TE2IP_XENLA
ID TE2IP_XENLA Reviewed; 513 AA.
AC Q71M44; Q6NRA0;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=XlRAP1;
GN Name=terf2ip; Synonyms=rap1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
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 [MRNA].
RA Nishiyama A., Ishikawa F.;
RT "Xenopus laevis telomeric protein Rap1.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2004) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH70865.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; EU422979; ACC76748.1; -; mRNA.
DR EMBL; AF460963; AAQ04769.1; -; mRNA.
DR EMBL; BC070865; AAH70865.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001084428.1; NM_001090959.2.
DR AlphaFoldDB; Q71M44; -.
DR SMR; Q71M44; -.
DR DNASU; 403377; -.
DR GeneID; 403377; -.
DR KEGG; xla:403377; -.
DR CTD; 403377; -.
DR Xenbase; XB-GENE-6079233; terf2ip.L.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 403377; Expressed in neurula embryo and 19 other tissues.
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: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 2: Evidence at transcript level;
KW Activator; Chromosome; Nucleus; Reference proteome; Telomere;
KW Transcription; Transcription regulation.
FT CHAIN 1..513
FT /note="Telomeric repeat-binding factor 2-interacting
FT protein 1"
FT /id="PRO_0000398644"
FT DOMAIN 1..91
FT /note="BRCT"
FT DOMAIN 186..241
FT /note="Myb-like"
FT REGION 92..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 497..513
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 92..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 85
FT /note="H -> D (in Ref. 3; AAH70865)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 57071 MW; 9367A309A95015A3 CRC64;
MATLGGLTHS HTLFVEDDGT PVRFYIPPGP LKRQLYQLII HGGGEMCRLQ QPGALLLSTP
GSAQGAQYVS TAYVMDCVRK GELLHVDDYR LDGSHGRKRQ SKGMKQDERE GESSHGSDGK
EQVKVGEGPE EEDELSDLGE LVIEEGLEED EQESDTVKIK KENKMDCSEA QKIGSLKSAR
IHQTGRNPFT EEEDVAILVY VRDNAPHRGT VTGIALWKEM EQRRVLKRTW QAIKDRYIKH
LKGKQGYRLP LSAASRSHDP SEDESPQPIT KKSRTNTSTP WTKRPGNIGR TSEKLGTALP
MEKSSTKAPA EQSDAVESTS INFPLEKRGQ HVTKGVVRRS EGEKKSSDMS KGAVSATSKE
DQEDGGDLHI FEIANMEFEV DDTPEIELPK RSLSLREFVM GEDPPSSQSQ TQVDEVSSSP
EDSESEGLQE ALLGMMSEFK LRLRDVTQAL LKNNGELSAT RHFLRTGSRP DGFPIWIRKD
DLDLQKADAE TQKRLIQKYG SDNVAKRVAF LAS
