TE2IP_BOVIN
ID TE2IP_BOVIN Reviewed; 399 AA.
AC Q0VCT3;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Telomeric repeat-binding factor 2-interacting protein 1;
DE Short=TERF2-interacting telomeric protein 1;
DE Short=TRF2-interacting telomeric protein 1;
DE AltName: Full=Repressor/activator protein 1 homolog;
DE Short=RAP1 homolog;
GN Name=TERF2IP; Synonyms=RAP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts both as a regulator of telomere function and as a
CC transcription regulator. Involved in the regulation of telomere length
CC and protection as a component of the shelterin complex (telosome). In
CC contrast to other components of the shelterin complex, it is
CC dispensible for telomere capping and does not participate in the
CC protection of telomeres against non-homologous end-joining (NHEJ)-
CC mediated repair. Instead, it is required to negatively regulate
CC telomere recombination and is essential for repressing homology-
CC directed repair (HDR), which can affect telomere length. Does not bind
CC DNA directly: recruited to telomeric double-stranded 5'-TTAGGG-3'
CC repeats via its interaction with TERF2. Independently of its function
CC in telomeres, also acts as a transcription regulator: recruited to
CC extratelomeric 5'-TTAGGG-3' sites via its association with TERF2 or
CC other factors, and regulates gene expression. When cytoplasmic,
CC associates with the I-kappa-B-kinase (IKK) complex and acts as a
CC regulator of the NF-kappa-B signaling by promoting IKK-mediated
CC phosphorylation of RELA/p65, leading to activate expression of NF-
CC kappa-B target genes (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Associates with the I-kappa-B-kinase (IKK) core complex,
CC composed of CHUK, IKBKB and IKBKG (By similarity). Homodimer. Component
CC of the shelterin complex (telosome) composed of TERF1, TERF2, TINF2,
CC TERF2IP ACD and POT1. Interacts with TERF2 (but not TERF1) with its C-
CC terminus. Interacts with SLX4/BTBD12. Interacts with TERF2; the
CC interaction is direct (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91VL8}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q91VL8}. Chromosome
CC {ECO:0000250|UniProtKB:Q91VL8}. Chromosome, telomere
CC {ECO:0000250|UniProtKB:Q91VL8}. Note=Associates with chromosomes, both
CC at telomeres and in extratelomeric sites. Also exists as a cytoplasmic
CC form, where it associates with the IKK complex.
CC {ECO:0000250|UniProtKB:Q91VL8}.
CC -!- SIMILARITY: Belongs to the RAP1 family. {ECO:0000305}.
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DR EMBL; BC120017; AAI20018.1; -; mRNA.
DR RefSeq; NP_001068880.1; NM_001075412.2.
DR AlphaFoldDB; Q0VCT3; -.
DR SMR; Q0VCT3; -.
DR STRING; 9913.ENSBTAP00000020830; -.
DR PaxDb; Q0VCT3; -.
DR PRIDE; Q0VCT3; -.
DR Ensembl; ENSBTAT00000020830; ENSBTAP00000020830; ENSBTAG00000015686.
DR GeneID; 509625; -.
DR KEGG; bta:509625; -.
DR CTD; 54386; -.
DR VEuPathDB; HostDB:ENSBTAG00000015686; -.
DR VGNC; VGNC:50057; TERF2IP.
DR eggNOG; ENOG502RPXS; Eukaryota.
DR GeneTree; ENSGT00390000005351; -.
DR HOGENOM; CLU_028192_0_0_1; -.
DR InParanoid; Q0VCT3; -.
DR OMA; TQHSWQA; -.
DR OrthoDB; 602157at2759; -.
DR TreeFam; TF332348; -.
DR Reactome; R-BTA-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-BTA-110331; Cleavage of the damaged purine.
DR Reactome; R-BTA-171319; Telomere Extension By Telomerase.
DR Reactome; R-BTA-9670095; Inhibition of DNA recombination at telomere.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000015686; Expressed in corpus epididymis and 106 other tissues.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0070187; C:shelterin complex; IBA:GO_Central.
DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; IEA:Ensembl.
DR GO; GO:0019902; F:phosphatase binding; IEA:Ensembl.
DR GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0048239; P:negative regulation of DNA recombination at telomere; ISS:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0032205; P:negative regulation of telomere maintenance; IEA:Ensembl.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:1901985; P:positive regulation of protein acetylation; IEA:Ensembl.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0016233; P:telomere capping; IEA:Ensembl.
DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; ISS:UniProtKB.
DR Gene3D; 1.10.10.2170; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR021661; Rap1_C.
DR InterPro; IPR038104; Rap1_C_sf.
DR InterPro; IPR015010; Rap1_Myb_dom.
DR InterPro; IPR039595; TE2IP/Rap1.
DR PANTHER; PTHR16466; PTHR16466; 2.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF08914; Myb_DNA-bind_2; 1.
DR Pfam; PF11626; Rap1_C; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Chromosome; Cytoplasm; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Telomere; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CHAIN 2..399
FT /note="Telomeric repeat-binding factor 2-interacting
FT protein 1"
FT /id="PRO_0000398639"
FT DOMAIN 10..101
FT /note="BRCT"
FT DOMAIN 130..190
FT /note="Myb-like"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 383..399
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 211..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..306
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CROSSLNK 114
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CROSSLNK 196
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CROSSLNK 210
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CROSSLNK 242
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CROSSLNK 372
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
SQ SEQUENCE 399 AA; 44221 MW; 484102D9D3271EC5 CRC64;
MAEAMELGKD PNGPTHSSTL FVREDGSSMS FYVRPSPAKR RLSTLILHGG GTLCRVQEPG
AVLLAQPGEA AAEASGDFIS TQYILDCVER NEKLELEAYR LGPAPAAYQA PETKPGVLAG
GVAAAEPEPQ SQAGRMVFTD ADDVAIITYV KEHARSASSV TGNALWKAME KSSLTQHSWQ
SMKDRYLKRL RGQEHKYLLG EAPVSPSSQK LKRKAEQDPE AADSGEPQNK RTPDLPEEEF
EKEEIKENEA AVKKMLVEAT REFEEIVVDE SPDFEIHITM CDDDPCTPEE DSETQPDEEE
EEEEKVSAPE VGAAIKIIRQ LMEKFNLDLS TVTQAFLKNS GELEATSSFL ESGQRADGYP
IWSRQDDLDL QKDDEATRDA LVKKFGAQNV ARRIEFRKK
