RFA2_XENTR
ID RFA2_XENTR Reviewed; 275 AA.
AC Q6DFS2;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Replication protein A 32 kDa subunit;
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; Synonyms=repa2, rpa32, rpa34;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) 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. {ECO:0000250|UniProtKB:P15927}.
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}.
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; BC076661; AAH76661.1; -; mRNA.
DR RefSeq; NP_001006795.1; NM_001006794.1.
DR AlphaFoldDB; Q6DFS2; -.
DR SMR; Q6DFS2; -.
DR STRING; 8364.ENSXETP00000061861; -.
DR PaxDb; Q6DFS2; -.
DR DNASU; 448500; -.
DR GeneID; 448500; -.
DR KEGG; xtr:448500; -.
DR CTD; 6118; -.
DR Xenbase; XB-GENE-487430; rpa2.
DR eggNOG; KOG3108; Eukaryota.
DR OrthoDB; 924826at2759; -.
DR Reactome; R-XTR-110312; Translesion synthesis by REV1.
DR Reactome; R-XTR-176187; Activation of ATR in response to replication stress.
DR Reactome; R-XTR-5655862; Translesion synthesis by POLK.
DR Reactome; R-XTR-5656121; Translesion synthesis by POLI.
DR Reactome; R-XTR-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-XTR-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-XTR-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-XTR-5696400; Dual Incision in GG-NER.
DR Reactome; R-XTR-6782135; Dual incision in TC-NER.
DR Reactome; R-XTR-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-XTR-68962; Activation of the pre-replicative complex.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; IBA:GO_Central.
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:0035861; C:site of double-strand break; IBA:GO_Central.
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..275
FT /note="Replication protein A 32 kDa subunit"
FT /id="PRO_0000429836"
FT DNA_BIND 76..150
FT /note="OB"
FT REGION 23..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 275 AA; 29352 MW; B45BF3A344723365 CRC64;
MWNNHGGFDG GYGGSGMGGG GYMQSPGGFG SPAPTQGEKK SRSRSQQIVP CTVSQLLSAT
QNDEMFRIGE AELSQVTIVG IVRHAEKAPT NILYKVDDMT AAPMDVRQWV DTDEASCENM
VVPPGSYVKV AGHLRSFQNK KSVVAFKIAP VDDMNEFVSH MLEVVHAHMT MNSQGAPSGG
GSAVALNTPG RLGDSGGAFS GGNDNATNGL TPHQSQILNL IKSFKGNEGM AFEELKNRLH
GMNVNTIRQA VDFLSNEGHI YSTVDDEHYK STDGD
