TERF1_MOUSE
ID TERF1_MOUSE Reviewed; 421 AA.
AC P70371; Q9CY71;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Telomeric repeat-binding factor 1;
DE AltName: Full=TTAGGG repeat-binding factor 1;
GN Name=Terf1; Synonyms=Trf1;
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 [GENOMIC DNA / MRNA].
RC STRAIN=129/Sv, and BALB/cJ; TISSUE=Brain;
RX PubMed=9002672; DOI=10.1093/hmg/6.1.69;
RA Broccoli D., Chong L., Oelmann S., Fernald A.A., Marziliano N.,
RA van Steensel B., Kipling D., le Beau M.M., de Lange T.;
RT "Comparison of the human and mouse genes encoding the telomeric protein,
RT TRF1: chromosomal localization, expression and conserved protein domains.";
RL Hum. Mol. Genet. 6:69-76(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-312.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [4]
RP INTERACTION WITH GNL3L AND TIN2.
RX PubMed=19487455; DOI=10.1083/jcb.200812121;
RA Zhu Q., Meng L., Hsu J.K., Lin T., Teishima J., Tsai R.Y.;
RT "GNL3L stabilizes the TRF1 complex and promotes mitotic transition.";
RL J. Cell Biol. 185:827-839(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [6]
RP FUNCTION, AND INTERACTION WITH CCDC79.
RX PubMed=24413433; DOI=10.1038/ncb2896;
RA Shibuya H., Ishiguro K.I., Watanabe Y.;
RT "The TRF1-binding protein TERB1 promotes chromosome movement and telomere
RT rigidity in meiosis.";
RL Nat. Cell Biol. 16:145-156(2014).
CC -!- FUNCTION: Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and
CC negatively regulates telomere length. Involved in the regulation of the
CC mitotic spindle. Component of the shelterin complex (telosome) that is
CC involved in the regulation of telomere length and protection. Shelterin
CC associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by
CC telomerase and protects chromosome ends; without its protective
CC activity, telomeres are no longer hidden from the DNA damage
CC surveillance and chromosome ends are inappropriately processed by DNA
CC repair pathways. {ECO:0000269|PubMed:24413433}.
CC -!- SUBUNIT: Homodimer; can contain both isoforms. Found in a complex with
CC POT1; TINF2 and TNKS1. Interacts with ATM, TINF2, TNKS1, TNKS2, PINX1,
CC NEK2 and MAPRE1. Component of the shelterin complex (telosome) composed
CC of TERF1, TERF2, TINF2, TERF2IP ACD and POT1. Interacts with RLIM (via
CC N-terminus). Interacts with FBXO4. Interaction with TINF2 protects
CC against interaction with FBXO4 and subsequent polyubiquitination and
CC proteasomal degradation (By similarity). Interacts with GNL3L; this
CC interaction promotes homodimerization. Interacts with TIN2.
CC Interactions with GNL3L and TIN2 are mutually exclusive. Interacts with
CC RTEL1 (By similarity). Interacts with CCDC79/TERB1. {ECO:0000250,
CC ECO:0000269|PubMed:19487455, ECO:0000269|PubMed:24413433}.
CC -!- INTERACTION:
CC P70371; Q6ZQJ5: Dna2; NbExp=4; IntAct=EBI-6919183, EBI-6919222;
CC P70371; Q8C0V1-1: Terb1; NbExp=4; IntAct=EBI-6919183, EBI-16089839;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC Chromosome, telomere {ECO:0000250}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250}. Note=Colocalizes with telomeric DNA in interphase and
CC prophase cells. Telomeric localization decreases in metaphase, anaphase
CC and telophase. Associates with the mitotic spindle (By similarity).
CC {ECO:0000250}.
CC -!- DOMAIN: The acidic N-terminal domain binds to the ankyrin repeats of
CC TNKS1 and TNKS2. The C-terminal domain binds microtubules (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The TRFH dimerization region mediates the interaction with
CC TINF2. {ECO:0000250}.
CC -!- DOMAIN: The HTH domain is an independent structural unit and mediates
CC binding to telomeric DNA. {ECO:0000250}.
CC -!- PTM: Phosphorylated preferentially on Ser-219 in an ATM-dependent
CC manner in response to ionizing DNA damage. {ECO:0000250}.
CC -!- PTM: ADP-ribosylation by TNKS1 or TNKS2 diminishes its ability to bind
CC to telomeric DNA. {ECO:0000250}.
CC -!- PTM: Ubiquitinated by RLIM/RNF12, leading to its degradation by the
CC proteasome. Ubiquitinated by a SCF (SKP1-CUL1-F-box protein) ubiquitin-
CC protein ligase complex, leading to its degradation by the proteasome
CC (By similarity). {ECO:0000250}.
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DR EMBL; U65586; AAB53970.1; -; mRNA.
DR EMBL; BC034866; AAH34866.1; -; mRNA.
DR EMBL; U70994; AAB17974.1; -; Genomic_DNA.
DR EMBL; AK021235; BAB32340.1; -; mRNA.
DR CCDS; CCDS14827.1; -.
DR RefSeq; NP_033378.1; NM_009352.3.
DR AlphaFoldDB; P70371; -.
DR SMR; P70371; -.
DR BioGRID; 204116; 12.
DR ComplexPortal; CPX-153; Shelterin complex.
DR DIP; DIP-44231N; -.
DR IntAct; P70371; 15.
DR MINT; P70371; -.
DR STRING; 10090.ENSMUSP00000140744; -.
DR iPTMnet; P70371; -.
DR PhosphoSitePlus; P70371; -.
DR EPD; P70371; -.
DR MaxQB; P70371; -.
DR PaxDb; P70371; -.
DR PeptideAtlas; P70371; -.
DR PRIDE; P70371; -.
DR ProteomicsDB; 262975; -.
DR Antibodypedia; 12281; 692 antibodies from 40 providers.
DR DNASU; 21749; -.
DR Ensembl; ENSMUST00000188371; ENSMUSP00000140744; ENSMUSG00000025925.
DR GeneID; 21749; -.
DR KEGG; mmu:21749; -.
DR UCSC; uc007ajf.2; mouse.
DR CTD; 7013; -.
DR MGI; MGI:109634; Terf1.
DR VEuPathDB; HostDB:ENSMUSG00000025925; -.
DR eggNOG; ENOG502RYK3; Eukaryota.
DR GeneTree; ENSGT00940000155268; -.
DR HOGENOM; CLU_034265_0_0_1; -.
DR InParanoid; P70371; -.
DR OMA; AVAAEWM; -.
DR OrthoDB; 605826at2759; -.
DR PhylomeDB; P70371; -.
DR TreeFam; TF333209; -.
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; 21749; 18 hits in 73 CRISPR screens.
DR ChiTaRS; Terf1; mouse.
DR PRO; PR:P70371; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P70371; protein.
DR Bgee; ENSMUSG00000025925; Expressed in yolk sac and 248 other tissues.
DR ExpressionAtlas; P70371; baseline and differential.
DR Genevisible; P70371; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0000783; C:nuclear telomere cap complex; IDA:BHF-UCL.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0070187; C:shelterin complex; ISO:MGI.
DR GO; GO:0005819; C:spindle; ISO:MGI.
DR GO; GO:0071532; F:ankyrin repeat binding; ISO:MGI.
DR GO; GO:0008301; F:DNA binding, bending; ISO:MGI.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; ISS:UniProtKB.
DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0003720; F:telomerase activity; ISO:MGI.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:BHF-UCL.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045141; P:meiotic telomere clustering; IMP:MGI.
DR GO; GO:0008156; P:negative regulation of DNA replication; ISO:MGI.
DR GO; GO:1904850; P:negative regulation of establishment of protein localization to telomere; ISO:MGI.
DR GO; GO:1904911; P:negative regulation of establishment of RNA localization to telomere; ISO:MGI.
DR GO; GO:1905778; P:negative regulation of exonuclease activity; 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:1905839; P:negative regulation of telomeric D-loop disassembly; ISO:MGI.
DR GO; GO:1904792; P:positive regulation of shelterin complex assembly; ISO:MGI.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; IC:ComplexPortal.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0016233; P:telomere capping; ISO:MGI.
DR GO; GO:0000723; P:telomere maintenance; ISO:MGI.
DR GO; GO:0007004; P:telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0061820; P:telomeric D-loop disassembly; ISO:MGI.
DR Gene3D; 1.25.40.210; -; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR013867; Telomere_rpt-bd_fac_dimer_dom.
DR InterPro; IPR036507; Telomere_rpt-bd_fac_dimer_sf.
DR InterPro; IPR017357; TERF1/2.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF08558; TRF; 1.
DR PIRSF; PIRSF038016; Telomere_bd-1_Pin2; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF63600; SSF63600; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
PE 1: Evidence at protein level;
KW Acetylation; ADP-ribosylation; Cell cycle; Cell division; Chromosome;
KW Cytoplasm; Cytoskeleton; DNA-binding; Isopeptide bond; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome; Telomere; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P54274"
FT CHAIN 2..421
FT /note="Telomeric repeat-binding factor 1"
FT /id="PRO_0000197130"
FT DOMAIN 362..419
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 390..415
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..255
FT /note="TRFH dimerization"
FT /evidence="ECO:0000250"
FT REGION 252..365
FT /note="Interaction with RLIM"
FT /evidence="ECO:0000250"
FT REGION 253..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 313..367
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 263..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P54274"
FT MOD_RES 206
FT /note="Phosphoserine; by ATM"
FT /evidence="ECO:0000250|UniProtKB:P54274"
FT CROSSLNK 200
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P54274"
FT CONFLICT 283..312
FT /note="SVNGQQSTETEPLVDTVSSIRSHKNALSQL -> RSFAPSLPYGSTSCDYHI
FT RKQTGIYGIIIQ (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 421 AA; 48224 MW; 3F648F18C3ECF20A CRC64;
MAETVSSAAR DAPSREGWTD SDSPEQEEVG DDAELLQCQL QLGTPREMEN AELVAEVEAV
AAGWMLDFLC LSLCRAFRDG RSEDFRRTRD SAEAIIHGLH RLTAYQLKTV YICQFLTRVA
SGKALDAQFE VDERITPLES ALMIWNSIEK EHDKLHDEIK NLIKIQAVAV CMEIGSFKEA
EEVFERIFGD PEFYTPLERK LLKIISQKDV FHSLFQHFSY SCMMEKIQSY VGDVLSEKSS
TFLMKAATKV VENEKARTQA SKDRPDATNT GMDTEVGLNK EKSVNGQQST ETEPLVDTVS
SIRSHKNALS QLKHRRAPSD FSRNEARTGT LQCETTMERN RRTSGRNRLC VSENQPDTDD
KSGRRKRQTW LWEEDRILKC GVKKYGEGNW AKILSHYKFN NRTSVMLKDR WRTMKRLKLI
S
