RFA2B_XENLA
ID RFA2B_XENLA Reviewed; 274 AA.
AC A1L2H9;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Replication protein A 32 kDa subunit-B;
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-b; Synonyms=repa2, 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=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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:0000250}. Nucleus, PML body
CC {ECO:0000250}. Note=Redistributes to discrete nuclear foci upon DNA
CC 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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 2 family.
CC {ECO:0000305}.
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DR EMBL; BC129535; AAI29536.1; -; mRNA.
DR RefSeq; NP_001090609.1; NM_001097140.1.
DR AlphaFoldDB; A1L2H9; -.
DR SMR; A1L2H9; -.
DR DNASU; 100036853; -.
DR GeneID; 100036853; -.
DR KEGG; xla:100036853; -.
DR CTD; 100036853; -.
DR Xenbase; XB-GENE-17342450; rpa2.S.
DR OMA; EIASHFI; -.
DR OrthoDB; 924826at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 100036853; Expressed in ovary and 18 other tissues.
DR GO; GO:0000785; C:chromatin; ISS: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; ISS: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:2000001; P:regulation of DNA damage checkpoint; 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 2: Evidence at transcript level;
KW DNA damage; DNA recombination; DNA repair; DNA replication; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..274
FT /note="Replication protein A 32 kDa subunit-B"
FT /id="PRO_0000429835"
FT DNA_BIND 73..147
FT /note="OB"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 274 AA; 29379 MW; C3A6FBCD506A2D2F CRC64;
MWNNQGGFDG GSGMGGGGYM QSPGGFGSPA PTQGEKKSRS RSQQIVPCTV SQLLSATQND
EVFRIGETEL SQVIIVGIVR HAEKAPTNIL YKVDDMTAAP MDVRQWVDTD EASCENMVVP
PGSYVKVAGH LRSFQNKKSV VAFKIAPVDD MNEFVSHMLE VVHSHMVMNS QGAPSGGGST
MALNTPGRMG IGDSGGAFSG GNDNPTNGLT PHQNQILNLI KSCKGNEGMA FEELKNRLHG
MNVNSIRKTV DFLSNEGHIY STIDDEHYKS TDGD
