ID M3YW11_MUSPF Unreviewed; 827 AA.
AC M3YW11;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 28-JAN-2026, entry version 62.
DE RecName: Full=Telomere length regulation protein TEL2 homolog {ECO:0000256|ARBA:ARBA00018231};
GN Name=TELO2 {ECO:0000313|Ensembl:ENSMPUP00000015521.1,
GN ECO:0000313|RefSeq:XP_044928133.1, ECO:0000313|RefSeq:XP_044928134.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000015521.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000015521.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2024) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_044928133.1, ECO:0000313|RefSeq:XP_044928134.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_044928133.1,
RC ECO:0000313|RefSeq:XP_044928134.1};
RG RefSeq;
RL Submitted (APR-2025) to UniProtKB.
CC -!- FUNCTION: Regulator of the DNA damage response (DDR). Part of the TTT
CC complex that is required to stabilize protein levels of the
CC phosphatidylinositol 3-kinase-related protein kinase (PIKK) family
CC proteins. The TTT complex is involved in the cellular resistance to DNA
CC damage stresses, like ionizing radiation (IR), ultraviolet (UV) and
CC mitomycin C (MMC). Together with the TTT complex and HSP90 may
CC participate in the proper folding of newly synthesized PIKKs. Promotes
CC assembly, stabilizes and maintains the activity of mTORC1 and mTORC2
CC complexes, which regulate cell growth and survival in response to
CC nutrient and hormonal signals. May be involved in telomere length
CC regulation. {ECO:0000256|ARBA:ARBA00053387}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the TEL2 family.
CC {ECO:0000256|ARBA:ARBA00006133}.
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DR EMBL; AEYP01027867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_044928133.1; XM_045072198.1.
DR RefSeq; XP_044928134.1; XM_045072199.1.
DR AlphaFoldDB; M3YW11; -.
DR STRING; 9669.ENSMPUP00000015521; -.
DR Ensembl; ENSMPUT00000015762.1; ENSMPUP00000015521.1; ENSMPUG00000015631.1.
DR GeneID; 101691666; -.
DR KEGG; mpuf:101691666; -.
DR CTD; 9894; -.
DR eggNOG; KOG4346; Eukaryota.
DR GeneTree; ENSGT00390000006698; -.
DR HOGENOM; CLU_008764_1_0_1; -.
DR OMA; FYPQNYF; -.
DR OrthoDB; 10258062at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0110078; C:TTT Hsp90 cochaperone complex; IEA:Ensembl.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:Ensembl.
DR GO; GO:0060090; F:molecular adaptor activity; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0042162; F:telomeric DNA binding; IEA:TreeGrafter.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; IEA:TreeGrafter.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR FunFam; 1.25.40.720:FF:000001; Telomere length regulation protein TEL2; 1.
DR FunFam; 1.25.40.720:FF:000003; Telomere length regulation protein TEL2 homolog; 1.
DR Gene3D; 1.25.40.720; Telomere length regulation protein 2, C-terminal domain; 2.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR038528; TEL2_C_sf.
DR InterPro; IPR051970; TEL2_Regulation.
DR InterPro; IPR057348; TELO2_ARM.
DR InterPro; IPR019337; Telomere_length_regulation_dom.
DR PANTHER; PTHR15830; TELOMERE LENGTH REGULATION PROTEIN TEL2 FAMILY MEMBER; 1.
DR PANTHER; PTHR15830:SF10; TELOMERE LENGTH REGULATION PROTEIN TEL2 HOMOLOG; 1.
DR Pfam; PF25320; TELO2_ARM; 1.
DR Pfam; PF10193; Telomere_reg-2; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715}.
FT DOMAIN 325..422
FT /note="TELO2 ARM repeat"
FT /evidence="ECO:0000259|Pfam:PF25320"
FT DOMAIN 511..619
FT /note="Telomere length regulation protein conserved"
FT /evidence="ECO:0000259|Pfam:PF10193"
FT REGION 445..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..465
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..650
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 90677 MW; 1FA93BE9B863EB4D CRC64;
MDPARSAVLL AVQEALHNLS TSEDGGHILS TLGALKRYLQ GAENPALPGE QEEFARMHFS
AVLRCLVGRL SPGWLGLLPD GQLEDLWASF FLEGPADQAF LVLMESIEGA AGPSFHLMKV
AQLLARFLSM GRMAAVMEGQ CRPPAEPAFP LLQETLLTKV VGLPDQLGNR LQRENLEAFL
PQNYFPLLGE EIMRALQAVV DSLRGGWDCS ISFLSRVLGK ACVHGRQKEI LGVLVPRLTA
LSEGSCLWQR VCWRLVESVP DRAMEALLMG LVEVAAGPEV LSRLLGNLVV KSRKARFVMT
RKILFLQHRH STPTLQSLLG YLAMDSQRRP LLVQVLRELL ETWGSSSAVR HTPLPQQRYV
STALLICLVH LGEAELWDSR DELLASLMAG VKNRLDSSLP AVRRLGMIVA EVASARIHPE
GPRLRFQYEE DELSRELLAL AAPLPGADSP AEADASPSVA PVAAENPDRG NADGGVPQAQ
LEGSGSDLDS DDELVPYDMS GDQELKSGKA PAYVRDCVEA LTSSEDWERW EAALRALEGL
ILRSPAAVRE VSVELAKVLL HLEEKTSVVG FEGLRQRALV AVVVTDPAPV AEYLTSQFYA
VNFSLRQRMD ILDVLTLAAQ ELSRPGRLPK APQCGSPSPS SQPSSTPAPA WRAVVEERIR
NKTRRFSQGS ARRGPDARPN EFNLVAGYFF FPLLRHFDRP LVTFDLLGED QLVLGRLVHT
LGALMYLAVN TTVAVAMGKA LLEFVWTLRF HGDAFVRQGL LSAVSSVLLS VPAERLLADL
PDELLEARPW LADVAEQDPD EDCRLLAVRA LLLLEKLRHT LVPPAPP
//
