RAD14_SCHPO
ID RAD14_SCHPO Reviewed; 289 AA.
AC O59753;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=DNA repair protein rad14 {ECO:0000305};
DE AltName: Full=XP-A family homolog rhp14 {ECO:0000303|PubMed:11408483};
GN Name=rhp14 {ECO:0000303|PubMed:11408483};
GN Synonyms=rad14 {ECO:0000312|PomBase:SPBC649.03};
GN ORFNames=SPBC649.03 {ECO:0000312|PomBase:SPBC649.03};
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.
RX PubMed=10080187; DOI=10.1038/6838;
RA Fleck O., Lehmann E., Schaer P., Kohli J.;
RT "Involvement of nucleotide-excision repair in msh2 pms1-independent
RT mismatch repair.";
RL Nat. Genet. 21:314-317(1999).
RN [3]
RP FUNCTION.
RX PubMed=11408483; DOI=10.1074/jbc.m104039200;
RA Hohl M., Christensen O., Kunz C., Naegeli H., Fleck O.;
RT "Binding and repair of mismatched DNA mediated by Rhp14, the fission yeast
RT homologue of human XPA.";
RL J. Biol. Chem. 276:30766-30772(2001).
RN [4]
RP FUNCTION, AND INTERACTION WITH HRQ1.
RX PubMed=22064477; DOI=10.1128/mcb.06184-11;
RA Groocock L.M., Prudden J., Perry J.J., Boddy M.N.;
RT "The RecQ4 orthologue Hrq1 is critical for DNA interstrand cross-link
RT repair and genome stability in fission yeast.";
RL Mol. Cell. Biol. 32:276-287(2012).
CC -!- FUNCTION: Involved in nucleotide excision repair (NER). Functional in
CC repair of ultraviolet radiation induced damages and in mitotic mutation
CC avoidance. Binds damaged DNA. Binds specifically to base-base
CC mismatches or small insertion/deletion loops with unpaired nucleotides.
CC Maintains GT repeat stability. Functions as a part of the short-patch
CC excision repair system. {ECO:0000269|PubMed:10080187,
CC ECO:0000269|PubMed:11408483, ECO:0000269|PubMed:22064477}.
CC -!- SUBUNIT: Interacts with hrq1. {ECO:0000269|PubMed:22064477}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P28519}.
CC -!- SIMILARITY: Belongs to the XPA family. {ECO:0000255}.
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DR EMBL; CU329671; CAA19045.1; -; Genomic_DNA.
DR PIR; T40596; T40596.
DR RefSeq; NP_595222.1; NM_001021128.2.
DR AlphaFoldDB; O59753; -.
DR SMR; O59753; -.
DR BioGRID; 277635; 100.
DR STRING; 4896.SPBC649.03.1; -.
DR iPTMnet; O59753; -.
DR MaxQB; O59753; -.
DR PaxDb; O59753; -.
DR PRIDE; O59753; -.
DR EnsemblFungi; SPBC649.03.1; SPBC649.03.1:pep; SPBC649.03.
DR GeneID; 2541120; -.
DR KEGG; spo:SPBC649.03; -.
DR PomBase; SPBC649.03; rhp14.
DR VEuPathDB; FungiDB:SPBC649.03; -.
DR eggNOG; KOG4017; Eukaryota.
DR HOGENOM; CLU_053731_0_1_1; -.
DR InParanoid; O59753; -.
DR OMA; MMLFLRF; -.
DR PhylomeDB; O59753; -.
DR Reactome; R-SPO-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-SPO-5696400; Dual Incision in GG-NER.
DR Reactome; R-SPO-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR PRO; PR:O59753; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000110; C:nucleotide-excision repair factor 1 complex; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; ISO:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IGI:PomBase.
DR GO; GO:1901255; P:nucleotide-excision repair involved in interstrand cross-link repair; IMP:PomBase.
DR GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; IBA:GO_Central.
DR GO; GO:0033683; P:nucleotide-excision repair, DNA incision; ISO:PomBase.
DR GO; GO:0070914; P:UV-damage excision repair; IMP:PomBase.
DR Gene3D; 3.90.530.10; -; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR000465; XPA.
DR InterPro; IPR022656; XPA_C.
DR InterPro; IPR037129; XPA_sf.
DR InterPro; IPR022652; Znf_XPA_CS.
DR PANTHER; PTHR10142; PTHR10142; 1.
DR Pfam; PF05181; XPA_C; 1.
DR Pfam; PF01286; XPA_N; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
DR TIGRFAMs; TIGR00598; rad14; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..289
FT /note="DNA repair protein rad14"
FT /id="PRO_0000274248"
FT ZN_FING 116..140
FT /evidence="ECO:0000250|UniProtKB:P28519"
SQ SEQUENCE 289 AA; 34663 MW; F9C2D8B582D30D6F CRC64;
MENSSIVKSP NPTIEEQRNE IEKLKNLTGI EEVHVDGAKV NKRKRTFDEQ SEITKDYIEY
DFSKIEDTKG GYLLEEKKVE DLREKPAERE LREQEERQKK LRLAPLNLDP ETAPKCFECD
SIELDTKYFD IFHCRVCHTC REKYPDKYSL LTKTECKLDY LLTEPELQDQ ELLPRLLKAN
PHQQGWSNMM LYLRYQVEEF AKKKWGSMEA LDAEFERREV QKKEMKEKKF EKQLLELRKR
TRTSNYSRMS IREKRKHVHS YDEEFEKPNE PGVIVQRCKC GLEIEQLEI
