ID RFA3_HUMAN Reviewed; 121 AA. AC P35244; Q549U6; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 03-NOV-2009, entry version 87. DE RecName: Full=Replication protein A 14 kDa subunit; DE Short=RP-A p14; DE AltName: Full=Replication factor A protein 3; DE Short=RF-A protein 3; GN Name=RPA3; Synonyms=REPA3, RPA14; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=93203195; PubMed=8454588; RA Umbricht C.B., Kelly T.J.; RT "Cloning, overexpression, and genomic mapping of the 14-kDa subunit of RT human replication protein A."; RL J. Biol. Chem. 268:6131-6138(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22737999; PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney, and Lung; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP INTERACTION WITH RPA4. RX MEDLINE=95280910; PubMed=7760808; RA Keshav K.F., Chen C., Dutta A.; RT "Rpa4, a homolog of the 34-kilodalton subunit of the replication RT protein A complex."; RL Mol. Cell. Biol. 15:3119-3128(1995). RN [7] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [8] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH RPA1 AND RPA2. RX PubMed=11927569; DOI=10.1093/emboj/21.7.1855; RA Bochkareva E., Korolev S., Lees-Miller S.P., Bochkarev A.; RT "Structure of the RPA trimerization core and its role in the multistep RT DNA-binding mechanism of RPA."; RL EMBO J. 21:1855-1863(2002). CC -!- FUNCTION: Required for DNA recombination, repair and replication. CC The activity of RP-A is mediated by single-stranded DNA binding CC and protein interactions. CC -!- SUBUNIT: Heterotrimer of 70, 32 and 14 kDa chains. The DNA-binding CC activity may reside exclusively on the 70 kDa subunit. Interacts CC with RPA4. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/rpa3/"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L07493; AAA58350.1; -; mRNA. DR EMBL; BT007320; AAP35984.1; -; mRNA. DR EMBL; DQ003136; AAX84517.1; -; Genomic_DNA. DR EMBL; AC004948; AAQ96878.1; -; Genomic_DNA. DR EMBL; BC005264; AAH05264.1; -; mRNA. DR EMBL; BC009868; AAH09868.1; -; mRNA. DR IPI; IPI00017373; -. DR PIR; A46008; A46008. DR RefSeq; NP_002938.1; -. DR UniGene; Hs.487540; -. DR PDB; 1L1O; X-ray; 2.80 A; A/D=1-121. DR PDB; 1QUQ; X-ray; 2.50 A; B/D=1-121. DR PDB; 2PI2; X-ray; 2.00 A; E/F/G/H=1-121. DR PDB; 2PQA; X-ray; 2.50 A; B/D=1-121. DR PDB; 2Z6K; X-ray; 3.00 A; C/D=1-121. DR PDBsum; 1L1O; -. DR PDBsum; 1QUQ; -. DR PDBsum; 2PI2; -. DR PDBsum; 2PQA; -. DR PDBsum; 2Z6K; -. DR DIP; DIP:24190N; -. DR IntAct; P35244; 3. DR STRING; P35244; -. DR PeptideAtlas; P35244; -. DR PRIDE; P35244; -. DR Ensembl; ENST00000223129; ENSP00000223129; ENSG00000106399; Homo sapiens. DR Ensembl; ENST00000396682; ENSP00000379914; ENSG00000106399; Homo sapiens. DR Ensembl; ENST00000401447; ENSP00000385383; ENSG00000106399; Homo sapiens. DR Ensembl; ENST00000402771; ENSP00000384246; ENSG00000106399; Homo sapiens. DR Ensembl; ENST00000406109; ENSP00000384652; ENSG00000106399; Homo sapiens. DR GeneID; 6119; -. DR KEGG; hsa:6119; -. DR UCSC; uc003sri.1; human. DR CTD; 6119; -. DR GeneCards; GC07M007643; -. DR H-InvDB; HIX0017394; -. DR H-InvDB; HIX0057108; -. DR HGNC; HGNC:10291; RPA3. DR HPA; HPA005708; -. DR MIM; 179837; gene. DR PharmGKB; PA29357; -. DR HOGENOM; P35244; -. DR HOVERGEN; P35244; -. DR OMA; TIMCASY; -. DR Reactome; REACT_152; Cell Cycle, Mitotic. DR Reactome; REACT_1538; Cell Cycle Checkpoints. DR Reactome; REACT_216; DNA Repair. DR Reactome; REACT_383; DNA Replication. DR Reactome; REACT_7970; Telomere Maintenance. DR NextBio; 23763; -. DR ArrayExpress; P35244; -. DR Bgee; P35244; -. DR CleanEx; HS_RPA3; -. DR Genevestigator; P35244; -. DR GermOnline; ENSG00000106399; Homo sapiens. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0005662; C:DNA replication factor A complex; TAS:ProtInc. DR GO; GO:0005654; C:nucleoplasm; EXP:Reactome. DR GO; GO:0003697; F:single-stranded DNA binding; TAS:ProtInc. DR GO; GO:0006260; P:DNA replication; EXP:Reactome. DR GO; GO:0000718; P:nucleotide-excision repair, DNA damage removal; EXP:Reactome. DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; EXP:Reactome. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR013970; Rep_factor-A_3. DR Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1. DR Pfam; PF08661; Rep_fac-A_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA replication; Nucleus. FT CHAIN 1 121 Replication protein A 14 kDa subunit. FT /FTId=PRO_0000097276. FT HELIX 4 6 FT STRAND 10 12 FT HELIX 14 19 FT STRAND 24 34 FT STRAND 38 44 FT STRAND 50 54 FT STRAND 65 73 FT STRAND 79 86 FT STRAND 90 92 FT HELIX 96 108 FT HELIX 110 112 SQ SEQUENCE 121 AA; 13569 MW; 3FD99851959FB498 CRC64; MVDMMDLPRS RINAGMLAQF IDKPVCFVGR LEKIHPTGKM FILSDGEGKN GTIELMEPLD EEISGIVEVV GRVTAKATIL CTSYVQFKED SHPFDLGLYN EAVKIIHDFP QFYPLGIVQH D //