POTE1_MOUSE
ID POTE1_MOUSE Reviewed; 640 AA.
AC Q91WC1; Q8BUH9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Protection of telomeres protein 1;
DE Short=mPot1;
DE AltName: Full=POT1-like telomere end-binding protein;
GN Name=Pot1; Synonyms=Pot1a;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Aorta, Cerebellum, Lung, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Component of the telomerase ribonucleoprotein (RNP) complex
CC that is essential for the replication of chromosome termini. Is a
CC component of the double-stranded telomeric DNA-binding TRF1 complex
CC which is involved in the regulation of telomere length by cis-
CC inhibition of telomerase. Also acts as a single-stranded telomeric DNA-
CC binding protein and thus may act as a downstream effector of the TRF1
CC complex and may transduce information about telomere maintenance and/or
CC length to the telomere terminus. Component of the shelterin complex
CC (telosome) that is involved in the regulation of telomere length and
CC protection. Shelterin associates with arrays of double-stranded TTAGGG
CC repeats added by telomerase and protects chromosome ends; without its
CC protective activity, telomeres are no longer hidden from the DNA damage
CC surveillance and chromosome ends are inappropriately processed by DNA
CC repair pathways. Binds to two or more telomeric single-stranded 5'-
CC TTAGGG-3' repeats (G-strand) and with high specificity to a minimal
CC telomeric single-stranded 5'-TAGGGTTAG-3' sequence. Binds telomeric
CC single-stranded sequences internally or at proximity of a 3'-end. Its
CC activity is TERT dependent but it does not increase TERT activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer or homooligomer. Component of the shelterin complex
CC (telosome) composed of TERF1, TERF2, TINF2, TERF2IP, ACD and POT1.
CC Binds single-stranded telomeric DNA as a monomer. Associated component
CC of the telomerase holoenzyme complex. Found in a complex with TERF1,
CC TINF2 and TNKS1. Interacts with TNKS1. Forms heterodimers with ACD.
CC Identified in a complex with ACD and single-stranded telomeric DNA.
CC {ECO:0000250|UniProtKB:Q9NUX5}.
CC -!- INTERACTION:
CC Q91WC1; Q5EE38-1: Acd; NbExp=2; IntAct=EBI-7051001, EBI-15647355;
CC Q91WC1; O89023: Tpp1; NbExp=2; IntAct=EBI-7051001, EBI-7051084;
CC Q91WC1; Q96AP0: ACD; Xeno; NbExp=3; IntAct=EBI-7051001, EBI-717666;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere
CC {ECO:0000250}. Note=Colocalizes with telomeric DNA. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91WC1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91WC1-2; Sequence=VSP_010848, VSP_010849;
CC -!- SIMILARITY: Belongs to the telombin family. {ECO:0000305}.
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DR EMBL; AK036052; BAC29288.1; -; mRNA.
DR EMBL; AK040864; BAC30723.1; -; mRNA.
DR EMBL; AK085041; BAC39349.1; -; mRNA.
DR EMBL; BC016121; AAH16121.1; -; mRNA.
DR CCDS; CCDS39442.1; -. [Q91WC1-1]
DR RefSeq; NP_598692.1; NM_133931.4. [Q91WC1-1]
DR AlphaFoldDB; Q91WC1; -.
DR SMR; Q91WC1; -.
DR BioGRID; 221602; 2.
DR ComplexPortal; CPX-153; Shelterin complex.
DR DIP; DIP-29608N; -.
DR IntAct; Q91WC1; 4.
DR MINT; Q91WC1; -.
DR STRING; 10090.ENSMUSP00000110986; -.
DR PhosphoSitePlus; Q91WC1; -.
DR EPD; Q91WC1; -.
DR MaxQB; Q91WC1; -.
DR PaxDb; Q91WC1; -.
DR PeptideAtlas; Q91WC1; -.
DR PRIDE; Q91WC1; -.
DR ProteomicsDB; 289369; -. [Q91WC1-1]
DR ProteomicsDB; 289370; -. [Q91WC1-2]
DR DNASU; 101185; -.
DR Ensembl; ENSMUST00000115330; ENSMUSP00000110986; ENSMUSG00000029676. [Q91WC1-1]
DR Ensembl; ENSMUST00000166445; ENSMUSP00000131928; ENSMUSG00000029676. [Q91WC1-1]
DR GeneID; 101185; -.
DR KEGG; mmu:101185; -.
DR UCSC; uc009bce.1; mouse. [Q91WC1-1]
DR UCSC; uc009bcf.1; mouse. [Q91WC1-2]
DR CTD; 101185; -.
DR MGI; MGI:2141503; Pot1a.
DR VEuPathDB; HostDB:ENSMUSG00000029676; -.
DR eggNOG; KOG4757; Eukaryota.
DR GeneTree; ENSGT00390000018285; -.
DR HOGENOM; CLU_019567_0_0_1; -.
DR InParanoid; Q91WC1; -.
DR OMA; RKITIHF; -.
DR OrthoDB; 940962at2759; -.
DR PhylomeDB; Q91WC1; -.
DR TreeFam; TF328398; -.
DR Reactome; R-MMU-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-MMU-110331; Cleavage of the damaged purine.
DR Reactome; R-MMU-171319; Telomere Extension By Telomerase.
DR Reactome; R-MMU-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-MMU-174414; Processive synthesis on the C-strand of the telomere.
DR Reactome; R-MMU-174417; Telomere C-strand (Lagging Strand) Synthesis.
DR Reactome; R-MMU-174430; Telomere C-strand synthesis initiation.
DR Reactome; R-MMU-174437; Removal of the Flap Intermediate from the C-strand.
DR Reactome; R-MMU-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-MMU-9670095; Inhibition of DNA recombination at telomere.
DR BioGRID-ORCS; 101185; 15 hits in 76 CRISPR screens.
DR ChiTaRS; Pot1a; mouse.
DR PRO; PR:Q91WC1; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q91WC1; protein.
DR Bgee; ENSMUSG00000029676; Expressed in undifferentiated genital tubercle and 243 other tissues.
DR ExpressionAtlas; Q91WC1; baseline and differential.
DR Genevisible; Q91WC1; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0000783; C:nuclear telomere cap complex; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0070187; C:shelterin complex; ISO:MGI.
DR GO; GO:1905773; F:8-hydroxy-2'-deoxyguanosine DNA binding; ISO:MGI.
DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; ISO:MGI.
DR GO; GO:1990955; F:G-rich single-stranded DNA binding; ISO:MGI.
DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; ISO:MGI.
DR GO; GO:0043047; F:single-stranded telomeric DNA binding; IDA:MGI.
DR GO; GO:0010521; F:telomerase inhibitor activity; ISO:MGI.
DR GO; GO:0061821; F:telomeric D-loop binding; ISO:MGI.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:BHF-UCL.
DR GO; GO:0051276; P:chromosome organization; IGI:MGI.
DR GO; GO:0032508; P:DNA duplex unwinding; ISO:MGI.
DR GO; GO:0070200; P:establishment of protein localization to telomere; ISO:MGI.
DR GO; GO:0051974; P:negative regulation of telomerase activity; ISO:MGI.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:1905776; P:positive regulation of DNA helicase activity; ISO:MGI.
DR GO; GO:0060383; P:positive regulation of DNA strand elongation; ISO:MGI.
DR GO; GO:0051096; P:positive regulation of helicase activity; ISO:MGI.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISO:MGI.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; IC:ComplexPortal.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:1905774; P:regulation of DNA helicase activity; ISO:MGI.
DR GO; GO:2001032; P:regulation of double-strand break repair via nonhomologous end joining; ISO:MGI.
DR GO; GO:0032210; P:regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0032202; P:telomere assembly; ISO:MGI.
DR GO; GO:0016233; P:telomere capping; ISO:MGI.
DR GO; GO:0007004; P:telomere maintenance via telomerase; ISS:UniProtKB.
DR GO; GO:0061820; P:telomeric D-loop disassembly; ISO:MGI.
DR Gene3D; 2.40.50.140; -; 2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR028389; POT1.
DR InterPro; IPR032042; POT1PC.
DR InterPro; IPR011564; Telomer_end-bd_POT1/Cdc13.
DR PANTHER; PTHR14513; PTHR14513; 1.
DR Pfam; PF02765; POT1; 1.
DR Pfam; PF16686; POT1PC; 1.
DR SMART; SM00976; Telo_bind; 1.
DR SUPFAM; SSF50249; SSF50249; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; DNA-binding; Nucleus; Reference proteome;
KW Telomere.
FT CHAIN 1..640
FT /note="Protection of telomeres protein 1"
FT /id="PRO_0000121730"
FT VAR_SEQ 538
FT /note="A -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010848"
FT VAR_SEQ 539..640
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010849"
SQ SEQUENCE 640 AA; 70863 MW; 64393BA48F14965E CRC64;
MSLVSTAPYT YTPLNLLKEG TIANVYGVVK FFKPPYVSKG TDYCSVVTIV DQTNVKLTCM
LFSGNYEALP IIYKVGDIVR FHRLKIQVYK NELQGINCSG FASLTFEGTV GMPVTARTSS
KVFSFTPQDQ KMVEALRVWA SKHISASSTL VQLCDAQPMQ YYDLTCQLLG KAQVDSTAFL
LKVWDGTQTV LPSWRVSTQD LTFEGDLSHI ERLQSLVVDI LVYDNHVQVA RSIEVGCFLR
LYSLHTKLQP GNSETSSSES LRLEFHLHGG TSYGRGIRVL PDTSPCVDQL KKALEGANLP
VTETSTGICQ SENGDSSALS NSGSGAVSPY EEERCQQVSA TILTNHQHLE KTPLCAILTQ
KAPQQYRVRA KLRSYLPRRL SQSVKLLCPK CHSVQEVPHG DSLDKILQDA ATEAPDIKLK
ATSLYYSKVW TTEDQGGRQV AVHFVKNNGI LPASSECLIL IEGGRLCEVS KLSSKFHSVM
PVRSGPESLE LLTLSAPFLI QGKVHHYGCK QCSSLKPIQN LNSRFHKGPW TPSSVAEALG
VVPLQYVFVM VFTLDDGTGV LEAYLKDSEH FFKIPASEVL TDDDLQRSLE TIMDMICPPG
IKVDAYPWLE CLLKSYNVTI GTERRICYQI FDTTVAENVV
