TEP1_MOUSE
ID TEP1_MOUSE Reviewed; 2629 AA.
AC P97499;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Telomerase protein component 1;
DE AltName: Full=Telomerase-associated protein 1;
DE Short=Telomerase protein 1;
DE AltName: Full=p240;
DE AltName: Full=p80 telomerase homolog;
GN Name=Tep1; Synonyms=Tp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, RNA-BINDING, AND
RP IDENTIFICATION IN THE TELOMERASE RIBONUCLEOPROTEIN COMPLEX.
RX PubMed=9020079; DOI=10.1126/science.275.5302.973;
RA Harrington L., McPhail T., Mar V., Zhou W., Oulton R., Bass M.B.,
RA Arruda I., Robinson M.O.;
RT "A mammalian telomerase-associated protein.";
RL Science 275:973-977(1997).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=9118230; DOI=10.1016/s0092-8674(00)81933-9;
RA Nakayama J., Saito M., Nakamura H., Matsuura A., Ishikawa F.;
RT "TLP1: a gene encoding a protein component of mammalian telomerase is a
RT novel member of WD repeats family.";
RL Cell 88:875-884(1997).
RN [3]
RP RNA-BINDING.
RX PubMed=10551828; DOI=10.1074/jbc.274.46.32712;
RA Kickhoefer V.A., Stephen A.G., Harrington L., Robinson M.O., Rome L.H.;
RT "Vaults and telomerase share a common subunit, TEP1.";
RL J. Biol. Chem. 274:32712-32717(1999).
RN [4]
RP FUNCTION IN VAULT RNA LOCALIZATION/STABILIZATION, AND IDENTIFICATION IN THE
RP VAULTS RIBONUCLEOPROTEIN PARTICLE.
RX PubMed=11149928; DOI=10.1083/jcb.152.1.157;
RA Kickhoefer V.A., Liu Y., Kong L.B., Snow B.E., Stewart P.L., Harrington L.,
RA Rome L.H.;
RT "The telomerase/vault-associated protein TEP1 is required for vault RNA
RT stability and its association with the vault particle.";
RL J. Cell Biol. 152:157-164(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Liver, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the telomerase ribonucleoprotein complex that is
CC essential for the replication of chromosome termini (By similarity).
CC Also a component of the ribonucleoprotein vaults particle, a multi-
CC subunit structure involved in nucleo-cytoplasmic transport
CC (PubMed:11149928). Responsible for the localizing and stabilizing vault
CC RNA (vRNA) association in the vault ribonucleoprotein particle
CC (PubMed:11149928). {ECO:0000250|UniProtKB:Q99973,
CC ECO:0000269|PubMed:11149928}.
CC -!- SUBUNIT: Associated component of the telomerase holoenzyme complex (By
CC similarity). Component of the vault ribonucleoprotein particle, at
CC least composed of MVP, PARP4 and one or more vault RNAs (vRNAs)
CC (PubMed:11149928, PubMed:9020079). Binds to VAULTRC1, VAULTRC2 and
CC VAULTRC4/hvg4 vRNAs (PubMed:11149928, PubMed:9020079).
CC {ECO:0000250|UniProtKB:Q99973, ECO:0000269|PubMed:11149928,
CC ECO:0000269|PubMed:9020079}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome, telomere.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9020079,
CC ECO:0000269|PubMed:9118230}.
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DR EMBL; U86137; AAC53043.1; -; mRNA.
DR CCDS; CCDS36907.1; -.
DR PIR; T30987; T30987.
DR RefSeq; NP_033377.1; NM_009351.2.
DR AlphaFoldDB; P97499; -.
DR BioGRID; 204114; 2.
DR STRING; 10090.ENSMUSP00000006444; -.
DR iPTMnet; P97499; -.
DR PhosphoSitePlus; P97499; -.
DR EPD; P97499; -.
DR MaxQB; P97499; -.
DR PaxDb; P97499; -.
DR PeptideAtlas; P97499; -.
DR PRIDE; P97499; -.
DR ProteomicsDB; 263278; -.
DR Antibodypedia; 6875; 109 antibodies from 27 providers.
DR DNASU; 21745; -.
DR Ensembl; ENSMUST00000006444; ENSMUSP00000006444; ENSMUSG00000006281.
DR GeneID; 21745; -.
DR KEGG; mmu:21745; -.
DR UCSC; uc007tlt.1; mouse.
DR CTD; 7011; -.
DR MGI; MGI:109573; Tep1.
DR VEuPathDB; HostDB:ENSMUSG00000006281; -.
DR eggNOG; KOG3602; Eukaryota.
DR eggNOG; KOG4155; Eukaryota.
DR GeneTree; ENSGT00940000161338; -.
DR HOGENOM; CLU_000342_0_0_1; -.
DR InParanoid; P97499; -.
DR OMA; WINKPQT; -.
DR OrthoDB; 29963at2759; -.
DR PhylomeDB; P97499; -.
DR TreeFam; TF328424; -.
DR BioGRID-ORCS; 21745; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Tep1; mouse.
DR PRO; PR:P97499; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P97499; protein.
DR Bgee; ENSMUSG00000006281; Expressed in duodenum and 189 other tissues.
DR ExpressionAtlas; P97499; baseline and differential.
DR Genevisible; P97499; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0005697; C:telomerase holoenzyme complex; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IMP:UniProtKB.
DR GO; GO:0003720; F:telomerase activity; ISO:MGI.
DR GO; GO:0070034; F:telomerase RNA binding; IDA:BHF-UCL.
DR GO; GO:0000722; P:telomere maintenance via recombination; ISO:MGI.
DR Gene3D; 2.130.10.10; -; 6.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR025139; DUF4062.
DR InterPro; IPR045804; DUF5920.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008850; TEP1_N.
DR InterPro; IPR008858; TROVE_dom.
DR InterPro; IPR037214; TROVE_dom_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF13271; DUF4062; 1.
DR Pfam; PF19334; DUF5920; 1.
DR Pfam; PF05729; NACHT; 1.
DR Pfam; PF05386; TEP1_N; 4.
DR Pfam; PF05731; TROVE; 1.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 16.
DR SUPFAM; SSF140864; SSF140864; 1.
DR SUPFAM; SSF50978; SSF50978; 4.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50837; NACHT; 1.
DR PROSITE; PS51226; TEP1_N; 4.
DR PROSITE; PS50988; TROVE; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 8.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Chromosome; Nucleotide-binding; Nucleus; Reference proteome;
KW Repeat; Ribonucleoprotein; RNA-binding; Telomere; WD repeat.
FT CHAIN 1..2629
FT /note="Telomerase protein component 1"
FT /id="PRO_0000050983"
FT REPEAT 1..30
FT /note="TEP1 N-terminal 1"
FT REPEAT 31..60
FT /note="TEP1 N-terminal 2"
FT REPEAT 61..90
FT /note="TEP1 N-terminal 3"
FT REPEAT 91..120
FT /note="TEP1 N-terminal 4"
FT DOMAIN 227..685
FT /note="TROVE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00343"
FT DOMAIN 1171..1578
FT /note="NACHT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT REPEAT 1420..1462
FT /note="WD 1"
FT REPEAT 1681..1720
FT /note="WD 2"
FT REPEAT 1723..1761
FT /note="WD 3"
FT REPEAT 1764..1803
FT /note="WD 4"
FT REPEAT 1805..1844
FT /note="WD 5"
FT REPEAT 1847..1886
FT /note="WD 6"
FT REPEAT 1889..1930
FT /note="WD 7"
FT REPEAT 1932..1971
FT /note="WD 8"
FT REPEAT 1974..2013
FT /note="WD 9"
FT REPEAT 2015..2054
FT /note="WD 10"
FT REPEAT 2067..2106
FT /note="WD 11"
FT REPEAT 2113..2151
FT /note="WD 12"
FT REPEAT 2154..2191
FT /note="WD 13"
FT REPEAT 2193..2241
FT /note="WD 14"
FT REPEAT 2244..2282
FT /note="WD 15"
FT REPEAT 2285..2324
FT /note="WD 16"
FT REPEAT 2326..2362
FT /note="WD 17"
FT REPEAT 2375..2424
FT /note="WD 18"
FT REPEAT 2467..2507
FT /note="WD 19"
FT REPEAT 2555..2592
FT /note="WD 20"
FT REPEAT 2594..2628
FT /note="WD 21"
FT REGION 386..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1177..1184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
SQ SEQUENCE 2629 AA; 291460 MW; 62F73691F900A77B CRC64;
MEKLCGHVPG HSDILSLKNR CLTMLPDLQP LEKIHGHRSV HSDILSLENQ CLTMLSDLQP
TERIDGHISV HPDILSLENR CLTMLPDLQP LEKLCGHMSS HPDVLSLENQ CLATLPTVKS
TALTSPLLQG LHISHTAQAD LHSLKTSNCL LPELPTKKTP CFSEELDLPP GPRALKSMSA
TAQVQEVALG QWCVSKEKEF QEEESTEVPM PLYSLSLEEE EVEAPVLKLT SGDSGFHPET
TDQVLQEKKM ALLTLLCSAL ASNVNVKDAS DLTRASILEV CSALASLEPE FILKASLYAR
QQLNLRDIAN TVLAVAALLP ACRPHVRRYY SAIVHLPSDW IQVAEFYQSL AEGDEKKLVS
LPACLRAAMT DKFAEFDEYQ LAKYNPRKHR SKRRSRQPPR PQKTERPFSE RGKCFPKSLW
PLKNEQITFE AAYNAMPEKN RLPRFTLKKL VEYLHIHKPA QHVQALLGYR YPATLELFSR
SHLPGPWESS RAGQRMKLRR PETWERELSL RGNKASVWEE LIDNGKLPFM AMLRNLCNLL
RTGISARHHE LVLQRLQHEK SVVHSRQFPF RFLNAHDSID KLEAQLRSKA SPFPSNTTLM
KRIMIRNSKK NRRPASRKHL CTLTRRQLRA AMTIPVMYEQ LKREKLRLHK ARQWNCDVEL
LERYRQALET AVNLSVKHNL SPMPGRTLLV YLTDANADRL CPKSHSQGPP LNYVLLLIGM
MVARAEQVTV CLCGGGFVKT PVLTADEGIL KTAIKLQAQV QELEGNDEWP LDTFGKYLLS
LAVQRTPIDR VILFGQRMDT ELLKVAKQII WQHVNSKCLF VGVLLQKTQY ISPNLNPNDV
TLSGCTDGIL KFIAEHGASR LLEHVGQLDK LFKIPPPPGK TQAPSLRPLE ENIPGPLGPI
SQHGWRNIRL FISSTFRDMH GERDLLMRSV LPALQARVFP HRISLHAIDL RWGITEEETR
RNRQLEVCLG EVENSQLFVG ILGSRYGYIP PSYDLPDHPH FHWTHEYPSG RSVTEMEVMQ
FLNRGQRSQP SAQALIYFRD PDFLSSVPDA WKPDFISESE EAAHRVSELK RYLHEQKEVT
CRSYSCEWGG VAAGRPYTGG LEEFGQLVLQ DVWSMIQKQH LQPGAQLEQP TSISEDDLIQ
TSFQQLKTPT SPARPRLLQD TVQQLLLPHG RLSLVTGQAG QGKTAFLASL VSALKVPDQP
NEPPFVFFHF AAARPDQCLA LNLLRRLCTH LRQKLGELSA LPSTYRGLVW ELQQKLLLKF
AQSLQPAQTL VLIIDGADKL VDRNGQLISD WIPKSLPRRV HLVLSVSSDS GLGETLQQSQ
GAYVVALGSL VPSSRAQLVR EELALYGKRL EESPFNNQMR LLLAKQGSSL PLYLHLVTDY
LRLFTLYEQV SERLRTLPAT LPLLLQHILS TLEQEHGHDV LPQALTALEV TRSGLTVDQL
HAILSTWLIL PKETKSWEEV LAASHSGNPF PLCPFAYLVQ SLRSLLGEGP VERPGARLCL
SDGPLRTTIK RRYGKRLGLE KTAHVLIAAH LWKTCDPDAS GTFRSCPPEA LKDLPYHLLQ
SGNHGLLAEF LTNLHVVAAY LEVGLVPDLL EAHVLYASSK PEANQKLPAA DVAVFHTFLR
QQASLLTQYP LLLLQQAASQ PEESPVCCQA PLLTQRWHDQ FTLKWINKPQ TLKGQQSLSL
TMSSSPTAVA FSPNGQRAAV GTASGTIYLL NLKTWQEEKA VVSGCDGISS FAFLSDTALF
LTTFDGHLEL WDLQHGCWVF QTKAHQYQIT GCCLSPDRRL LATVCLGGYL KLWDTVRGQL
AFQYTHPKSL NCVAFHPEGQ VVATGSWAGS ITFFQADGLK VTKELGAPGP SVCSLAFNKP
GKIVAVGRID GTVELWAWQE GARLAAFPAQ CGCVSAVLFL HAGDRFLTAG EDGKAQLWSG
FLGRPRGCLG SLPLSPALSV ALNPDGDQVA VGYREDGINI YKISSGSQGP QHQELNVAVS
ALVWLSPSVL VSGAEDGSLH GWMFKGDSLH SLWLLSRYQK PVLGLAASRE LMAAASEDFT
VRLWPRQLLT QPHVHAVELP CCAELRGHEG PVCCCSFSPD GGILATAGRD RNLLCWDMKI
AQAPLLIHTF SSCHRDWITG CAWTKDNILV SCSSDGSVGL WNPEAGQQLG QFSGHQSAVS
AVVAVEEHIV SVSRDGTLKV WDHQGVELTS IPAHSGPISQ CAAALEPRPG GQPGSELLVV
TVGLDGATKL WHPLLVCQIR TLQGHSGPVT AAAASEASGL LLTSDDSSVQ LWQIPKEADD
SYKPRSSVAI TAVAWAPDGS MVVSGNEAGE LTLWQQAKAV ATAQAPGRVS HLIWYSANSF
FVLSANENVS EWQVGLRKGS TSTSSSLHLK RVLQEDWGVL TGLGLAPDGQ SLILMKEDVE
LLEMKPGSIP SSICRRYGVH SSILCTSKEY GLFYLQQGDS GLLSILEQKE SGEFEEILDF
NLNLNNPNGS PVSITQAKPE SESSLLCATS DGMLWNLSEC TSEGEWIVDN IWQKKAKKPK
TQTLETELSP HSELDFSIDC WIDPTNLKAQ QCKKIHLGSV TALHVLPGLL VTASKDRDVK
LWERPSMQLL GLFRCEGPVS CLEPWMEPSS PLQLAVGDTQ GNLYFLSWE
