RFA2A_XENLA
ID RFA2A_XENLA Reviewed; 276 AA.
AC Q6IP18;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Replication protein A 32 kDa subunit-A;
DE Short=RP-A p32;
DE AltName: Full=Replication factor A protein 2;
DE Short=RF-A protein 2;
DE AltName: Full=Replication protein A 34 kDa subunit;
DE Short=RP-A p34;
GN Name=rpa2-a; Synonyms=repa2, rpa2, rpa32, rpa34;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION IN REPLICATION CHECKPOINT ACTIVATION, MUTAGENESIS OF SER-26;
RP SER-32 AND THR-36, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=23047005; DOI=10.1016/j.bbrc.2012.09.139;
RA Recolin B., Maiorano D.;
RT "Implication of RPA32 phosphorylation in S-phase checkpoint signalling at
RT replication forks stalled with aphidicolin in Xenopus egg extracts.";
RL Biochem. Biophys. Res. Commun. 427:785-789(2012).
CC -!- FUNCTION: As part of the heterotrimeric replication protein A complex
CC (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates,
CC that form during DNA replication or upon DNA stress. It prevents their
CC reannealing and in parallel, recruits and activates different proteins
CC and complexes involved in DNA metabolism. Thereby, it plays an
CC essential role both in DNA replication and the cellular response to DNA
CC damage. {ECO:0000269|PubMed:23047005}.
CC -!- SUBUNIT: Component of the replication protein A complex (RPA/RP-A), a
CC heterotrimeric complex composed of RPA1, RPA2 and RPA3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23047005}. Nucleus,
CC PML body {ECO:0000250}. Note=Redistributes to discrete nuclear foci
CC upon DNA damage in an ATR-dependent manner. {ECO:0000250}.
CC -!- PTM: Differentially phosphorylated throughout the cell cycle, becoming
CC phosphorylated at the G1-S transition and dephosphorylated in late
CC mitosis. Phosphorylation increases upon replication fork stalling.
CC {ECO:0000269|PubMed:23047005}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 2 family.
CC {ECO:0000305}.
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DR EMBL; BC072101; AAH72101.1; -; mRNA.
DR RefSeq; NP_001085393.1; NM_001091924.1.
DR AlphaFoldDB; Q6IP18; -.
DR SMR; Q6IP18; -.
DR DNASU; 443819; -.
DR GeneID; 443819; -.
DR KEGG; xla:443819; -.
DR CTD; 443819; -.
DR Xenbase; XB-GENE-865703; rpa2.L.
DR OMA; TYKIDDG; -.
DR OrthoDB; 924826at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 443819; Expressed in blastula and 19 other tissues.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005662; C:DNA replication factor A complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0003684; F:damaged DNA binding; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0006284; P:base-excision repair; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0006298; P:mismatch repair; ISS:UniProtKB.
DR GO; GO:0006289; P:nucleotide-excision repair; ISS:UniProtKB.
DR GO; GO:0034502; P:protein localization to chromosome; ISS:UniProtKB.
DR GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR040260; RFA2-like.
DR InterPro; IPR014646; Rfa2/RPA32.
DR InterPro; IPR014892; RPA_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13989; PTHR13989; 1.
DR Pfam; PF08784; RPA_C; 1.
DR PIRSF; PIRSF036949; RPA32; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA recombination; DNA repair; DNA replication; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..276
FT /note="Replication protein A 32 kDa subunit-A"
FT /id="PRO_0000429834"
FT DNA_BIND 77..151
FT /note="OB"
FT REGION 19..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 26
FT /note="S->A: Not phosphorylated but normally recruited to
FT chromatin and able to stimulate replication checkpoint
FT signaling upon replication fork stalling; when associated
FT with A-32 and A-36."
FT /evidence="ECO:0000269|PubMed:23047005"
FT MUTAGEN 32
FT /note="S->A: Not phosphorylated but normally recruited to
FT chromatin and able to stimulate replication checkpoint
FT signaling upon replication fork stalling; when associated
FT with A-26 and A-36."
FT /evidence="ECO:0000269|PubMed:23047005"
FT MUTAGEN 36
FT /note="T->A: Not phosphorylated but normally recruited to
FT chromatin and able to stimulate replication checkpoint
FT signaling upon replication fork stalling; when associated
FT with A-26 and A-32."
FT /evidence="ECO:0000269|PubMed:23047005"
SQ SEQUENCE 276 AA; 29448 MW; CD3D37D315E84EE1 CRC64;
MWNNHGGFDG GYGGSGMGGG GGYMQSPGGF GSPAPTQGEK KSRSRSQQIV PCTVSQLLSA
TQNDEVFRIG EAELSQVTIV GIVRHAEKAP TNILYKVDDM TAAPMDVRQW VDTDEASCEN
MVVPPGSYVK VAGHLRSFQN KKSVVAFKIA PVEDMNEFVS HMLEVVHAHM AMNSQGAPSG
GGSTVALSTP GRVGDSGRAF SGGNDNPTNG LTPHQSQILS LIKSCKGNEG MAFEELKNRL
HGMNVNTIRQ AVEFLSNEGH IYSTIDDEHY KCTDGD
