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Database: UniProt
Entry: A0A2K5MXC7_CERAT
LinkDB: A0A2K5MXC7_CERAT
Original site: A0A2K5MXC7_CERAT 
ID   A0A2K5MXC7_CERAT        Unreviewed;       400 AA.
AC   A0A2K5MXC7;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Telomeric repeat-binding factor 2-interacting protein 1 {ECO:0000256|ARBA:ARBA00017805, ECO:0000256|RuleBase:RU367107};
DE            Short=TERF2-interacting telomeric protein 1 {ECO:0000256|RuleBase:RU367107};
DE   AltName: Full=Repressor/activator protein 1 homolog {ECO:0000256|ARBA:ARBA00032471, ECO:0000256|RuleBase:RU367107};
GN   Name=TERF2IP {ECO:0000313|Ensembl:ENSCATP00000029730.1};
OS   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000029730.1, ECO:0000313|Proteomes:UP000233060};
RN   [1] {ECO:0000313|Ensembl:ENSCATP00000029730.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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.
CC       {ECO:0000256|RuleBase:RU367107}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU367107}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367107}.
CC       Chromosome, telomere {ECO:0000256|RuleBase:RU367107}.
CC   -!- SIMILARITY: Belongs to the RAP1 family. {ECO:0000256|ARBA:ARBA00010467,
CC       ECO:0000256|RuleBase:RU367107}.
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DR   RefSeq; XP_011949971.1; XM_012094581.1.
DR   AlphaFoldDB; A0A2K5MXC7; -.
DR   STRING; 9531.ENSCATP00000029730; -.
DR   Ensembl; ENSCATT00000053990.1; ENSCATP00000029730.1; ENSCATG00000038084.1.
DR   GeneID; 105601729; -.
DR   KEGG; caty:105601729; -.
DR   CTD; 54386; -.
DR   GeneTree; ENSGT00390000005351; -.
DR   OMA; MEKFAVD; -.
DR   OrthoDB; 2920206at2759; -.
DR   Proteomes; UP000233060; Unplaced.
DR   Bgee; ENSCATG00000038084; Expressed in pituitary gland and 12 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR   GO; GO:0070187; C:shelterin complex; IEA:Ensembl.
DR   GO; GO:0098505; F:G-rich strand telomeric DNA binding; IEA:Ensembl.
DR   GO; GO:0019902; F:phosphatase binding; IEA:Ensembl.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0032205; P:negative regulation of telomere maintenance; IEA:Ensembl.
DR   GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0031848; P:protection from non-homologous end joining at telomere; IEA:Ensembl.
DR   GO; GO:0070198; P:protein localization to chromosome, telomeric region; IEA:Ensembl.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   GO; GO:0010833; P:telomere maintenance via telomere lengthening; IEA:UniProtKB-UniRule.
DR   CDD; cd11655; rap1_myb-like; 1.
DR   CDD; cd11653; rap1_RCT; 1.
DR   Gene3D; 1.10.10.2170; -; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 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; TELOMERE REPEAT-BINDING FACTOR 2-INTERACTING PROTEIN 1; 1.
DR   PANTHER; PTHR16466:SF6; TELOMERIC REPEAT-BINDING FACTOR 2-INTERACTING PROTEIN 1; 1.
DR   Pfam; PF16589; BRCT_2; 1.
DR   Pfam; PF08914; Myb_DNA-bind_2; 1.
DR   Pfam; PF11626; Rap1_C; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|RuleBase:RU367107};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU367107};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367107};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW   Telomere {ECO:0000256|ARBA:ARBA00022895, ECO:0000256|RuleBase:RU367107};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163,
KW   ECO:0000256|RuleBase:RU367107};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|RuleBase:RU367107}.
FT   DOMAIN          20..100
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|Pfam:PF16589"
FT   DOMAIN          132..195
FT                   /note="Rap1 Myb"
FT                   /evidence="ECO:0000259|Pfam:PF08914"
FT   DOMAIN          323..398
FT                   /note="TRF2-interacting telomeric protein/Rap1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11626"
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   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"
SQ   SEQUENCE   400 AA;  44341 MW;  3848D29202915EE9 CRC64;
     MAEAMDLGKD PNGPTHSSTL FVKEDGSSMS 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
//
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