TE2IP_XENTR
ID TE2IP_XENTR Reviewed; 509 AA.
AC B8QB46; Q0V9G9;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 73.
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;
DE Short=XtRAP1;
GN Name=terf2ip; Synonyms=rap1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=19329760; DOI=10.1096/fj.09-129619;
RA Vizlin-Hodzic D., Ryme J., Simonsson S., Simonsson T.;
RT "Developmental studies of Xenopus shelterin complexes: the message to reset
RT telomere length is already present in the egg.";
RL FASEB J. 23:2587-2594(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6; TISSUE=Heart;
RG NIH - Xenopus Gene Collection (XGC) 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). Does
CC not bind DNA directly: recruited to telomeric double-stranded 5'-
CC TTAGGG-3' repeats via its interaction with terf2. Independently of its
CC function in telomeres, also acts as a transcription regulator:
CC recruited to extratelomeric 5'-TTAGGG-3' sites via its association with
CC terf2 or other factors, and regulates gene expression (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Component of the shelterin complex (telosome).
CC Interacts with terf2; the interaction is direct (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q91VL8}.
CC Chromosome, telomere {ECO:0000250|UniProtKB:Q91VL8}.
CC -!- SIMILARITY: Belongs to the RAP1 family. {ECO:0000305}.
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DR EMBL; EU422980; ACC76749.1; -; mRNA.
DR EMBL; BC121572; AAI21573.1; -; mRNA.
DR RefSeq; NP_001137395.1; NM_001143923.1.
DR AlphaFoldDB; B8QB46; -.
DR SMR; B8QB46; -.
DR PRIDE; B8QB46; -.
DR GeneID; 779476; -.
DR KEGG; xtr:779476; -.
DR CTD; 54386; -.
DR Xenbase; XB-GENE-5905850; terf2ip.
DR eggNOG; ENOG502RPXS; Eukaryota.
DR InParanoid; B8QB46; -.
DR OrthoDB; 602157at2759; -.
DR Reactome; R-XTR-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-XTR-110331; Cleavage of the damaged purine.
DR Reactome; R-XTR-171306; Packaging Of Telomere Ends.
DR Reactome; R-XTR-171319; Telomere Extension By Telomerase.
DR Reactome; R-XTR-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-XTR-174430; Telomere C-strand synthesis initiation.
DR Reactome; R-XTR-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-XTR-9670095; Inhibition of DNA recombination at telomere.
DR Proteomes; UP000008143; Chromosome 10.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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; IBA:GO_Central.
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; 1.
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 Activator; Chromosome; Nucleus; Reference proteome; Telomere;
KW Transcription; Transcription regulation.
FT CHAIN 1..509
FT /note="Telomeric repeat-binding factor 2-interacting
FT protein 1"
FT /id="PRO_0000398645"
FT DOMAIN 1..91
FT /note="BRCT"
FT DOMAIN 185..239
FT /note="Myb-like"
FT REGION 93..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 493..509
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 93..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 325
FT /note="G -> W (in Ref. 1; ACC76749)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="N -> E (in Ref. 1; ACC76749)"
FT /evidence="ECO:0000305"
FT CONFLICT 343..344
FT /note="TE -> SD (in Ref. 1; ACC76749)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 509 AA; 56249 MW; F88D0708E57083B3 CRC64;
MAALGGLTHS RTLFVDDDGT PMSFYVPPGP LKRQLYPLIT HGGGEMCRMQ QPGALLLSAP
GSAQGAQYVS TAYIMDCVRI DKLLDVDDYR LDGSHGRPRK SQGSKKEERA PQQKVGESSQ
ESDQKQQAKV GGDLEEGDKL SDPGEPVNEE SLGSVSSTRK KENKMDCSEA QKIGSLKSAR
IHQTRRNVFT EKEDVAIMLY VRENAPHRGT GVSLWKEMEQ KQVVKRTWQA IKNRYFRYLK
GKRNYVLPLT DDSSSQEPSD DEEECPQPIT KKSRISDSTP CTEKPGVAEK TGEKLSTDTS
VEGPSTEKSD AAKTSNVNLP VEERGQEVTE GAIKRSEGNK KSTEMNEEAV SASSKENQDD
GADLHIFEIA NLEFEVEDTP ELEVPKRSFG LKEFVMGEDL PSSQSQTQVD EVSSSPDASE
SEGLQEALLS MMSEFKLSLC DVTQALLKNN GELAATRHFL QTGSRPDGYP IWVRKDDLDL
QKDDAETLKR LIQKYGADNV AKRVAFLAS
