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   25-JAN-2012, entry version 109.
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 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.,
RA   Wold M.S.;
RT   "An alternative form of replication protein a prevents viral
RT   replication in vitro.";
RL   J. Biol. Chem. 284:5324-5331(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND THR-52, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [9]
RP   FUNCTION OF THE ARPA COMPLEX.
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
RT   human tissues supports DNA repair.";
RL   J. Biol. Chem. 285:4788-4797(2010).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [11]
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   -!- FUNCTION: Functions as component of the alternative replication
CC       protein A complex (aRPA). aRPA binds single-stranded DNA and
CC       probably plays a role in DNA repair; it does not support
CC       chromosomal DNA replication and cell cycle progression through S-
CC       phase. In vitro, aRPA cannot promote efficient priming by DNA
CC       polymerase alpha but supports DNA polymerase delta synthesis in
CC       the presence of PCNA and replication factor C (RFC), the dual
CC       incision/excision reaction of nucleotide excision repair and
CC       RAD51-dependent strand exchange.
CC   -!- SUBUNIT: Heterotrimer of 70, 32 and 14 kDa chains (canonical
CC       replication protein A complex). Component of the alternative
CC       replication protein A complex (aRPA) composed of RPA1, RPA3 and
CC       RPA4. The DNA-binding activity may reside exclusively on the 70
CC       kDa subunit. Interacts with RPA4.
CC   -!- INTERACTION:
CC       P43351:RAD52; NbExp=2; IntAct=EBI-621428, EBI-706448;
CC       P27694:RPA1; NbExp=4; IntAct=EBI-621428, EBI-621389;
CC       P15927:RPA2; NbExp=3; IntAct=EBI-621428, EBI-621404;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/rpa3/";
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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; NM_002947.3.
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   PDB; 3KDF; X-ray; 1.98 A; A/C=2-121.
DR   PDBsum; 1L1O; -.
DR   PDBsum; 1QUQ; -.
DR   PDBsum; 2PI2; -.
DR   PDBsum; 2PQA; -.
DR   PDBsum; 2Z6K; -.
DR   PDBsum; 3KDF; -.
DR   ProteinModelPortal; P35244; -.
DR   SMR; P35244; 2-118.
DR   DIP; DIP-24190N; -.
DR   IntAct; P35244; 9.
DR   STRING; P35244; -.
DR   PhosphoSite; P35244; -.
DR   DMDM; 464608; -.
DR   PeptideAtlas; P35244; -.
DR   PRIDE; P35244; -.
DR   Ensembl; ENST00000223129; ENSP00000223129; ENSG00000106399.
DR   Ensembl; ENST00000396682; ENSP00000379914; ENSG00000106399.
DR   Ensembl; ENST00000402771; ENSP00000384246; ENSG00000106399.
DR   GeneID; 6119; -.
DR   KEGG; hsa:6119; -.
DR   UCSC; uc003sri.1; human.
DR   CTD; 6119; -.
DR   GeneCards; GC07M007643; -.
DR   H-InvDB; HIX0017394; -.
DR   HGNC; HGNC:10291; RPA3.
DR   HPA; HPA005708; -.
DR   MIM; 179837; gene.
DR   neXtProt; NX_P35244; -.
DR   GeneTree; ENSGT00390000008029; -.
DR   HOGENOM; HBG716382; -.
DR   HOVERGEN; HBG003004; -.
DR   InParanoid; P35244; -.
DR   OMA; TIMCASY; -.
DR   OrthoDB; EOG4NVZMT; -.
DR   PhylomeDB; P35244; -.
DR   Reactome; REACT_111183; Meiosis.
DR   Reactome; REACT_152; Cell Cycle, Mitotic.
DR   Reactome; REACT_1538; Cell Cycle Checkpoints.
DR   Reactome; REACT_216; DNA Repair.
DR   Reactome; REACT_22172; Chromosome Maintenance.
DR   Reactome; REACT_383; DNA Replication.
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; TAS:Reactome.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003697; F:single-stranded DNA binding; TAS:ProtInc.
DR   GO; GO:0000075; P:cell cycle checkpoint; TAS:Reactome.
DR   GO; GO:0000730; P:DNA recombinase assembly; TAS:Reactome.
DR   GO; GO:0006271; P:DNA strand elongation involved in DNA replication; TAS:Reactome.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0000216; P:M/G1 transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0000718; P:nucleotide-excision repair, DNA damage removal; TAS:Reactome.
DR   GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; TAS:Reactome.
DR   GO; GO:0000084; P:S phase of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0000722; P:telomere maintenance via recombination; TAS:Reactome.
DR   GO; GO:0032201; P:telomere maintenance via semi-conservative replication; TAS:Reactome.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR016027; NA-bd_OB-fold-like.
DR   InterPro; IPR013970; Rep_factor-A_3.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   KO; K10740; -.
DR   Pfam; PF08661; Rep_fac-A_3; 1.
DR   SUPFAM; SSF50249; Nucleic_acid_OB; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; DNA damage; DNA recombination;
KW   DNA repair; DNA replication; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN         1    121       Replication protein A 14 kDa subunit.
FT                                /FTId=PRO_0000097276.
FT   MOD_RES      44     44       Phosphoserine.
FT   MOD_RES      52     52       Phosphothreonine.
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
//