TINF2_MOUSE
ID TINF2_MOUSE Reviewed; 341 AA.
AC Q9QXG9; E9Q126;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=TERF1-interacting nuclear factor 2;
DE AltName: Full=TRF1-interacting nuclear protein 2;
GN Name=Tinf2; Synonyms=Tin2;
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].
RC TISSUE=Ovary, and Uterus;
RA Cheong C., Lee H.-W.;
RT "TIN2 regulates telomere length in mouse cells.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP INTERACTION WITH TERF1.
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).
CC -!- FUNCTION: 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 TTAGGG 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. Plays a role in shelterin complex assembly (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Found in a complex with POT1; TERF1 and TNKS1.
CC Component of the shelterin complex (telosome) composed of TERF1, TERF2,
CC TINF2, TERF2IP, ACD and POT1 (By similarity). Interacts with TERF1.
CC {ECO:0000250, ECO:0000269|PubMed:19487455}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere
CC {ECO:0000250}.
CC -!- DOMAIN: The TBM domain mediates interaction with TERF1. {ECO:0000250}.
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DR EMBL; AF214013; AAF23504.1; -; mRNA.
DR EMBL; CT025679; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q9QXG9; -.
DR SMR; Q9QXG9; -.
DR ComplexPortal; CPX-153; Shelterin complex.
DR IntAct; Q9QXG9; 2.
DR MINT; Q9QXG9; -.
DR STRING; 10090.ENSMUSP00000007733; -.
DR iPTMnet; Q9QXG9; -.
DR PhosphoSitePlus; Q9QXG9; -.
DR EPD; Q9QXG9; -.
DR MaxQB; Q9QXG9; -.
DR PaxDb; Q9QXG9; -.
DR PeptideAtlas; Q9QXG9; -.
DR PRIDE; Q9QXG9; -.
DR ProteomicsDB; 259104; -.
DR MGI; MGI:107246; Tinf2.
DR eggNOG; ENOG502S5UZ; Eukaryota.
DR InParanoid; Q9QXG9; -.
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 ChiTaRS; Tinf2; mouse.
DR PRO; PR:Q9QXG9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9QXG9; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0000783; C:nuclear telomere cap complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0010370; C:perinucleolar chromocenter; ISO:MGI.
DR GO; GO:0070187; C:shelterin complex; ISO:MGI.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:BHF-UCL.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:MGI.
DR GO; GO:0010836; P:negative regulation of protein ADP-ribosylation; ISO:MGI.
DR GO; GO:0032205; P:negative regulation of telomere maintenance; IDA:MGI.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; IC:ComplexPortal.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; ISO:MGI.
DR GO; GO:1904356; P:regulation of telomere maintenance via telomere lengthening; ISO:MGI.
DR GO; GO:0032202; P:telomere assembly; ISO:MGI.
DR GO; GO:0016233; P:telomere capping; ISO:MGI.
DR CDD; cd11657; TIN2_N; 1.
DR InterPro; IPR039098; TINF2.
DR InterPro; IPR029400; TINF2_N.
DR PANTHER; PTHR15512; PTHR15512; 1.
DR Pfam; PF14973; TINF2_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; Nucleus; Reference proteome; Telomere.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BSI4"
FT CHAIN 2..341
FT /note="TERF1-interacting nuclear factor 2"
FT /id="PRO_0000072542"
FT REGION 283..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 243..265
FT /note="TBM"
FT MOTIF 249..255
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSI4"
FT CONFLICT 337
FT /note="S -> G (in Ref. 1; AAF23504)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 341 AA; 37887 MW; 41A07CE00DC2B4D7 CRC64;
MAPPPGVGPA SLRFAAAASW LVVRRRRVEH FPKVVEFLQS LRAAAPGLVC YRHHERLCMS
LKAKVVVELI LQARPWDQVL NALKHHFPAE SRTTKEDRKL LEARENFCLL VKHLSEDPPS
SLQELEQDYG ESFLVAMEKL LFEYLCQLEK ALPPVRAQEL QDALSWSQPG SFITSSVALH
QYGMDMGWTF PESSTSGSGN LIEPMEESPH QQTRPAFHSP LPKAKLGPHQ PASLEHPEHL
AGHRFNLAPL GKRKSRSHWT SAKACHKERP TVMLLPFRNM GLPAQDLSNP KSREEPGAAS
AASVGTEPVC TEEAKTPSRP LGKRALEETP PDSPAASRRT V
