IRC21_YEAST
ID IRC21_YEAST Reviewed; 201 AA.
AC Q04772; D6VZP7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Increased recombination centers protein 21;
GN Name=IRC21; OrderedLocusNames=YMR073C; ORFNames=YM9916.12C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP FUNCTION.
RX PubMed=16121259; DOI=10.1371/journal.pgen.0010024;
RA Lee W., St Onge R.P., Proctor M., Flaherty P., Jordan M.I., Arkin A.P.,
RA Davis R.W., Nislow C., Giaever G.;
RT "Genome-wide requirements for resistance to functionally distinct DNA-
RT damaging agents.";
RL PLoS Genet. 1:235-246(2005).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=18085829; DOI=10.1371/journal.pgen.0030228;
RA Alvaro D., Lisby M., Rothstein R.;
RT "Genome-wide analysis of Rad52 foci reveals diverse mechanisms impacting
RT recombination.";
RL PLoS Genet. 3:E228-E228(2007).
CC -!- FUNCTION: Involved in resistance to carboplatin and cisplatin. Is
CC probably involved in a pathway contributing to genomic integrity.
CC {ECO:0000269|PubMed:16121259}.
CC -!- DISRUPTION PHENOTYPE: Displays increased levels of spontaneous RAD52
CC foci in proliferating diploid cells. {ECO:0000269|PubMed:18085829}.
CC -!- MISCELLANEOUS: Present with 450 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cytochrome b5 family. {ECO:0000305}.
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DR EMBL; Z48952; CAA88798.1; -; Genomic_DNA.
DR EMBL; AY557971; AAS56297.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09971.1; -; Genomic_DNA.
DR PIR; S52833; S52833.
DR RefSeq; NP_013789.1; NM_001182571.1.
DR AlphaFoldDB; Q04772; -.
DR SMR; Q04772; -.
DR BioGRID; 35248; 219.
DR STRING; 4932.YMR073C; -.
DR MaxQB; Q04772; -.
DR PaxDb; Q04772; -.
DR PRIDE; Q04772; -.
DR EnsemblFungi; YMR073C_mRNA; YMR073C; YMR073C.
DR GeneID; 855095; -.
DR KEGG; sce:YMR073C; -.
DR SGD; S000004677; IRC21.
DR VEuPathDB; FungiDB:YMR073C; -.
DR eggNOG; KOG0536; Eukaryota.
DR HOGENOM; CLU_046313_2_0_1; -.
DR InParanoid; Q04772; -.
DR OMA; YCITDYL; -.
DR BioCyc; YEAST:G3O-32775-MON; -.
DR PRO; PR:Q04772; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04772; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IGI:SGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; HMP:SGD.
DR Gene3D; 3.10.120.10; -; 1.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR018506; Cyt_B5_heme-BS.
DR Pfam; PF00173; Cyt-b5; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SUPFAM; SSF55856; SSF55856; 1.
DR PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Metal-binding; Reference proteome.
FT CHAIN 1..201
FT /note="Increased recombination centers protein 21"
FT /id="PRO_0000166039"
FT DOMAIN 122..200
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 158
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT BINDING 182
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
SQ SEQUENCE 201 AA; 23182 MW; 7686E1DEF08DDDFE CRC64;
MSSDGMNRDV SNSKPNVRFA APQRLSVAHP AISSPLHMPM SKSSRKPLVR TKIRLDPGHS
ALDWHSLTSN PANYYTKFVS LQLIQDLLDD PVFQKDNFKF SPSQLKNQLL VQKIPLYKIM
PPLRINRKIV KKHCKGEDEL WCVINGKVYD ISSYLKFHPG GTDILIKHRN SDDLITYFNK
YHQWVNYEKL LQVCFIGVVC E
