0000303|PubMed:9258332};
DE AltName: Full=BolA-like protein 1 {ECO:0000305};
GN Name=uvi31 {ECO:0000303|PubMed:12521307, ECO:0000303|PubMed:9258332};
GN ORFNames=SPBC16E9.06c {ECO:0000312|PomBase:SPBC16E9.06c};
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], DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=JY741 {ECO:0000303|PubMed:9258332};
RX PubMed=9258332;
RX DOI=10.1002/(sici)1098-2280(1997)30:1<72::aid-em10>3.0.co;2-n;
RA Kim S.H., Kim M., Lee J.K., Kim M.J., Jin Y.H., Seong R.H., Hong S.H.,
RA Joe C.O., Park S.D.;
RT "Identification and expression of uvi31+, a UV-inducible gene from
RT Schizosaccharomyces pombe.";
RL Environ. Mol. Mutagen. 30:72-81(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=JY741 {ECO:0000303|PubMed:12521307};
RX PubMed=12521307;
RA Kim M.J., Kim H.S., Lee J.K., Lee C.B., Park S.D.;
RT "Regulation of septation and cytokinesis during resumption of cell division
RT requires uvi31+, a UV-inducible gene of fission yeast.";
RL Mol. Cells 14:425-430(2002).
RN [3]
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 [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: Acts as a mitochondrial iron-sulfur (Fe-S) cluster assembly
CC factor that facilitates [4Fe-4S] cluster insertion into a subset of
CC mitochondrial proteins such as lipoyl synthase (LS) and succinate
CC dehydrogenase (SDH). Required during the last step of iron-sulfur
CC protein assembly when the iron-sulfur cluster is inserted into the
CC target protein. Probably acts together with the monothiol glutaredoxin
CC grx5. Not required for [2Fe-2S] cluster insertion into mitochondrial
CC proteins (By similarity). May be involved in control of cell division,
CC especially during the resumption from cell cycle arrest
CC (PubMed:12521307). {ECO:0000250|UniProtKB:Q3E793,
CC ECO:0000269|PubMed:12521307}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q3E793}. Cytoplasm
CC {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- DEVELOPMENTAL STAGE: Expression varies throughout the cell cycle, with
CC the highest expression in G1 phase before septation. Expression is also
CC increased after S phase arrest. {ECO:0000269|PubMed:9258332}.
CC -!- INDUCTION: Expression shows cellular growth phase dependency, with the
CC maximal expression at the diauxic shift. Expression is rapidly
CC decreased when cells approach stationary phase (PubMed:9258332). By UV
CC light (PubMed:12521307, PubMed:9258332). Expressed maximally (3.2-fold)
CC at 4 hours after exposure to 240 J/m(2) of UV light (PubMed:9258332).
CC {ECO:0000269|PubMed:12521307, ECO:0000269|PubMed:9258332}.
CC -!- DISRUPTION PHENOTYPE: Leads to delayed spore germination and the
CC unidirectional cell extension is not followed by cell division.
CC Proliferates faster with smaller cell size than the wild-type cell
CC during vegetative growth, but no other significant cellular anomaly,
CC such as defects in septation or cytokinesis are detected. Sensitive to
CC UV light. Shows a normal cell cycle delay after UV irradiation, but
CC displays aberrant septum formation and defects in cytokinesis when
CC released from the UV damage checkpoint. However, chromosome segregation
CC is not affected. {ECO:0000269|PubMed:12521307}.
CC -!- SIMILARITY: Belongs to the BolA/IbaG family. {ECO:0000305}.
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DR EMBL; Z72498; CAA96579.1; -; Genomic_DNA.
DR EMBL; U57848; AAB02694.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB16898.1; -; Genomic_DNA.
DR PIR; T39580; T39580.
DR RefSeq; NP_595788.1; NM_001021689.2.
DR AlphaFoldDB; Q12238; -.
DR SMR; Q12238; -.
DR BioGRID; 276405; 2.
DR STRING; 4896.SPBC16E9.06c.1; -.
DR MaxQB; Q12238; -.
DR PaxDb; Q12238; -.
DR EnsemblFungi; SPBC16E9.06c.1; SPBC16E9.06c.1:pep; SPBC16E9.06c.
DR GeneID; 2539858; -.
DR KEGG; spo:SPBC16E9.06c; -.
DR PomBase; SPBC16E9.06c; uvi31.
DR VEuPathDB; FungiDB:SPBC16E9.06c; -.
DR eggNOG; KOG2313; Eukaryota.
DR HOGENOM; CLU_109462_2_1_1; -.
DR InParanoid; Q12238; -.
DR OMA; HKHAGHY; -.
DR PhylomeDB; Q12238; -.
DR PRO; PR:Q12238; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0106035; P:protein maturation by [4Fe-4S] cluster transfer; ISO:PomBase.
DR Gene3D; 3.30.300.90; -; 1.
DR InterPro; IPR002634; BolA.
DR InterPro; IPR036065; BolA-like_sf.
DR Pfam; PF01722; BolA; 1.
DR PIRSF; PIRSF003113; BolA; 1.
DR SUPFAM; SSF82657; SSF82657; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Cytoplasm; Mitochondrion; Nucleus;
KW Reference proteome.
FT CHAIN 1..102
FT /note="UV-induced protein uvi31"
FT /id="PRO_0000201231"
SQ SEQUENCE 102 AA; 11806 MW; 1B336DF20988E8D4 CRC64;
MIRRFFHTMG RQDRIYKTLS EALKTDKITL YNDSYKHSHH IAMKGVPDTN ETHFRLEIVS
PEFSGMSRVA RHRLVYGLLK DEFDGGLHAL QITSSKTPDE VS
