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Protein

Replication protein A 14 kDa subunit

Gene

Rpa3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin, in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Plays also a role in base excision repair (BER), probably through interaction with UNG. Through RFWD3 may activate CHEK1 and play a role in replication checkpoint control. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. RPA3 has its own single-stranded DNA-binding activity and may be responsible for polarity of the binding of the complex to DNA.By similarity

GO - Molecular functioni

GO - Biological processi

  • base-excision repair Source: MGI
  • DNA replication Source: MGI
  • double-strand break repair via homologous recombination Source: MGI
  • mismatch repair Source: MGI
  • nucleotide-excision repair Source: MGI
  • regulation of cell proliferation Source: MGI
  • regulation of mitotic cell cycle Source: MGI
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair, DNA replication

Enzyme and pathway databases

ReactomeiR-MMU-110312. Translesion synthesis by REV1.
R-MMU-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-MMU-110320. Translesion Synthesis by POLH.
R-MMU-174437. Removal of the Flap Intermediate from the C-strand.
R-MMU-176187. Activation of ATR in response to replication stress.
R-MMU-3371453. Regulation of HSF1-mediated heat shock response.
R-MMU-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
R-MMU-5358606. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
R-MMU-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-MMU-5655862. Translesion synthesis by POLK.
R-MMU-5656121. Translesion synthesis by POLI.
R-MMU-5656169. Termination of translesion DNA synthesis.
R-MMU-5685938. HDR through Single Strand Annealing (SSA).
R-MMU-5685942. HDR through Homologous Recombination (HRR).
R-MMU-5693607. Processing of DNA double-strand break ends.
R-MMU-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-MMU-5696395. Formation of Incision Complex in GG-NER.
R-MMU-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-MMU-5696400. Dual Incision in GG-NER.
R-MMU-6782135. Dual incision in TC-NER.
R-MMU-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-MMU-6783310. Fanconi Anemia Pathway.
R-MMU-6804756. Regulation of TP53 Activity through Phosphorylation.
R-MMU-68962. Activation of the pre-replicative complex.
R-MMU-69166. Removal of the Flap Intermediate.
R-MMU-69473. G2/M DNA damage checkpoint.
R-MMU-912446. Meiotic recombination.
R-MMU-912497. Meiotic Recombination.

Names & Taxonomyi

Protein namesi
Recommended name:
Replication protein A 14 kDa subunit
Short name:
RP-A p14
Alternative name(s):
Replication factor A protein 3
Short name:
RF-A protein 3
Gene namesi
Name:Rpa3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1915490. Rpa3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 121120Replication protein A 14 kDa subunitPRO_0000097277Add
BLAST

Proteomic databases

EPDiQ9CQ71.
MaxQBiQ9CQ71.
PaxDbiQ9CQ71.
PeptideAtlasiQ9CQ71.
PRIDEiQ9CQ71.

PTM databases

PhosphoSiteiQ9CQ71.

Expressioni

Gene expression databases

BgeeiENSMUSG00000012483.
CleanExiMM_RPA3.
GenevisibleiQ9CQ71. MM.

Interactioni

Subunit structurei

Component of the canonical replication protein A complex (RPA), a heterotrimer composed of RPA1, RPA2 and RPA3. Also component of the aRPA, the alternative replication protein A complex, a trimeric complex similar to the replication protein A complex/RPA but where RPA1 and RPA3 are associated with RPA4 instead of RPA2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi212756. 2 interactions.
IntActiQ9CQ71. 3 interactions.
STRINGi10090.ENSMUSP00000012627.

Structurei

3D structure databases

ProteinModelPortaliQ9CQ71.
SMRiQ9CQ71. Positions 3-116.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiENOG410IZRM. Eukaryota.
ENOG4111REI. LUCA.
GeneTreeiENSGT00390000008029.
HOGENOMiHOG000252930.
HOVERGENiHBG003004.
InParanoidiQ9CQ71.
KOiK10740.
OMAiKPRINCS.
OrthoDBiEOG091G1178.
PhylomeDBiQ9CQ71.
TreeFamiTF105243.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR013970. Rfa2.
[Graphical view]
PfamiPF08661. Rep_fac-A_3. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CQ71-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDIMQLPKA RVNASMLPQY IDRPVCFVGK LEKIHPTGKM FILSDGEGKN
60 70 80 90 100
GTIELMEPLD EEISGIVEVV GKVTAKATVL CASYTLFKED TNRFDLELYN
110 120
EAVKIINELP QFFPVGLPQH E
Length:121
Mass (Da):13,584
Last modified:June 1, 2001 - v1
Checksum:iBC108B58ABB59190
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005285 mRNA. Translation: BAB23932.1.
AK009916 mRNA. Translation: BAB26583.1.
AK021228 mRNA. Translation: BAB32338.1.
BC028489 mRNA. Translation: AAH28489.1.
CCDSiCCDS19909.1.
RefSeqiNP_080908.1. NM_026632.4.
UniGeneiMm.29073.

Genome annotation databases

EnsembliENSMUST00000012627; ENSMUSP00000012627; ENSMUSG00000012483.
GeneIDi68240.
KEGGimmu:68240.
UCSCiuc009axl.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005285 mRNA. Translation: BAB23932.1.
AK009916 mRNA. Translation: BAB26583.1.
AK021228 mRNA. Translation: BAB32338.1.
BC028489 mRNA. Translation: AAH28489.1.
CCDSiCCDS19909.1.
RefSeqiNP_080908.1. NM_026632.4.
UniGeneiMm.29073.

3D structure databases

ProteinModelPortaliQ9CQ71.
SMRiQ9CQ71. Positions 3-116.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212756. 2 interactions.
IntActiQ9CQ71. 3 interactions.
STRINGi10090.ENSMUSP00000012627.

PTM databases

PhosphoSiteiQ9CQ71.

Proteomic databases

EPDiQ9CQ71.
MaxQBiQ9CQ71.
PaxDbiQ9CQ71.
PeptideAtlasiQ9CQ71.
PRIDEiQ9CQ71.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000012627; ENSMUSP00000012627; ENSMUSG00000012483.
GeneIDi68240.
KEGGimmu:68240.
UCSCiuc009axl.2. mouse.

Organism-specific databases

CTDi6119.
MGIiMGI:1915490. Rpa3.

Phylogenomic databases

eggNOGiENOG410IZRM. Eukaryota.
ENOG4111REI. LUCA.
GeneTreeiENSGT00390000008029.
HOGENOMiHOG000252930.
HOVERGENiHBG003004.
InParanoidiQ9CQ71.
KOiK10740.
OMAiKPRINCS.
OrthoDBiEOG091G1178.
PhylomeDBiQ9CQ71.
TreeFamiTF105243.

Enzyme and pathway databases

ReactomeiR-MMU-110312. Translesion synthesis by REV1.
R-MMU-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-MMU-110320. Translesion Synthesis by POLH.
R-MMU-174437. Removal of the Flap Intermediate from the C-strand.
R-MMU-176187. Activation of ATR in response to replication stress.
R-MMU-3371453. Regulation of HSF1-mediated heat shock response.
R-MMU-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
R-MMU-5358606. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
R-MMU-5651801. PCNA-Dependent Long Patch Base Excision Repair.
R-MMU-5655862. Translesion synthesis by POLK.
R-MMU-5656121. Translesion synthesis by POLI.
R-MMU-5656169. Termination of translesion DNA synthesis.
R-MMU-5685938. HDR through Single Strand Annealing (SSA).
R-MMU-5685942. HDR through Homologous Recombination (HRR).
R-MMU-5693607. Processing of DNA double-strand break ends.
R-MMU-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-MMU-5696395. Formation of Incision Complex in GG-NER.
R-MMU-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-MMU-5696400. Dual Incision in GG-NER.
R-MMU-6782135. Dual incision in TC-NER.
R-MMU-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-MMU-6783310. Fanconi Anemia Pathway.
R-MMU-6804756. Regulation of TP53 Activity through Phosphorylation.
R-MMU-68962. Activation of the pre-replicative complex.
R-MMU-69166. Removal of the Flap Intermediate.
R-MMU-69473. G2/M DNA damage checkpoint.
R-MMU-912446. Meiotic recombination.
R-MMU-912497. Meiotic Recombination.

Miscellaneous databases

PROiQ9CQ71.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000012483.
CleanExiMM_RPA3.
GenevisibleiQ9CQ71. MM.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR013970. Rfa2.
[Graphical view]
PfamiPF08661. Rep_fac-A_3. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRFA3_MOUSE
AccessioniPrimary (citable) accession number: Q9CQ71
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 2001
Last modified: September 7, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.