RFA3_TETTS
ID RFA3_TETTS Reviewed; 121 AA.
AC A0A0U8UFF4; I7MK73;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 1.
DT 25-MAY-2022, entry version 19.
DE RecName: Full=Replication protein A 14 kDa subunit {ECO:0000305};
DE Short=RP-A p14 {ECO:0000305};
DE AltName: Full=Replication factor A protein 3 {ECO:0000305};
DE Short=RF-A protein 3 {ECO:0000305};
DE AltName: Full=Telomeric repeat-binding subunit 3 {ECO:0000303|PubMed:27895115};
GN Name=RPA2; Synonyms=TEB3 {ECO:0000303|PubMed:27895115};
GN ORFNames=TTHERM_00439320 {ECO:0000312|EMBL:EAR97584.3};
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210;
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
RN [2]
RP IDENTIFICATION, FUNCTION, AND STRUCTURE BY ELECTRON MICROSCOPY OF THE
RP TELOMERASE HOLOENZYME.
RX PubMed=26472759; DOI=10.1126/science.aab4070;
RA Jiang J., Chan H., Cash D.D., Miracco E.J., Ogorzalek Loo R.R., Upton H.E.,
RA Cascio D., O'Brien Johnson R., Collins K., Loo J.A., Zhou Z.H., Feigon J.;
RT "Structure of Tetrahymena telomerase reveals previously unknown subunits,
RT functions, and interactions.";
RL Science 350:AAB4070-AAB4070(2015).
RN [3]
RP FUNCTION, IDENTIFICATION IN THE RPA COMPLEX, AND IDENTIFICATION IN THE
RP TELOMERASE HOLOENZYME COMPLEX.
RX PubMed=27895115; DOI=10.1074/jbc.m116.763664;
RA Upton H.E., Chan H., Feigon J., Collins K.;
RT "Shared subunits of Tetrahymena telomerase holoenzyme and replication
RT protein A have different functions in different cellular complexes.";
RL J. Biol. Chem. 292:217-228(2017).
RN [4] {ECO:0007744|PDB:6D6V}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.80 ANGSTROMS) OF THE TELOMERASE
RP HOLOENZYME IN COMPLEX WITH TELOMERIC DNA AND TER RNA.
RX PubMed=29775593; DOI=10.1016/j.cell.2018.04.038;
RA Jiang J., Wang Y., Susac L., Chan H., Basu R., Zhou Z.H., Feigon J.;
RT "Structure of telomerase with telomeric DNA.";
RL Cell 173:1179-1190(2018).
CC -!- FUNCTION: Component of the heterotrimeric replication protein A (RPA)
CC and holoenzyme telomerase ribonucleoprotein complexes (PubMed:26472759,
CC PubMed:27895115). As part of the heterotrimeric RPA complex, binds and
CC stabilizes single-stranded DNA intermediates that form during DNA
CC replication or upon DNA stress (By similarity). It prevents their
CC reannealing and in parallel, recruits and activates different proteins
CC and complexes involved in DNA metabolism (By similarity). Thereby, it
CC plays an essential role both in DNA replication and the cellular
CC response to DNA damage (By similarity). In the cellular response to DNA
CC damage, the RPA complex controls DNA repair and DNA damage checkpoint
CC activation (By similarity). Also part of a subcomplex of the holoenzyme
CC telomerase ribonucleoprotein complex: this subcomplex that contains
CC TEB1, RPA2/TEB2, RPA3/TEB3, but not RPA1, mediates the recruitment of
CC telomerase to telomeric DNA via specific interaction between TEB1 and
CC telomeric ssDNA (PubMed:27895115). In the holoenzyme telomerase
CC ribonucleoprotein complex, RPA2/TEB2 and RPA3/TEB3 act as assembly
CC factors for TEB1 incorporation into telomerase holoenzyme
CC (PubMed:27895115). In the holoenzyme telomerase ribonucleoprotein
CC complex, RPA3/TEB3 does not contribute to ssDNA affinity, while it
CC contributes to ssDNA affinity in the RPA complex (PubMed:27895115).
CC {ECO:0000250|UniProtKB:P35244, ECO:0000269|PubMed:26472759,
CC ECO:0000269|PubMed:27895115}.
CC -!- SUBUNIT: Component of the replication protein A complex (RPA), a
CC heterotrimeric complex composed of RPA1, RPA2/TEB2 and RPA3/TEB3
CC (PubMed:27895115). Component of the telomerase holoenzyme complex,
CC composed of the catalytic core (the catalytic subunit TERT, the
CC telomerase RNA template component TER and TAP65/p65), which is
CC associated with two heterotrimeric subcomplexes: (i) the replication
CC protein A (RPA)-related subcomplex, composed of TEB1, RPA2/TEB2 and
CC RPA3/TEB3 and (ii) the CST-like subcomplex, composed of TAP75/p75,
CC TAP45/p45 and TAP19/p19 (PubMed:26472759, PubMed:29775593). TEB1 and
CC the CST-like subcomplex are tethered to the catalytic core by TAP50/p50
CC (PubMed:26472759, PubMed:29775593). {ECO:0000269|PubMed:26472759,
CC ECO:0000269|PubMed:27895115, ECO:0000269|PubMed:29775593}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P35244}.
CC Chromosome, telomere {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 3 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAR97584.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; GG662663; EAR97584.3; ALT_SEQ; Genomic_DNA.
DR EMBL; BK009379; DAA64974.1; -; mRNA.
DR RefSeq; XP_001017829.3; XM_001017829.3.
DR PDB; 6D6V; EM; 4.80 A; F=1-121.
DR PDB; 7LMA; EM; 3.30 A; F=1-121.
DR PDB; 7LMB; EM; 3.80 A; F=1-121.
DR PDBsum; 6D6V; -.
DR PDBsum; 7LMA; -.
DR PDBsum; 7LMB; -.
DR AlphaFoldDB; A0A0U8UFF4; -.
DR SMR; A0A0U8UFF4; -.
DR DIP; DIP-61871N; -.
DR IntAct; A0A0U8UFF4; 2.
DR STRING; 5911.EAR97584; -.
DR GeneID; 7828936; -.
DR KEGG; tet:TTHERM_00439320; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005662; C:DNA replication factor A complex; IDA:UniProtKB.
DR GO; GO:0005697; C:telomerase holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR013970; Rfa2.
DR Pfam; PF08661; Rep_fac-A_3; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Nucleus; Reference proteome; Telomere.
FT CHAIN 1..121
FT /note="Replication protein A 14 kDa subunit"
FT /id="PRO_0000449915"
FT HELIX 16..21
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:7LMA"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 79..91
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:7LMA"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:7LMA"
SQ SEQUENCE 121 AA; 13995 MW; C7D3E6BB5EE626FA CRC64;
MDAEQEQVMY PRILFEQMAQ FRGKKVTVVG NVCNEDQNDS LVIEFGPTGL NQHVVIDNYR
RVDLNNTTKF VEIRGVVLNQ NIVSCEELTE FEQKDPFDFD TYSKLIHLSQ SDKLSSLFTD
Q
