ID A0A2Y9NXW7_DELLE Unreviewed; 398 AA.
AC A0A2Y9NXW7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-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};
GN Name=TERF2IP {ECO:0000313|RefSeq:XP_022438860.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022438860.1};
RN [1] {ECO:0000313|RefSeq:XP_022438860.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022438860.1};
RG RefSeq;
RL Submitted (NOV-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_022438860.1; XM_022583152.2.
DR AlphaFoldDB; A0A2Y9NXW7; -.
DR STRING; 9749.A0A2Y9NXW7; -.
DR Ensembl; ENSDLET00000003261; ENSDLEP00000002859; ENSDLEG00000002312.
DR KEGG; dle:111179497; -.
DR InParanoid; A0A2Y9NXW7; -.
DR OrthoDB; 2920206at2759; -.
DR Proteomes; UP000248483; Unplaced.
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 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:UP000248483};
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 21..100
FT /note="BRCT"
FT /evidence="ECO:0000259|Pfam:PF16589"
FT DOMAIN 134..197
FT /note="Rap1 Myb"
FT /evidence="ECO:0000259|Pfam:PF08914"
FT DOMAIN 321..396
FT /note="TRF2-interacting telomeric protein/Rap1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11626"
FT REGION 106..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..305
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 398 AA; 44264 MW; 85A1DCA09D05FB06 CRC64;
MAEAMDLGKD PNGPTHSSTL FVREDGSSMS FYVRPSPAKR RLSTLILHGG GTLCRMQEPG
AVLLAQPGEA AAEASGDFIS TQYILDCVER NERLELEAYR LGPALGADQA PETKPGAQAG
GAAVTEPELQ PHAGRIVFTD ADDVAILTYV KEHARSPSSV TGNALWKAME KSSLTQHSWQ
SMKDRYLKRL RGQEHKYLLG EAPVSPSSQK LKRKTEQDPE DADSGEPQNK RTPDLPEEEF
EKEEIKENEE AVKKMLVEAT REFEEIVVDE SPDFEIHITM CDDDPPTPEE DSETQPDEEE
EEEKVSAPEV GAAIKIIRQL MEKFNLDLST VTQAFLKNSG ELEATSSFLE SGQRADGYPI
WSRQDDLDLQ KDDEGTRDAL VKKFGAQNVA RRIEFRKK
//
