TAP50_TETTS
ID TAP50_TETTS Reviewed; 422 AA.
AC D2CVN8; Q24BW8;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 25-MAY-2022, entry version 16.
DE RecName: Full=Telomerase-associated protein of 50 kDa {ECO:0000303|PubMed:19941821};
DE Short=p50 {ECO:0000303|PubMed:19941821};
GN Name=TAP50 {ECO:0000303|PubMed:19941821};
GN ORFNames=TTHERM_01049190 {ECO:0000312|EMBL:EAS05269.4};
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=23918804; DOI=10.1128/mcb.00792-13;
RA Hong K., Upton H., Miracco E.J., Jiang J., Zhou Z.H., Feigon J.,
RA Collins K.;
RT "Tetrahymena telomerase holoenzyme assembly, activation, and inhibition by
RT domains of the p50 central hub.";
RL Mol. Cell. Biol. 33:3962-3971(2013).
RN [4]
RP STRUCTURE BY ELECTRON MICROSCOPY OF THE TELOMERASE HOLOENZYME, AND
RP FUNCTION.
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 [5]
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 [6]
RP STRUCTURE BY ELECTRON MICROSCOPY OF THE TELOMERASE HOLOENZYME IN COMPLEX
RP 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: Tethering component of the holoenzyme telomerase
CC ribonucleoprotein (RNP) complex (PubMed:23552895). Telomerase is an
CC essential ribonucleoprotein enzyme that copies new telomeric repeats
CC onto chromosome ends by repetitively synthesizing the short telomere-
CC repeat sequence 5'-TTGGGG-3' using an RNA template component TER
CC (PubMed:23552895). In the telomerase holoenzyme complex, acts as a hub
CC that anchors the two heterotrimeric subcomplexes with the catalytic
CC core (PubMed:23552895, PubMed:23918804). {ECO:0000269|PubMed:23552895,
CC ECO:0000269|PubMed:23918804}.
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:23552895, PubMed:26472759, PubMed:29775593).
CC TEB1 and the CST-like subcomplex are tethered to the catalytic core by
CC TAP50/p50 (PubMed:19941821, PubMed:23552895, PubMed:26472759,
CC PubMed:29775593). {ECO:0000269|PubMed:19941821,
CC ECO:0000269|PubMed:23552895, ECO:0000269|PubMed:26472759,
CC ECO:0000269|PubMed:29775593}.
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Critically short telomeres.
CC {ECO:0000269|PubMed:19941821}.
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DR EMBL; EU873083; ACJ61513.1; -; mRNA.
DR EMBL; GG662375; EAS05269.4; -; Genomic_DNA.
DR RefSeq; XP_001025514.4; XM_001025514.4.
DR PDB; 7LMA; EM; 3.30 A; G=1-422.
DR PDB; 7LMB; EM; 3.80 A; G=1-422.
DR PDBsum; 7LMA; -.
DR PDBsum; 7LMB; -.
DR AlphaFoldDB; D2CVN8; -.
DR SMR; D2CVN8; -.
DR DIP; DIP-60204N; -.
DR DIP; DIP-61865N; -.
DR IntAct; D2CVN8; 5.
DR STRING; 5911.EAS05269; -.
DR EnsemblProtists; EAS05269; EAS05269; TTHERM_01049190.
DR GeneID; 7826301; -.
DR KEGG; tet:TTHERM_01049190; -.
DR HOGENOM; CLU_712698_0_0_1; -.
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:0007004; P:telomere maintenance via telomerase; IMP:UniProtKB.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Reference proteome; Telomere.
FT CHAIN 1..422
FT /note="Telomerase-associated protein of 50 kDa"
FT /id="PRO_0000449910"
FT HELIX 2..6
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 10..28
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 34..40
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:7LMA"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 88..93
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 100..117
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 120..134
FT /evidence="ECO:0007829|PDB:7LMA"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:7LMA"
FT HELIX 163..183
FT /evidence="ECO:0007829|PDB:7LMA"
SQ SEQUENCE 422 AA; 49987 MW; A31D4A76AC6F3306 CRC64;
MKLLLQNQNI FQKLKNTLNG CIKKFYDTYQ DLEQMQKFEM IVEDKLLFRY SCSQSEMFSA
QIQAHYLEKR VLQLTDGNVK YIVNFRDKGV LDKANFFDTP NNSLVIIRQW SYEIYYTKNT
FQINLVIDEM RCIDIITTIF YCKLELDFTQ GIKGISKSSS FSNQIYEYSA QYYKAIQLLK
KLLINDSYIS ELYNSTKSKQ QPRLFIFQSF KPKMNLAEQN LSRQFEQCQQ DDFGDGCLLQ
IVNYTHQSLK QIENKNNSNQ IVNGQNEISK KKRVLKSNED LYKISLQKQL KIFQEEEIEL
HSQSTIRNQT NQQLETFESD TSKRNSEKIL HSINELNTSK QKVNQMNSSQ HQIQKLENNN
LNKNILNQIN ENDIKNELEE RQQQHLTQSF NSKAQLKKII TLKKNQDILL FKPQEQEGSK
KY
