RFA4_HUMAN
ID RFA4_HUMAN Reviewed; 261 AA.
AC Q13156; Q3SY03;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Replication protein A 30 kDa subunit;
DE Short=RP-A p30;
DE AltName: Full=Replication factor A protein 4;
DE Short=RF-A protein 4;
GN Name=RPA4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND INTERACTION WITH RPA1 AND RPA3.
RX PubMed=7760808; DOI=10.1128/mcb.15.6.3119;
RA Keshav K.F., Chen C., Dutta A.;
RT "Rpa4, a homolog of the 34-kilodalton subunit of the replication protein A
RT complex.";
RL Mol. Cell. Biol. 15:3119-3128(1995).
RN [2]
RP SEQUENCE REVISION TO 10.
RA Keshav K.F.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-33.
RG NIEHS SNPs program;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION IN THE ARPA COMPLEX, AND FUNCTION OF THE ARPA COMPLEX.
RX PubMed=19116208; DOI=10.1074/jbc.m808963200;
RA Mason A.C., Haring S.J., Pryor J.M., Staloch C.A., Gan T.F., Wold M.S.;
RT "An alternative form of replication protein a prevents viral replication in
RT vitro.";
RL J. Biol. Chem. 284:5324-5331(2009).
RN [7]
RP FUNCTION OF THE ARPA COMPLEX.
RX PubMed=20545304; DOI=10.1021/bi100380n;
RA Mason A.C., Roy R., Simmons D.T., Wold M.S.;
RT "Functions of alternative replication protein A in initiation and
RT elongation.";
RL Biochemistry 49:5919-5928(2010).
RN [8]
RP FUNCTION OF THE ARPA COMPLEX, AND TISSUE SPECIFICITY.
RX PubMed=19996105; DOI=10.1074/jbc.m109.079418;
RA Kemp M.G., Mason A.C., Carreira A., Reardon J.T., Haring S.J.,
RA Borgstahl G.E., Kowalczykowski S.C., Sancar A., Wold M.S.;
RT "An alternative form of replication protein a expressed in normal human
RT tissues supports DNA repair.";
RL J. Biol. Chem. 285:4788-4797(2010).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19942684; DOI=10.1093/nar/gkp1062;
RA Haring S.J., Humphreys T.D., Wold M.S.;
RT "A naturally occurring human RPA subunit homolog does not support DNA
RT replication or cell-cycle progression.";
RL Nucleic Acids Res. 38:846-858(2010).
CC -!- FUNCTION: As part of the alternative replication protein A complex,
CC aRPA, binds single-stranded DNA and probably plays a role in DNA
CC repair. Compared to the RPA2-containing, canonical RPA complex, may not
CC support chromosomal DNA replication and cell cycle progression through
CC S-phase. The aRPA may not promote efficient priming by DNA polymerase
CC alpha but could support DNA polymerase delta synthesis in the presence
CC of PCNA and replication factor C (RFC), the dual incision/excision
CC reaction of nucleotide excision repair and RAD51-dependent strand
CC exchange. {ECO:0000269|PubMed:19116208, ECO:0000269|PubMed:19942684,
CC ECO:0000269|PubMed:19996105, ECO:0000269|PubMed:20545304}.
CC -!- SUBUNIT: Component of the aRPA, the alternative replication protein A
CC complex, a trimeric complex similar to the replication protein A
CC complex/RPA but where RPA1 and RPA3 are associated with RPA4 instead of
CC RPA2. Interacts with RPA1 and RPA3. {ECO:0000269|PubMed:19116208,
CC ECO:0000269|PubMed:7760808}.
CC -!- INTERACTION:
CC Q13156; Q6GMV3: PTRHD1; NbExp=3; IntAct=EBI-2856301, EBI-12807218;
CC Q13156; P27694: RPA1; NbExp=6; IntAct=EBI-2856301, EBI-621389;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19942684}.
CC Note=Localizes to DNA repair foci after DNA damage.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in placental and colon
CC mucosa. Widely expressed at intermediate or lower levels.
CC {ECO:0000269|PubMed:19996105}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 2 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/hsu24186/";
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DR EMBL; U24186; AAB08488.2; -; mRNA.
DR EMBL; AF494047; AAM09569.1; -; Genomic_DNA.
DR EMBL; Z86061; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069791; AAH69791.1; -; mRNA.
DR EMBL; BC069808; AAH69808.1; -; mRNA.
DR EMBL; BC069824; AAH69824.1; -; mRNA.
DR EMBL; BC104013; AAI04014.1; -; mRNA.
DR EMBL; BC104014; AAI04015.1; -; mRNA.
DR CCDS; CCDS35345.1; -.
DR RefSeq; NP_037479.1; NM_013347.4.
DR AlphaFoldDB; Q13156; -.
DR SMR; Q13156; -.
DR BioGRID; 118975; 18.
DR ComplexPortal; CPX-1879; Replication protein A complex, RPA4 variant.
DR DIP; DIP-24241N; -.
DR IntAct; Q13156; 9.
DR STRING; 9606.ENSP00000362131; -.
DR BioMuta; RPA4; -.
DR DMDM; 14917036; -.
DR MassIVE; Q13156; -.
DR PaxDb; Q13156; -.
DR PeptideAtlas; Q13156; -.
DR PRIDE; Q13156; -.
DR ProteomicsDB; 59196; -.
DR Antibodypedia; 28489; 190 antibodies from 23 providers.
DR DNASU; 29935; -.
DR Ensembl; ENST00000373040.4; ENSP00000362131.3; ENSG00000204086.4.
DR GeneID; 29935; -.
DR KEGG; hsa:29935; -.
DR MANE-Select; ENST00000373040.4; ENSP00000362131.3; NM_013347.4; NP_037479.1.
DR UCSC; uc004efv.5; human.
DR CTD; 29935; -.
DR GeneCards; RPA4; -.
DR HGNC; HGNC:30305; RPA4.
DR HPA; ENSG00000204086; Tissue enhanced (choroid plexus, testis).
DR MIM; 300767; gene.
DR neXtProt; NX_Q13156; -.
DR OpenTargets; ENSG00000204086; -.
DR PharmGKB; PA134988548; -.
DR VEuPathDB; HostDB:ENSG00000204086; -.
DR eggNOG; KOG3108; Eukaryota.
DR GeneTree; ENSGT00940000166006; -.
DR HOGENOM; CLU_051033_1_0_1; -.
DR InParanoid; Q13156; -.
DR OMA; DEHHFKA; -.
DR OrthoDB; 924826at2759; -.
DR PhylomeDB; Q13156; -.
DR TreeFam; TF105242; -.
DR PathwayCommons; Q13156; -.
DR Reactome; R-HSA-68962; Activation of the pre-replicative complex.
DR SignaLink; Q13156; -.
DR BioGRID-ORCS; 29935; 12 hits in 700 CRISPR screens.
DR GeneWiki; RPA4; -.
DR GenomeRNAi; 29935; -.
DR Pharos; Q13156; Tbio.
DR PRO; PR:Q13156; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q13156; protein.
DR Bgee; ENSG00000204086; Expressed in secondary oocyte and 80 other tissues.
DR Genevisible; Q13156; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; IBA:GO_Central.
DR GO; GO:0005662; C:DNA replication factor A complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IDA:ComplexPortal.
DR GO; GO:0006260; P:DNA replication; IBA:GO_Central.
DR GO; GO:0006270; P:DNA replication initiation; TAS:ProtInc.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IDA: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 repair; DNA-binding; Nucleus; Reference proteome.
FT CHAIN 1..261
FT /note="Replication protein A 30 kDa subunit"
FT /id="PRO_0000097280"
FT DNA_BIND 74..148
FT /note="OB"
FT REGION 175..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 33
FT /note="A -> T (in dbSNP:rs2642219)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_019170"
SQ SEQUENCE 261 AA; 28868 MW; 6A925FAEDBE21718 CRC64;
MSKSGFGSYG SISAADGASG GSDQLCERDA TPAIKTQRPK VRIQDVVPCN VNQLLSSTVF
DPVFKVRGII VSQVSIVGVI RGAEKASNHI CYKIDDMTAK PIEARQWFGR EKVKQVTPLS
VGVYVKVFGI LKCPTGTKSL EVLKIHVLED MNEFTVHILE TVNAHMMLDK ARRDTTVESV
PVSPSEVNDA GDNDESHRNF IQDEVLRLIH ECPHQEGKSI HELRAQLCDL SVKAIKEAID
YLTVEGHIYP TVDREHFKSA D
