TAP19_TETTS
ID TAP19_TETTS Reviewed; 164 AA.
AC D2CVN7; I7MM24;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=Telomerase-associated protein of 19 kDa {ECO:0000303|PubMed:19941821};
DE Short=p19 {ECO:0000303|PubMed:19941821};
GN Name=TAP19 {ECO:0000303|PubMed:19941821};
GN ORFNames=TTHERM_00658760 {ECO:0000312|EMBL:EAS03832.1};
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 [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 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 [4] {ECO:0007744|PDB:5DFM}
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 1-157, AND STRUCTURE BY ELECTRON
RP 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 [5] {ECO:0007744|PDB:5DOF, ECO:0007744|PDB:5DOI}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 12-174 IN COMPLEX WITH TAP45 AND
RP TAP75, FUNCTION, IDENTIFICATION IN THE TELOMERASE HOLOENZYME, AND
RP MUTAGENESIS OF ARG-38; TYR-145; MET-147; ALA-158 AND ILE-161.
RX PubMed=26551074; DOI=10.1038/nsmb.3126;
RA Wan B., Tang T., Upton H., Shuai J., Zhou Y., Li S., Chen J.,
RA Brunzelle J.S., Zeng Z., Collins K., Wu J., Lei M.;
RT "The Tetrahymena telomerase p75-p45-p19 subcomplex is a unique CST
RT complex.";
RL Nat. Struct. Mol. Biol. 22:1023-1026(2015).
CC -!- FUNCTION: Component of a CST-like subcomplex of the holoenzyme
CC telomerase ribonucleoprotein complex, which stimulates telomerase
CC complementary-strand synthesis (PubMed:26551074). 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:26551074). The CST-like subcomplex (also named 7-4-1) binds
CC telomeric single-stranded DNA and coordinates telomere G-strand and C-
CC strand synthesis (PubMed:26551074). {ECO:0000269|PubMed:26551074}.
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:26551074, PubMed:26472759).
CC TEB1 and the CST-like subcomplex are tethered to the catalytic core by
CC TAP50/p50 (PubMed:19941821, PubMed:23552895, PubMed:26472759).
CC {ECO:0000269|PubMed:19941821, ECO:0000269|PubMed:23552895,
CC ECO:0000269|PubMed:26472759, ECO:0000269|PubMed:26551074}.
CC -!- INTERACTION:
CC D2CVN7; Q6JXI5: TAP45; NbExp=9; IntAct=EBI-16181555, EBI-16181547;
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Critically short telomeres.
CC {ECO:0000269|PubMed:19941821}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAS03832.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; EU873082; ACJ61512.1; -; mRNA.
DR EMBL; GG662471; EAS03832.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001024077.1; XM_001024077.1.
DR PDB; 5DFM; X-ray; 2.30 A; A/B=1-157.
DR PDB; 5DOF; X-ray; 1.70 A; A/B/C/D=1-157.
DR PDB; 5DOI; X-ray; 2.20 A; A/B/C/D=1-157.
DR PDBsum; 5DFM; -.
DR PDBsum; 5DOF; -.
DR PDBsum; 5DOI; -.
DR AlphaFoldDB; D2CVN7; -.
DR SMR; D2CVN7; -.
DR DIP; DIP-60206N; -.
DR DIP; DIP-61868N; -.
DR IntAct; D2CVN7; 5.
DR STRING; 5911.EAS03832; -.
DR EnsemblProtists; EAS03832; EAS03832; TTHERM_00658760.
DR GeneID; 7833732; -.
DR KEGG; tet:TTHERM_00658760; -.
DR HOGENOM; CLU_1543139_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..164
FT /note="Telomerase-associated protein of 19 kDa"
FT /id="PRO_0000449908"
FT MUTAGEN 38
FT /note="R->E: Abolished interaction with TAP45/p45;
FT overexpression causes telomere 3'-overhang elongation."
FT /evidence="ECO:0000269|PubMed:26551074"
FT MUTAGEN 145
FT /note="Y->A: Abolished interaction with TAP45/p45."
FT /evidence="ECO:0000269|PubMed:26551074"
FT MUTAGEN 147
FT /note="M->W: Abolished interaction with TAP45/p45."
FT /evidence="ECO:0000269|PubMed:26551074"
FT MUTAGEN 158
FT /note="A->R,W: Does not affect interaction with TAP45/p45."
FT /evidence="ECO:0000269|PubMed:26551074"
FT MUTAGEN 161
FT /note="I->R: Abolished interaction with TAP45/p45."
FT /evidence="ECO:0000269|PubMed:26551074"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:5DOF"
FT HELIX 19..23
FT /evidence="ECO:0007829|PDB:5DOF"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:5DOI"
FT STRAND 35..47
FT /evidence="ECO:0007829|PDB:5DOF"
FT HELIX 49..58
FT /evidence="ECO:0007829|PDB:5DOF"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:5DOF"
FT HELIX 65..77
FT /evidence="ECO:0007829|PDB:5DOF"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:5DOF"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:5DOF"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:5DOF"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:5DOF"
FT STRAND 122..131
FT /evidence="ECO:0007829|PDB:5DOF"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:5DOF"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:5DOF"
FT HELIX 150..159
FT /evidence="ECO:0007829|PDB:5DOF"
SQ SEQUENCE 164 AA; 19473 MW; 591F49EFC6915CFA CRC64;
MQQPKRNFDL YKLITDKQID FQVADLIQDE QSSFVSVRIY GQFKCFVPKS TIQEQLDKIK
NLSSKELAKN KIFKFLSEYN KNNQKQDELS HDYYGYFKVQ QHQFILNLEN AQREASLAVD
DFYFINGRIY KTNHDILILQ AHHVYQMQKP TLQLLQAASE INQN
