TE2IP_MACFA
ID TE2IP_MACFA Reviewed; 400 AA.
AC Q4R4I0; Q4R8V2;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
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; ORFNames=QtrA-13975, QtsA-11378;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Temporal cortex, and Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE00469.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB168345; BAE00469.1; ALT_FRAME; mRNA.
DR EMBL; AB169914; BAE01995.1; -; mRNA.
DR RefSeq; XP_005592646.1; XM_005592589.2.
DR AlphaFoldDB; Q4R4I0; -.
DR BMRB; Q4R4I0; -.
DR SMR; Q4R4I0; -.
DR STRING; 9541.XP_005592646.1; -.
DR GeneID; 102123393; -.
DR KEGG; mcf:102123393; -.
DR VEuPathDB; HostDB:ENSMFAG00000034117; -.
DR eggNOG; ENOG502RPXS; Eukaryota.
DR OMA; TQHSWQA; -.
DR OrthoDB; 602157at2759; -.
DR Proteomes; UP000233100; Chromosome 20.
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 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..400
FT /note="Telomeric repeat-binding factor 2-interacting
FT protein 1"
FT /id="PRO_0000398640"
FT DOMAIN 78..101
FT /note="BRCT"
FT DOMAIN 128..188
FT /note="Myb-like"
FT REGION 105..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 384..400
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 208..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..307
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 154
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 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT MOD_RES 206
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 194
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CROSSLNK 208
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CROSSLNK 212
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CROSSLNK 240
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
FT CROSSLNK 373
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NYB0"
SQ SEQUENCE 400 AA; 44369 MW; 32BB686C329763E1 CRC64;
MAEAMDLGKD PNGPTHSSTL FVREDGSSMS FYVRPSPAKR RLSTLILHGG GTVCRVQEPG
AVLLAQPGEA LAEASGDFIS TQYILDCVER NERLELEAYR LGSASAADTG SEAKPGALAE
GAAEPEPQRL AGRIAFTDAD DVAILTYVKE NARSPSSVTG NALWKAMEKS SLTQHSWQSL
KDRYLKHLRG QEHKYLLGDA PVSPSSQKLK RKAEEDPEAA DSGEPQNKRT PDLPEEEYVK
EEIQENEEAV KKMLVEATRE FEEVVVDESP PDFEIHITMC DDDPPTPEED SETQPDEEEE
EEEEEKVSQP EVGAAIKIIR QLMEKFNLDL STVTQAFLKN SGELEATSAF LASGQRADGY
PIWSRQDDID LQKDDEDTRE ALVKKFGAQN VARRIEFRKK
