TE2IP_RAT
ID TE2IP_RAT Reviewed; 393 AA.
AC Q5EAN7;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; BC090335; AAH90335.1; -; mRNA.
DR RefSeq; NP_001013161.1; NM_001013143.1.
DR AlphaFoldDB; Q5EAN7; -.
DR SMR; Q5EAN7; -.
DR STRING; 10116.ENSRNOP00000014660; -.
DR iPTMnet; Q5EAN7; -.
DR PhosphoSitePlus; Q5EAN7; -.
DR jPOST; Q5EAN7; -.
DR PaxDb; Q5EAN7; -.
DR PRIDE; Q5EAN7; -.
DR Ensembl; ENSRNOT00000114583; ENSRNOP00000085839; ENSRNOG00000010712.
DR GeneID; 307861; -.
DR KEGG; rno:307861; -.
DR UCSC; RGD:1309684; rat.
DR CTD; 54386; -.
DR RGD; 1309684; Terf2ip.
DR eggNOG; ENOG502RPXS; Eukaryota.
DR GeneTree; ENSGT00390000005351; -.
DR HOGENOM; CLU_028192_0_0_1; -.
DR InParanoid; Q5EAN7; -.
DR OMA; TQHSWQA; -.
DR OrthoDB; 602157at2759; -.
DR PhylomeDB; Q5EAN7; -.
DR TreeFam; TF332348; -.
DR Reactome; R-RNO-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-RNO-110331; Cleavage of the damaged purine.
DR Reactome; R-RNO-171306; Packaging Of Telomere Ends.
DR Reactome; R-RNO-171319; Telomere Extension By Telomerase.
DR Reactome; R-RNO-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-RNO-174414; Processive synthesis on the C-strand of the telomere.
DR Reactome; R-RNO-174417; Telomere C-strand (Lagging Strand) Synthesis.
DR Reactome; R-RNO-174430; Telomere C-strand synthesis initiation.
DR Reactome; R-RNO-174437; Removal of the Flap Intermediate from the C-strand.
DR Reactome; R-RNO-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-RNO-9670095; Inhibition of DNA recombination at telomere.
DR PRO; PR:Q5EAN7; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000010712; Expressed in lung and 20 other tissues.
DR Genevisible; Q5EAN7; RN.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0070187; C:shelterin complex; IBA:GO_Central.
DR GO; GO:0042162; F:telomeric DNA binding; ISO:RGD.
DR GO; GO:0048239; P:negative regulation of DNA recombination at telomere; ISS:UniProtKB.
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: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:0010833; P:telomere maintenance via telomere lengthening; ISS:UniProtKB.
DR Gene3D; 1.10.10.2170; -; 1.
DR InterPro; IPR001357; BRCT_dom.
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 1: Evidence at protein 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..393
FT /note="Telomeric repeat-binding factor 2-interacting
FT protein 1"
FT /id="PRO_0000398641"
FT DOMAIN 10..101
FT /note="BRCT"
FT DOMAIN 125..185
FT /note="Myb-like"
FT REGION 104..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 377..393
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 206..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..299
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 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CROSSLNK 111
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CROSSLNK 205
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CROSSLNK 209
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CROSSLNK 237
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CROSSLNK 366
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
SQ SEQUENCE 393 AA; 43418 MW; EFEE754F5AA59F49 CRC64;
MAEVMDLGKD PNGPTHSSTL FVREDGSAMS FYVRPSSAKR RLSTLILHGG GILCRVQKPG
AVLLAQPGEA LAEASGDFIS TQYILDCVER NEKLELEAYR LGLTEQASDP KPGASAEGST
EPEPQPLTGR IAYTDADDVA ILTYVKENAR SPSSVTGNAL WKAMEKSSLT QHSWQSLKDR
YLKHLQGQEH KYLLGNAPVS PSSQKLKRKA EQDPEAADSG EPQNKRTPDL PEEECVKGET
KENGEADNKL FEEATPELGE AVVDESPDFE IHITMCDGDP PTPEEDSETQ PDEEEEEPKV
STQEVGTAIK IIRQLMEKFN LDLSTVTQAL LKNSGELEAT SSFLESGRRP DGFPIWCRQD
DLDLQKDDDD TRNALVKKYG AQNVARRIEF RKK
