ID REV7_SCHPO Reviewed; 213 AA.
AC Q0E7J8;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=DNA polymerase zeta processivity subunit;
DE AltName: Full=Revertibility protein 7 {ECO:0000250|UniProtKB:P38927};
GN Name=rev7; ORFNames=SPAC12D12.09, SPBC12D12.09;
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] {ECO:0000312|EMBL:CAL45666.1}
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] {ECO:0000305}
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: Required for DNA damage induced mutagenesis. Involved in DNA
CC repair, mitochondrial DNA repair and translesion synthesis. Has a role
CC in the bypass of abasic (AP) sites (By similarity).
CC {ECO:0000250|UniProtKB:P38927}.
CC -!- SUBUNIT: Forms DNA polymerase zeta with rev3.
CC {ECO:0000250|UniProtKB:P38927}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the MAD2 family. {ECO:0000255}.
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DR EMBL; CU329671; CAL45666.1; -; Genomic_DNA.
DR RefSeq; XP_001713135.1; XM_001713083.2.
DR AlphaFoldDB; Q0E7J8; -.
DR SMR; Q0E7J8; -.
DR BioGRID; 276643; 14.
DR IntAct; Q0E7J8; 1.
DR STRING; 284812.Q0E7J8; -.
DR iPTMnet; Q0E7J8; -.
DR PaxDb; 4896-SPBC12D12-09-1; -.
DR EnsemblFungi; SPBC12D12.09.1; SPBC12D12.09.1:pep; SPBC12D12.09.
DR PomBase; SPBC12D12.09; rev7.
DR VEuPathDB; FungiDB:SPBC12D12.09; -.
DR eggNOG; KOG3186; Eukaryota.
DR HOGENOM; CLU_050394_1_1_1; -.
DR InParanoid; Q0E7J8; -.
DR OMA; DEASHEC; -.
DR Reactome; R-SPO-110312; Translesion synthesis by REV1.
DR Reactome; R-SPO-5655862; Translesion synthesis by POLK.
DR Reactome; R-SPO-5656121; Translesion synthesis by POLI.
DR PRO; PR:Q0E7J8; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000262; C:mitochondrial chromosome; IC:PomBase.
DR GO; GO:0043596; C:nuclear replication fork; IC:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0016035; C:zeta DNA polymerase complex; IBA:GO_Central.
DR GO; GO:0070987; P:error-free translesion synthesis; ISO:PomBase.
DR GO; GO:0042276; P:error-prone translesion synthesis; ISO:PomBase.
DR GO; GO:0043504; P:mitochondrial DNA repair; IC:PomBase.
DR Gene3D; 3.30.900.10; HORMA domain; 1.
DR InterPro; IPR003511; HORMA_dom.
DR InterPro; IPR036570; HORMA_dom_sf.
DR InterPro; IPR045091; Mad2-like.
DR PANTHER; PTHR11842; MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2; 1.
DR PANTHER; PTHR11842:SF10; MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2B; 1.
DR Pfam; PF02301; HORMA; 1.
DR SUPFAM; SSF56019; The spindle assembly checkpoint protein mad2; 1.
DR PROSITE; PS50815; HORMA; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; Mitochondrion; Nucleus; Reference proteome.
FT CHAIN 1..213
FT /note="DNA polymerase zeta processivity subunit"
FT /id="PRO_0000361056"
FT DOMAIN 10..206
FT /note="HORMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00109"
SQ SEQUENCE 213 AA; 25038 MW; EB42AE999B55549A CRC64;
MENDTGWSVK KCIDIFGEFL LVSIHCILYA RRLYPQDLFI KARKYNTIVW QSRHPILCEY
IEEVVQSCIE ELQTGSVHQV ALSIINKEQR EEERYVFSTD SIPIIPDFLL EKQISTNEPF
TDAYVEYMRA SLIQLLNITN GLPLIEQECT WTLRVTLKDG FPRPKQWEEW FLPPQARETD
ATRQFKGITI PVRNVDIGPM MTEIWVEKYT NSD
//
