TERF1_CRIGR
ID TERF1_CRIGR Reviewed; 438 AA.
AC O55036;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Telomeric repeat-binding factor 1;
DE AltName: Full=TTAGGG repeat-binding factor 1;
DE Flags: Fragment;
GN Name=TERF1; Synonyms=TRF1;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo, and Ovarian carcinoma;
RX PubMed=9798685; DOI=10.1038/sj.onc.1202138;
RA Smilenov L.B., Mellado W., Rao P.H., Sawant S.G., Umbricht C.B.,
RA Sukumar S., Pandita T.K.;
RT "Molecular cloning and chromosomal localization of Chinese hamster
RT telomeric protein chTRF1. Its potential role in chromosomal instability.";
RL Oncogene 17:2137-2142(1998).
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 (By similarity). {ECO:0000250}.
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 (By
CC similarity). Interacts with RTEL1. Interacts with CCDC79/TERB1 (By
CC similarity). {ECO:0000250}.
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 via its C-terminal
CC domain (By similarity). {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 -!- 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; AF043911; AAC02531.1; -; mRNA.
DR AlphaFoldDB; O55036; -.
DR BMRB; O55036; -.
DR SMR; O55036; -.
DR PRIDE; O55036; -.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
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 2: Evidence at transcript level;
KW Acetylation; ADP-ribosylation; Cell cycle; Cell division; Chromosome;
KW Cytoplasm; Cytoskeleton; DNA-binding; Isopeptide bond; Mitosis; Nucleus;
KW Phosphoprotein; Telomere; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P54274"
FT CHAIN 2..>438
FT /note="Telomeric repeat-binding factor 1"
FT /id="PRO_0000197128"
FT DOMAIN 375..432
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 403..428
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..268
FT /note="TRFH dimerization"
FT /evidence="ECO:0000250"
FT REGION 265..378
FT /note="Interaction with RLIM"
FT /evidence="ECO:0000250"
FT REGION 268..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 337..356
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 281..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..360
FT /note="Basic and acidic 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 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54274"
FT MOD_RES 219
FT /note="Phosphoserine; by ATM"
FT /evidence="ECO:0000250|UniProtKB:P54274"
FT CROSSLNK 213
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P54274"
FT CROSSLNK 325
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P54274"
FT CROSSLNK 366
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P54274"
FT NON_TER 438
SQ SEQUENCE 438 AA; 50186 MW; 7E3C2505D3E10F37 CRC64;
MAEDVSSTAP SPRGCADGRD ADPTEEQMAQ TQRNDQDQFE CQELLECQVQ VGAPDEEEEE
EEDSGLVAEA EAVAAGWMLH FLCLSLCRAF RDGRSEDFRR TRNSAEAIIH GLSSLTACQL
RTIYICQFLT RIAAGKTLDA QFENDERITP LESALMIWGS IEKEHDKLHE EIQNLIKIPA
IAVCMENGNF KEAEEVFERI FGDPNSHMPF KSKLLMIISQ KDTFHSFFQH FSYYHMMEKI
KSYVNYVLSE KSSTFLMKAA AKVVESKRTR TITSQDKPSG NDVEMETEAN LDTRKSVSDK
QSAVTESSEG TVSLLRSHKN LFLSKLQHGT QQQDLNKKER RVGTPQSTKK KKESRRATES
RIPVSKSQPV TPEKHRARKR QAWLWEEDKN LRSGVRKYGE GNWSKILLHY KFNNRTSVML
KDRWRTMKKL KLISSDSE
