ERCC1_ARATH
ID ERCC1_ARATH Reviewed; 410 AA.
AC Q9MA98;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=DNA excision repair protein ERCC-1;
DE Short=AtERCC1;
DE Short=AtRAD10;
DE EC=3.1.-.-;
DE AltName: Full=Ultraviolet hypersensitive 7;
GN Name=ERCC1; Synonyms=RAD10, UVR7; OrderedLocusNames=At3g05210;
GN ORFNames=T12H1.18;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Vonarx E.J., Anderson H.J., Kunz B.A.;
RT "A RAD10/ERCC1 homolog from Arabidopsis thaliana.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RX PubMed=12554710; DOI=10.1093/jxb/erg069;
RA Hefner E., Preuss S.B., Britt A.B.;
RT "Arabidopsis mutants sensitive to gamma radiation include the homologue of
RT the human repair gene ERCC1.";
RL J. Exp. Bot. 54:669-680(2003).
RN [7]
RP FUNCTION.
RX PubMed=15255863; DOI=10.1111/j.1365-313x.2004.02136.x;
RA Dubest S., Gallego M.E., White C.I.;
RT "Roles of the AtErcc1 protein in recombination.";
RL Plant J. 39:334-342(2004).
CC -!- FUNCTION: Seems to be involved in nucleotide excision repair (NER) of
CC damaged DNA (dark repair mechanism). The UVH1/RAD1-ERCC1/RAD10 complex
CC may act as an endonuclease making DNA incision 5' to the lesion site.
CC In vitro, is implicated in double strand breaks (DSBs) repair and is
CC required for homologous recombination in the presence of non-homologous
CC overhangs. In vitro, is involved in chromosomal recombination between
CC tandem repeats in both direct and inverted orientations. May mediate
CC the induction of a DNA-damage sensitive cell-cycle checkpoint during
CC the G2 phase. {ECO:0000269|PubMed:12554710,
CC ECO:0000269|PubMed:15255863}.
CC -!- SUBUNIT: Heterodimer with UVH1/RAD1. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ERCC1/RAD10/SWI10 family. {ECO:0000305}.
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; AF276082; AAF99316.1; -; mRNA.
DR EMBL; AC009177; AAF27027.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74205.1; -; Genomic_DNA.
DR EMBL; AY050335; AAK91352.1; -; mRNA.
DR EMBL; AY116935; AAM51569.1; -; mRNA.
DR EMBL; AY088915; AAM67221.1; -; mRNA.
DR RefSeq; NP_187172.1; NM_111394.5.
DR AlphaFoldDB; Q9MA98; -.
DR SMR; Q9MA98; -.
DR BioGRID; 5020; 3.
DR IntAct; Q9MA98; 3.
DR STRING; 3702.AT3G05210.1; -.
DR iPTMnet; Q9MA98; -.
DR PaxDb; Q9MA98; -.
DR PRIDE; Q9MA98; -.
DR ProteomicsDB; 220620; -.
DR EnsemblPlants; AT3G05210.1; AT3G05210.1; AT3G05210.
DR GeneID; 819685; -.
DR Gramene; AT3G05210.1; AT3G05210.1; AT3G05210.
DR KEGG; ath:AT3G05210; -.
DR Araport; AT3G05210; -.
DR TAIR; locus:2096329; AT3G05210.
DR eggNOG; KOG2841; Eukaryota.
DR HOGENOM; CLU_041616_4_0_1; -.
DR InParanoid; Q9MA98; -.
DR OrthoDB; 1336192at2759; -.
DR PhylomeDB; Q9MA98; -.
DR PRO; PR:Q9MA98; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9MA98; baseline and differential.
DR Genevisible; Q9MA98; AT.
DR GO; GO:0070522; C:ERCC4-ERCC1 complex; IBA:GO_Central.
DR GO; GO:0000110; C:nucleotide-excision repair factor 1 complex; IBA:GO_Central.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IMP:TAIR.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:TAIR.
DR GO; GO:0000710; P:meiotic mismatch repair; IBA:GO_Central.
DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR GO; GO:0010213; P:non-photoreactive DNA repair; IMP:TAIR.
DR GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; IBA:GO_Central.
DR GO; GO:0006294; P:nucleotide-excision repair, preincision complex assembly; IMP:TAIR.
DR GO; GO:0010332; P:response to gamma radiation; IMP:TAIR.
DR GO; GO:0010224; P:response to UV-B; IMP:TAIR.
DR GO; GO:0070914; P:UV-damage excision repair; IBA:GO_Central.
DR InterPro; IPR004579; ERCC1/RAD10/SWI10.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR010994; RuvA_2-like.
DR PANTHER; PTHR12749; PTHR12749; 1.
DR Pfam; PF03834; Rad10; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR TIGRFAMs; TIGR00597; rad10; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA excision; DNA recombination; DNA repair; DNA-binding;
KW Endonuclease; Hydrolase; Nuclease; Nucleus; Reference proteome.
FT CHAIN 1..410
FT /note="DNA excision repair protein ERCC-1"
FT /id="PRO_0000087005"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 410 AA; 45748 MW; D443AA3C89289AD9 CRC64;
MANEDDDGEK SRSLHQQIAR KPKTQIVIGV PSYQEVLESS QTKSTPPSLF KPSQSFSQAF
AFVKSSDVYS PPPPSSAAAS SSQPSGASQV PHSSSQTHQT DGASSSSTPV ATGSVPSNTT
QNRNAILVSH RQKGNPLLKH IRNVKWVFSD IIPDYVLGQN SCALYLSLRY HLLHPDYLYF
RIRELQKNFK LSVVLCHVDV EDTVKPLLEV TKTALLHDCT LLCAWSMTEC ARYLETIKVY
ENKPADLIQG QMDTDYLSRL NHSLTSIRHV NKSDVVTLGS TFGSLAHIID ASMEDLARCP
GIGERKVKRL YDTFHEPFKR ATSSYPSVVE PPIPEAPVEK DVNSEEPVEE DEDFVEDSRK
RKKKEPEPEK TVKTALSAVF ARYSDRLSKK KEKQKEKDTT TASDAETHQN
