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   04-NOV-2026, entry version 189.
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       Component of the vault particle, which is a massive ribonucleoprotein
CC       complex that may play a role in cargo transport and signal transduction
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). Associates with MVP to form part of the vault particle
CC       (PubMed:11149928). The vault is a massive cage-like structure; it
CC       consists of a dimer of half-vaults, with each half-vault comprising 39
CC       identical MVP subunits (PubMed:11149928). The two half-vaults assemble
CC       to form the complete vault, where minor vault components such as PARP4,
CC       TEP1 and vault RNAs (vRNAs) may bind to the interior (PubMed:11149928,
CC       PubMed:9020079). Binds to VAULTRC1, VAULTRC2 and VAULTRC4/hvg4 vRNAs
CC       (PubMed:11149928, PubMed:9020079). {ECO:0000250|UniProtKB:Q99973,
CC       ECO:0000269|PubMed:11149928, 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   BioGRID; 204114; 2.
DR   STRING; 10090.ENSMUSP00000006444; -.
DR   GlyCosmos; P97499; 1 site, 1 glycan.
DR   GlyGen; P97499; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P97499; -.
DR   PhosphoSitePlus; P97499; -.
DR   SwissPalm; P97499; -.
DR   PaxDb; 10090-ENSMUSP00000006444; -.
DR   PeptideAtlas; P97499; -.
DR   ProteomicsDB; 263278; -.
DR   Pumba; P97499; -.
DR   DNASU; 21745; -.
DR   Ensembl; ENSMPUT00000018276; ENSMPUP00000018013; ENSMPUG00000018125.
DR   Ensembl; ENSMUST00000006444.9; ENSMUSP00000006444.8; ENSMUSG00000006281.9.
DR   GeneID; 21745; -.
DR   KEGG; mmu:21745; -.
DR   UCSC; uc007tlt.1; mouse.
DR   CTD; 7011; -.
DR   VEuPathDB; HostDB:ENSMUSG00000006281; -.
DR   AGR; MGI:109573; -.
DR   MGI; MGI:109573; Tep1.
DR   eggNOG; KOG3602; Eukaryota.
DR   eggNOG; KOG4155; Eukaryota.
DR   GeneTree; ENSGT00940000161338; -.
DR   HOGENOM; CLU_000342_0_0_1; -.
DR   InParanoid; P97499; -.
DR   OMA; AAASXKK; -.
DR   OrthoDB; 427368at2759; -.
DR   PhylomeDB; P97499; -.
DR   PRO; PR:P97499; -.
DR   Bgee; ENSMUSG00000006281; Expressed in duodenum and 193 other cell types or tissues.
DR   ExpressionAtlas; P97499; baseline and differential.
DR   CDD; cd00200; WD40; 2.
DR   FunFam; 1.25.40.370:FF:000002; Telomerase associated protein 1; 1.
DR   FunFam; 2.130.10.10:FF:000636; Telomerase protein component 1; 1.
DR   FunFam; 2.130.10.10:FF:002153; Telomerase protein component 1; 1.
DR   Gene3D; 1.25.40.370; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 6.
DR   InterPro; IPR056829; Beta-prop_TEP1_2nd.
DR   InterPro; IPR056828; Beta-prop_TEP1_C.
DR   InterPro; IPR025139; DUF4062.
DR   InterPro; IPR045804; DUF5920.
DR   InterPro; IPR007111; NACHT_NTPase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR052652; Telomerase_Complex_Comp.
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; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR44791:SF1; TELOMERASE PROTEIN COMPONENT 1; 1.
DR   PANTHER; PTHR44791; TELOMERASE PROTEIN COMPONENT 1 TEP1; 1.
DR   Pfam; PF25047; Beta-prop_TEP1_2nd; 1.
DR   Pfam; PF25048; Beta-prop_TEP1_C; 1.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF140864; TROVE domain-like; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 4.
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.
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:GO_Central.
DR   GO; GO:0005697; C:telomerase holoenzyme complex; IDA:BHF-UCL.
DR   GO; GO:0019899; F:enzyme binding; ISO:GO_Central.
DR   GO; GO:0002039; F:p53 binding; ISO:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IMP:UniProtKB.
DR   GO; GO:0003720; F:telomerase activity; IEA:Ensembl.
DR   GO; GO:0070034; F:telomerase RNA binding; IDA:BHF-UCL.
DR   GO; GO:0000722; P:telomere maintenance via recombination; ISO:GO_Central.
DR   Proteomes; UP000000589; Chromosome 14.
DR   Antibodypedia; 6875; 117 antibodies from 30 providers.
DR   RNAct; P97499; protein.
DR   BioGRID-ORCS; 21745; 2 hits in 77 CRISPR screens.
DR   AlphaFoldDB; P97499; -.
DR   FunCoup; P97499; 193.
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        386..397
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..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
//