RFA2_TETTS
ID RFA2_TETTS Reviewed; 269 AA.
AC A0A0U8TRG9; W7XFB2;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 1.
DT 25-MAY-2022, entry version 16.
DE RecName: Full=Replication protein A 32 kDa subunit {ECO:0000305};
DE Short=RP-A p32 {ECO:0000305};
DE AltName: Full=Replication factor A protein 2 {ECO:0000305};
DE Short=RF-A protein 2 {ECO:0000305};
DE AltName: Full=Telomeric repeat-binding subunit 2 {ECO:0000303|PubMed:27895115};
GN Name=RPA2; Synonyms=TEB2 {ECO:0000303|PubMed:27895115};
GN ORFNames=TTHERM_001113129 {ECO:0000312|EMBL:EWS71464.1};
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 RPA complex, binds and stabilizes
CC single-stranded DNA (ssDNA) 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, RPA2/TEB2 does not contribute to ssDNA affinity, while it
CC contributes to ssDNA affinity in the RPA complex (PubMed:27895115).
CC {ECO:0000250|UniProtKB:P15927, 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:P15927}.
CC Chromosome, telomere {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 2 family.
CC {ECO:0000305}.
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DR EMBL; GG662333; EWS71464.1; -; Genomic_DNA.
DR EMBL; BK009378; DAA64973.1; -; mRNA.
DR RefSeq; XP_012656004.1; XM_012800550.1.
DR PDB; 6D6V; EM; 4.80 A; E=1-269.
DR PDB; 7LMA; EM; 3.30 A; E=1-269.
DR PDB; 7LMB; EM; 3.80 A; E=1-269.
DR PDBsum; 6D6V; -.
DR PDBsum; 7LMA; -.
DR PDBsum; 7LMB; -.
DR AlphaFoldDB; A0A0U8TRG9; -.
DR SMR; A0A0U8TRG9; -.
DR DIP; DIP-61870N; -.
DR IntAct; A0A0U8TRG9; 2.
DR GeneID; 24441731; -.
DR KEGG; tet:TTHERM_001113129; -.
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:UniProtKB-KW.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; DNA-binding; Nucleus; Reference proteome;
KW Telomere.
FT CHAIN 1..269
FT /note="Replication protein A 32 kDa subunit"
FT /id="PRO_0000449914"
FT DNA_BIND 69..149
FT /note="OB"
FT /evidence="ECO:0000250|UniProtKB:P15927"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 154..174
FT /evidence="ECO:0007829|PDB:7LMA"
SQ SEQUENCE 269 AA; 30955 MW; 457EFB4E824B0052 CRC64;
MSNRVQGGFD NNSGNNQSAQ KQQAEKIPQI TVPLNCFMIN QIVKAAKENP QAHSGNHYEW
YGAFENAIIT AKFEFLQSIN DSPKIMGKLS DSTGCIEVVI QKSKMSDELP EFVQAYEIEL
QNNGNRHKYV RAMLKMRKNA QIQLLYFSIV NDANEISRHG LDLCLRYLQR KHGIEDFMHM
TNDKAHNNHN ASAQKVHYQI DRNQQPKEQV LELMRQILKH NPNDQIPKSK IIEFFQSQLN
QVQINQILQQ LVSANEIFSV GSDNYLLNV
