TAP75_TETTS
ID TAP75_TETTS Reviewed; 622 AA.
AC A0PGB2; I7MHB0;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Telomerase-associated protein of 75 kDa {ECO:0000303|PubMed:17220281};
DE Short=p75 {ECO:0000303|PubMed:17220281};
GN Name=TAP75 {ECO:0000303|PubMed:17220281};
GN ORFNames=TTHERM_00059040 {ECO:0000312|EMBL:EAR87391.2};
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.
RX PubMed=17220281; DOI=10.1128/mcb.02105-06;
RA Witkin K.L., Prathapam R., Collins K.;
RT "Positive and negative regulation of Tetrahymena telomerase holoenzyme.";
RL Mol. Cell. Biol. 27:2074-2083(2007).
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 IDENTIFICATION IN THE TELOMERASE HOLOENZYME.
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 [4]
RP FUNCTION.
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).
RN [5]
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 [6]
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).
CC -!- FUNCTION: Component of a CST-like subcomplex of the holoenzyme
CC telomerase ribonucleoprotein complex, which stimulates telomerase
CC complementary-strand synthesis (Probable). Telomerase is an essential
CC ribonucleoprotein enzyme that copies new telomeric repeats onto
CC chromosome ends by repetitively synthesizing the short telomere-repeat
CC sequence 5'-TTGGGG-3' using an RNA template component TER (Probable).
CC The CST-like subcomplex (also named 7-4-1) binds telomeric single-
CC stranded DNA and coordinates telomere G-strand and C-strand synthesis
CC (Probable). {ECO:0000305|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:17220281, PubMed:19941821, PubMed:23552895, 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:17220281, ECO:0000269|PubMed:19941821,
CC ECO:0000269|PubMed:23552895, ECO:0000269|PubMed:26472759}.
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Telomere shortening without affecting the
CC accumulation of TER or TERT. {ECO:0000269|PubMed:17220281}.
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DR EMBL; AY522576; AAS97866.1; -; mRNA.
DR EMBL; GG662853; EAR87391.2; -; Genomic_DNA.
DR RefSeq; XP_001007636.2; XM_001007636.3.
DR AlphaFoldDB; A0PGB2; -.
DR DIP; DIP-60202N; -.
DR DIP; DIP-61866N; -.
DR IntAct; A0PGB2; 5.
DR STRING; 5911.EAR87391; -.
DR GeneID; 7829531; -.
DR KEGG; tet:TTHERM_00059040; -.
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.
PE 1: Evidence at protein level;
KW Chromosome; Reference proteome; Telomere.
FT CHAIN 1..622
FT /note="Telomerase-associated protein of 75 kDa"
FT /id="PRO_0000449911"
SQ SEQUENCE 622 AA; 73814 MW; 723B49CE222A2E31 CRC64;
MEIEEDLNLK ILEDVKKLYL QSFDYIKNGI SSSLPSDKKF LADDDIDLSR ITFLYKFISV
NPTLLLINEK TQAKRRIFQG EYLYGKKKIQ FNIIAKNLEI ERELIQFFKK PYQCYIMHNV
QVFQMLNKNK NNNVVEFMDS EDLQSSVDCQ LYYLIDESSH VLEDDSMDFI STLTRLSDSF
NSNEFVFETN YSIQISQMPK PLNTTHFKLL QPKVVNSFEG VILQVQEGKN ILQIEELIDQ
VYLNSRRDRF YILKVANGKN YMDFIEVYLV YDNEDQEAKQ QLQFYLKPFQ RILIFQSLKH
FTKNLKLFMI SFFYSSGVQP NNSNVKNFLV SHKGVEFFSR FDIQKNELLC KDLIKSYNKL
PLSNISKLLE DEGVMIRSNM KFQVRVKKVK YFKIRLNCLN CKQEWTVGLK NCINCKGQQS
YISYNIQVLV QDQHFLEQQA YIYLYDDLAA QFFNITESEK KELHLHLTKN ETFIQLYYSF
NKDYPLSIIK FKDKIFNKDI TNCIVAYPFA DIDNKIFNSQ QQIIQDENLR IESEKFIQNF
TEDNNLQESK LYYEKFKSKN KQQIFVNGTY ISTNYSQGQK ICLKPIPCLK VMYVFPQEDI
KLSALKIIEE INQLKIQIDQ LN
