TE2IP_DANRE
ID TE2IP_DANRE Reviewed; 616 AA.
AC Q6NYJ3; Q5BKV6;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 94.
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 Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NYJ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NYJ3-2; Sequence=VSP_039790;
CC -!- SIMILARITY: Belongs to the RAP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH66572.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH90914.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC066572; AAH66572.1; ALT_INIT; mRNA.
DR EMBL; BC090914; AAH90914.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q6NYJ3; -.
DR SMR; Q6NYJ3; -.
DR STRING; 7955.ENSDARP00000051258; -.
DR PaxDb; Q6NYJ3; -.
DR ZFIN; ZDB-GENE-131121-641; terf2ip.
DR eggNOG; ENOG502RPXS; Eukaryota.
DR InParanoid; Q6NYJ3; -.
DR PhylomeDB; Q6NYJ3; -.
DR Reactome; R-DRE-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-DRE-110331; Cleavage of the damaged purine.
DR Reactome; R-DRE-171306; Packaging Of Telomere Ends.
DR Reactome; R-DRE-171319; Telomere Extension By Telomerase.
DR Reactome; R-DRE-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-DRE-174414; Processive synthesis on the C-strand of the telomere.
DR Reactome; R-DRE-174417; Telomere C-strand (Lagging Strand) Synthesis.
DR Reactome; R-DRE-174430; Telomere C-strand synthesis initiation.
DR Reactome; R-DRE-174437; Removal of the Flap Intermediate from the C-strand.
DR Reactome; R-DRE-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-DRE-9670095; Inhibition of DNA recombination at telomere.
DR PRO; PR:Q6NYJ3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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 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; 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.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 2: Evidence at transcript level;
KW Activator; Alternative splicing; Chromosome; Nucleus; Reference proteome;
KW Telomere; Transcription; Transcription regulation.
FT CHAIN 1..616
FT /note="Telomeric repeat-binding factor 2-interacting
FT protein 1"
FT /id="PRO_0000398643"
FT DOMAIN 15..98
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 112..169
FT /note="Myb-like"
FT REGION 174..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 597..613
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 198..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 481..616
FT /note="QPDSPMSEEERPGPSSAVVPPSLNSSTSCSHIRETPEETLSRDLLEVKEQVI
FT NLMRETKKDLVEVTKALLKASGDLKRAQVFLLNGYDHETHGPLWTRLDDETLLAADPYE
FT LEQLQSKFGEEEVTRRKSFLATDVK -> CWRSRSRSLI (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_039790"
SQ SEQUENCE 616 AA; 68075 MW; 1AAA287DAC090182 CRC64;
MSKKKEASKI SPVLFLDPGG QSMRFYVRPG PTKMQLHPLI TSGGGNLCRN QEPGAILLID
PTDATNVTQN TGQKYISTKY ILDCVEQNQQ LDPNDYAIII GPSVQTRMAL RNQGSGRLGY
SSEEDAAILK FIEKRQQDAK GNLVWKEMEK RHVTEHSWQS MKDRFLKHLQ QKLADKPTKK
SPIKRKPLSF TQSPLRKKKV VEISEDESVQ KGDCPEAPMA TETGSINPPA SPERASSPPE
EPQAAGQPSQ ASSNDSQDET CVLVIETPES ENPRLDEDAP DASNEHSSLK KKRRKTCKTS
TTDSRSSRLE EDPVGQDIPD ESNAQSSPKK KRQKACKTST TDSRSSRLEE NPDRRDIPDE
STEQSSPNKS QMTSKISTSD SGNPIGDQGC DNPHGCNANS SPSKTRQTNS EASTPDSKKL
GILAKAAKEF EDSDVMDDSE ECENPCEVPI AEPSDAQESS ATPATLVREP ESQAEHHEET
QPDSPMSEEE RPGPSSAVVP PSLNSSTSCS HIRETPEETL SRDLLEVKEQ VINLMRETKK
DLVEVTKALL KASGDLKRAQ VFLLNGYDHE THGPLWTRLD DETLLAADPY ELEQLQSKFG
EEEVTRRKSF LATDVK
