ID A0A3P9NI59_POERE Unreviewed; 705 AA.
AC A0A3P9NI59;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 26.
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};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000009229.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000009229.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000009229.1};
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_008406782.1; XM_008408560.1.
DR RefSeq; XP_008406783.1; XM_008408561.1.
DR AlphaFoldDB; A0A3P9NI59; -.
DR STRING; 8081.ENSPREP00000009229; -.
DR Ensembl; ENSPRET00000009339.1; ENSPREP00000009229.1; ENSPREG00000006290.1.
DR GeneID; 103464448; -.
DR KEGG; pret:103464448; -.
DR CTD; 54386; -.
DR GeneTree; ENSGT00390000005351; -.
DR OMA; MRFFIRP; -.
DR OrthoDB; 2920206at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000006290; Expressed in caudal fin and 1 other cell type or tissue.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS50172; BRCT; 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:UP000242638};
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 35..100
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 164..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 705 AA; 76869 MW; 1F5AC947F14978DF CRC64;
MSSRQQDPAQ SISPVLFLTV EGEPMSFFLR PGPLKQKLQP LITAGGGTLC RVQVPGAILL
IDPEENSSVL ESDAHRYVST QYIHDCIKKE EQLNLDDYRL NPKAIQRSSS KLNNSGGSCA
GLLGGRIAYT PEEDAAILNF ISKRKSETGG NRLWQEMEKQ RVTSHSWQSM KSRFKDQLSK
NQSASTEVET KEDSNKLPEK KTEAKLNQES NAEKSPCEAT AGPAQTHSAE SDLTQIDVQS
IPAAVTPEQV ETPITASVTV DESKTSEEQP NINIQSESVE GETSHCCQTE EQAENQDSTE
TTELEKGEPL TPASPRKHHL SKNSPADQLK LSTITSSPNR TKQKLEASPV QEEPQRRLTR
RQLELEAASS SPEPYGKKLR SASSAAEQST ASPPHWKKTK AAVKLTNHRT QVAEEPPHKK
SRGKKAEAEV ESRVEQISSD AETKTVQPDE ASSALQKAEK KKEKRQLGIL EMATKEFEDD
FESDENEGPD LLNNAERTAE TTTASADAQQ PSDSSADPPG AQSNPEAEPS TQVAGPQTQS
SSSNCVPNTD APDAGSVQQP VSEVISSPSK AHLFIFDSES QVEDSQSVVG QGSAAPHHPQ
RSEDKDAAFS LTQTELEEDK QRIRELMAQT NQDLVSVTKA LLKTSGDFAA AADLLLNPSS
VSEPFWSRSD DSLLLSANPV SLQKLQEKYG EENVAKRIVF LEVKG
//
