TEB1_TETTS
ID TEB1_TETTS Reviewed; 701 AA.
AC D2CVN6; I7LVX8;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Telomeric repeat-binding subunit 1 {ECO:0000303|PubMed:20363756};
DE AltName: Full=Telomerase-associated protein of 82 kDa {ECO:0000303|PubMed:19941821};
DE Short=p82 {ECO:0000303|PubMed:19941821};
GN Name=TEB1 {ECO:0000303|PubMed:20363756};
GN Synonyms=TAP82 {ECO:0000303|PubMed:19941821};
GN ORFNames=TTHERM_00218760 {ECO:0000312|EMBL:EAS00303.2};
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 [MRNA], IDENTIFICATION IN THE TELOMERASE HOLOENZYME,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=SB210;
RX PubMed=19941821; DOI=10.1016/j.molcel.2009.09.041;
RA Min B., Collins K.;
RT "An RPA-related sequence-specific DNA-binding subunit of telomerase
RT holoenzyme is required for elongation processivity and telomere
RT maintenance.";
RL Mol. Cell 36:609-619(2009).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=20363756; DOI=10.1074/jbc.m110.119172;
RA Min B., Collins K.;
RT "Multiple mechanisms for elongation processivity within the reconstituted
RT tetrahymena telomerase holoenzyme.";
RL J. Biol. Chem. 285:16434-16443(2010).
RN [4]
RP FUNCTION, DNA-BINDING, AND MUTAGENESIS OF PHE-293; LYS-300; PHE-423;
RP TYR-450; PHE-590; PHE-603; PHE-648 AND LYS-660.
RX PubMed=25225329; DOI=10.1128/mcb.01030-14;
RA Upton H.E., Hong K., Collins K.;
RT "Direct single-stranded DNA binding by Teb1 mediates the recruitment of
RT Tetrahymena thermophila telomerase to telomeres.";
RL Mol. Cell. Biol. 34:4200-4212(2014).
RN [5]
RP FUNCTION.
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 [6] {ECO:0007744|PDB:3U4V, ECO:0007744|PDB:3U4Z, ECO:0007744|PDB:3U50}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 199-315 IN COMPLEX WITH ZINC,
RP FUNCTION, DNA-BINDING, AND MUTAGENESIS OF PHE-241; TYR-249; PHE-293;
RP TYR-388; LYS-403; ARG-406; LYS-408; LYS-419; PHE-423; TYR-450; LYS-457;
RP HIS-461; LYS-532; ARG-554; LYS-560; ARG-588; MET-601; PHE-603 AND LYS-660.
RX PubMed=22143754; DOI=10.1073/pnas.1113624108;
RA Zeng Z., Min B., Huang J., Hong K., Yang Y., Collins K., Lei M.;
RT "Structural basis for Tetrahymena telomerase processivity factor Teb1
RT binding to single-stranded telomeric-repeat DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20357-20361(2011).
RN [7]
RP STRUCTURE BY ELECTRON MICROSCOPY OF THE TELOMERASE HOLOENZYME.
RX PubMed=23552895; DOI=10.1038/nature12062;
RA Jiang J., Miracco E.J., Hong K., Eckert B., Chan H., Cash D.D., Min B.,
RA Zhou Z.H., Collins K., Feigon J.;
RT "The architecture of Tetrahymena telomerase holoenzyme.";
RL Nature 496:187-192(2013).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY OF THE 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 [9] {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: Single-stranded DNA (ssDNA)-binding protein that mediates the
CC recruitment of telomerase to telomeric DNA (PubMed:19941821,
CC PubMed:20363756, PubMed:25225329, PubMed:22143754). Telomerase is an
CC essential ribonucleoprotein (RNP) enzyme that copies new telomeric
CC repeats onto chromosome ends by repetitively synthesizing the short
CC telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component
CC TER (PubMed:19941821). Acts as part of a replication protein A (RPA)-
CC related subcomplex of the holoenzyme telomerase ribonucleoprotein
CC complex: TEB1 specifically recognizes and binds telomeric ssDNA,
CC thereby mediating the recruitment of the holoenzyme telomerase RNP
CC complex to telomeres (PubMed:19941821, PubMed:25225329,
CC PubMed:27895115). TEB1 is related to RPA1 subunit of the RPA complex
CC but is specific to telomeric DNA, which is not the case of RPA1
CC (PubMed:25225329). {ECO:0000269|PubMed:19941821,
CC ECO:0000269|PubMed:20363756, ECO:0000269|PubMed:22143754,
CC ECO:0000269|PubMed:25225329, ECO:0000269|PubMed:27895115}.
CC -!- SUBUNIT: Component of the telomerase holoenzyme complex, composed of
CC the catalytic core (the catalytic subunit TERT, the telomerase RNA
CC template component TER and TAP65/p65), which is associated with two
CC heterotrimeric subcomplexes: (i) the replication protein A (RPA)-
CC related subcomplex, composed of TEB1, RPA2/TEB2 and RPA3/TEB3 and (ii)
CC the CST-like subcomplex, composed of TAP75/p75, TAP45/p45 and TAP19/p19
CC (PubMed:19941821, PubMed:27895115, PubMed:23552895, PubMed:26472759,
CC PubMed:29775593). TEB1 and the CST-like subcomplex are tethered to the
CC catalytic core by TAP50/p50 (PubMed:19941821, PubMed:23552895,
CC PubMed:26472759, PubMed:29775593). {ECO:0000269|PubMed:19941821,
CC ECO:0000269|PubMed:23552895, ECO:0000269|PubMed:26472759,
CC ECO:0000269|PubMed:27895115, ECO:0000269|PubMed:29775593}.
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Critically short telomeres.
CC {ECO:0000269|PubMed:19941821}.
CC -!- SIMILARITY: Belongs to the replication factor A protein 1 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU873081; ACJ61511.1; -; mRNA.
DR EMBL; GG662621; EAS00303.2; -; Genomic_DNA.
DR RefSeq; XP_001020548.2; XM_001020548.2.
DR PDB; 3U4V; X-ray; 1.80 A; A/B=199-315.
DR PDB; 3U4Z; X-ray; 2.30 A; A/B=375-483.
DR PDB; 3U50; X-ray; 2.50 A; C=511-682.
DR PDB; 6D6V; EM; 4.80 A; D=1-701.
DR PDB; 7LMA; EM; 3.30 A; D=1-701.
DR PDB; 7LMB; EM; 3.80 A; D=1-701.
DR PDBsum; 3U4V; -.
DR PDBsum; 3U4Z; -.
DR PDBsum; 3U50; -.
DR PDBsum; 6D6V; -.
DR PDBsum; 7LMA; -.
DR PDBsum; 7LMB; -.
DR AlphaFoldDB; D2CVN6; -.
DR SMR; D2CVN6; -.
DR DIP; DIP-60201N; -.
DR DIP; DIP-61869N; -.
DR IntAct; D2CVN6; 2.
DR STRING; 5911.EAS00303; -.
DR GeneID; 7838227; -.
DR KEGG; tet:TTHERM_00218760; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005697; C:telomerase holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0007004; P:telomere maintenance via telomerase; IMP:UniProtKB.
DR CDD; cd04476; RPA1_DBD_C; 1.
DR Gene3D; 2.40.50.140; -; 3.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR InterPro; IPR013955; Rep_factor-A_C.
DR Pfam; PF08646; Rep_fac-A_C; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SUPFAM; SSF50249; SSF50249; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; DNA-binding; Metal-binding; Reference proteome;
KW Telomere; Zinc; Zinc-finger.
FT CHAIN 1..701
FT /note="Telomeric repeat-binding subunit 1"
FT /id="PRO_0000449913"
FT DNA_BIND 229..301
FT /note="OB"
FT /evidence="ECO:0000255"
FT ZN_FING 555..575
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT BINDING 555
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:22143754,
FT ECO:0007744|PDB:3U50"
FT BINDING 572
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:22143754,
FT ECO:0007744|PDB:3U50"
FT BINDING 575
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:22143754,
FT ECO:0007744|PDB:3U50"
FT MUTAGEN 241
FT /note="F->A: Reduced single-stranded telomeric DNA
FT binding."
FT /evidence="ECO:0000269|PubMed:22143754"
FT MUTAGEN 249
FT /note="Y->A: Reduced single-stranded telomeric DNA
FT binding."
FT /evidence="ECO:0000269|PubMed:22143754"
FT MUTAGEN 293
FT /note="F->A: Abolished single-stranded telomeric DNA
FT binding; does not affect telomerase activity of the
FT holoenzyme telomerase ribonucleoprotein complex."
FT /evidence="ECO:0000269|PubMed:22143754,
FT ECO:0000269|PubMed:25225329"
FT MUTAGEN 300
FT /note="K->A: Reduced single-stranded telomeric DNA binding;
FT does not affect telomerase activity of the holoenzyme
FT telomerase ribonucleoprotein complex."
FT /evidence="ECO:0000269|PubMed:25225329"
FT MUTAGEN 388
FT /note="Y->A: Reduced single-stranded telomeric DNA
FT binding."
FT /evidence="ECO:0000269|PubMed:22143754"
FT MUTAGEN 403
FT /note="K->A: Reduced single-stranded telomeric DNA
FT binding."
FT /evidence="ECO:0000269|PubMed:22143754"
FT MUTAGEN 406
FT /note="R->A: Reduced single-stranded telomeric DNA
FT binding."
FT /evidence="ECO:0000269|PubMed:22143754"
FT MUTAGEN 408
FT /note="K->A: Does not affect single-stranded telomeric DNA
FT binding."
FT /evidence="ECO:0000269|PubMed:22143754"
FT MUTAGEN 419
FT /note="K->A: Reduced single-stranded telomeric DNA
FT binding."
FT /evidence="ECO:0000269|PubMed:22143754"
FT MUTAGEN 423
FT /note="F->A: Reduced single-stranded telomeric DNA binding;
FT does not affect telomerase activity of the holoenzyme
FT telomerase ribonucleoprotein complex."
FT /evidence="ECO:0000269|PubMed:22143754,
FT ECO:0000269|PubMed:25225329"
FT MUTAGEN 450
FT /note="Y->A: Reduced single-stranded telomeric DNA binding;
FT does not affect telomerase activity of the holoenzyme
FT telomerase ribonucleoprotein complex."
FT /evidence="ECO:0000269|PubMed:22143754,
FT ECO:0000269|PubMed:25225329"
FT MUTAGEN 457
FT /note="K->A: Reduced single-stranded telomeric DNA
FT binding."
FT /evidence="ECO:0000269|PubMed:22143754"
FT MUTAGEN 461
FT /note="H->A: Reduced single-stranded telomeric DNA
FT binding."
FT /evidence="ECO:0000269|PubMed:22143754"
FT MUTAGEN 532
FT /note="K->A: Reduced single-stranded telomeric DNA
FT binding."
FT /evidence="ECO:0000269|PubMed:22143754"
FT MUTAGEN 554
FT /note="R->A: Reduced single-stranded telomeric DNA
FT binding."
FT /evidence="ECO:0000269|PubMed:22143754"
FT MUTAGEN 560
FT /note="K->A: Reduced single-stranded telomeric DNA
FT binding."
FT /evidence="ECO:0000269|PubMed:22143754"
FT MUTAGEN 588
FT /note="R->A: Reduced single-stranded telomeric DNA
FT binding."
FT /evidence="ECO:0000269|PubMed:22143754"
FT MUTAGEN 590
FT /note="F->A: Does not affect single-stranded telomeric DNA
FT binding; abolished telomerase activity of the holoenzyme
FT telomerase ribonucleoprotein complex."
FT /evidence="ECO:0000269|PubMed:25225329"
FT MUTAGEN 601
FT /note="M->A: Reduced single-stranded telomeric DNA
FT binding."
FT /evidence="ECO:0000269|PubMed:22143754"
FT MUTAGEN 603
FT /note="F->A: Strongly reduced single-stranded telomeric DNA
FT binding; reduced telomerase activity of the holoenzyme
FT telomerase ribonucleoprotein complex."
FT /evidence="ECO:0000269|PubMed:22143754,
FT ECO:0000269|PubMed:25225329"
FT MUTAGEN 648
FT /note="F->A: Does not affect single-stranded telomeric DNA
FT binding; abolished telomerase activity of the holoenzyme
FT telomerase ribonucleoprotein complex."
FT /evidence="ECO:0000269|PubMed:25225329"
FT MUTAGEN 660
FT /note="K->A: Abolished single-stranded telomeric DNA
FT binding; reduced telomerase activity of the holoenzyme
FT telomerase ribonucleoprotein complex."
FT /evidence="ECO:0000269|PubMed:22143754,
FT ECO:0000269|PubMed:25225329"
FT HELIX 205..210
FT /evidence="ECO:0007829|PDB:3U4V"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:3U4V"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:3U4V"
FT STRAND 227..237
FT /evidence="ECO:0007829|PDB:3U4V"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:3U4V"
FT STRAND 261..269
FT /evidence="ECO:0007829|PDB:3U4V"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:3U4V"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:3U4V"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:3U4V"
FT STRAND 296..302
FT /evidence="ECO:0007829|PDB:3U4V"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:3U4V"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:3U4V"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:3U4Z"
FT STRAND 387..399
FT /evidence="ECO:0007829|PDB:3U4Z"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:3U4Z"
FT STRAND 418..422
FT /evidence="ECO:0007829|PDB:3U4Z"
FT HELIX 426..430
FT /evidence="ECO:0007829|PDB:3U4Z"
FT TURN 431..433
FT /evidence="ECO:0007829|PDB:3U4Z"
FT STRAND 439..452
FT /evidence="ECO:0007829|PDB:3U4Z"
FT STRAND 454..457
FT /evidence="ECO:0007829|PDB:3U4Z"
FT STRAND 463..466
FT /evidence="ECO:0007829|PDB:3U4Z"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:3U4Z"
FT HELIX 517..525
FT /evidence="ECO:0007829|PDB:3U50"
FT STRAND 532..542
FT /evidence="ECO:0007829|PDB:3U50"
FT STRAND 551..554
FT /evidence="ECO:0007829|PDB:3U50"
FT STRAND 562..565
FT /evidence="ECO:0007829|PDB:3U50"
FT TURN 566..568
FT /evidence="ECO:0007829|PDB:3U50"
FT STRAND 569..572
FT /evidence="ECO:0007829|PDB:3U50"
FT TURN 573..576
FT /evidence="ECO:0007829|PDB:3U50"
FT STRAND 582..585
FT /evidence="ECO:0007829|PDB:3U50"
FT STRAND 587..593
FT /evidence="ECO:0007829|PDB:3U50"
FT STRAND 596..602
FT /evidence="ECO:0007829|PDB:3U50"
FT HELIX 604..614
FT /evidence="ECO:0007829|PDB:3U50"
FT HELIX 620..622
FT /evidence="ECO:0007829|PDB:3U50"
FT HELIX 623..631
FT /evidence="ECO:0007829|PDB:3U50"
FT TURN 632..634
FT /evidence="ECO:0007829|PDB:3U50"
FT HELIX 636..644
FT /evidence="ECO:0007829|PDB:3U50"
FT TURN 645..648
FT /evidence="ECO:0007829|PDB:3U50"
FT STRAND 650..659
FT /evidence="ECO:0007829|PDB:3U50"
FT STRAND 668..677
FT /evidence="ECO:0007829|PDB:3U50"
FT HELIX 680..696
FT /evidence="ECO:0007829|PDB:7LMA"
SQ SEQUENCE 701 AA; 81942 MW; 12FD297973E6562E CRC64;
MKLTKGGSYI LKKVDRKQFY QDEEIVMQIK KILGQKTTDC KQYIKCECID GLGDEALIYF
EMLANQNQHL QKNDVIMIQD YLNDKTQNDK IVVLVTRFQF CKASHVQPKT AQKESIQLLN
TEKTIIQKSK ITKNPAEEVL KFIEVNEKDN SSNSEDMIIE QQKQEIKNNQ KEKQSINGFN
LEDSYSNISD ITNFGGKSNF NIGSLSDQLS KQTLLISQLQ VGKNRFSFKF EGRVVYKSST
FQNQQDSKYF FITAQDANNQ EINLSFWQKV DQSYQTLKVG QYYYFIGGEV KQFKNNLELK
FKFGDYQIIP KETLSANYVQ PLALQPSKQF GNDSIGDSDY SIHNLIEKEE SIAQKGYNGQ
KNNKYRQNNN NSKHTLLISE VLKTSKQYLS VLAQVVDIQS SDKNIRLKIC DNSCNQELKV
VIFPDLCYEW RDKFSINKWY YFNEFVRQIY NDEVQLKNNI HSSIKESDDQ RKVITYNQEQ
GVFKKSISIN SNDSFEIKPK ISYKNNSNQE QRIYSSIEEI IQQAQASEIG QKKEFYVYGN
LVSIQMKNKL YYYRCTCQGK SVLKYHGDSF FCESCQQFIN PQVHLMLRAF VQDSTGTIPV
MIFDQQSSQL INQIDPSIHV QEAGQYVKNC IENGQEEIIR QLFSKLDFAR FIFEIQFENK
EFNNEQEIAY KVLKIEKENI KEESKYLLKK LEHLINNNQN N
