ID A0A3Q1HEL2_9TELE Unreviewed; 704 AA.
AC A0A3Q1HEL2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, 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};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000027135.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000027135.1}
RP IDENTIFICATION.
RG Ensembl;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3Q1HEL2; -.
DR Ensembl; ENSAPOT00000001962.1; ENSAPOP00000027135.1; ENSAPOG00000011492.1.
DR GeneTree; ENSGT00390000005351; -.
DR OrthoDB; 2920206at2759; -.
DR Proteomes; UP000257200; 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 CDD; cd11653; rap1_RCT; 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; 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.
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:UP000257200};
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 17..100
FT /note="BRCT"
FT /evidence="ECO:0000259|Pfam:PF16589"
FT DOMAIN 126..182
FT /note="Rap1 Myb"
FT /evidence="ECO:0000259|Pfam:PF08914"
FT DOMAIN 636..702
FT /note="TRF2-interacting telomeric protein/Rap1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11626"
FT REGION 106..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 77590 MW; 8936AFFAE82B053B CRC64;
MPSKQENVVQ PAYSPVLFMN VDGQPMSFFL RPGPTKRKLQ PLITAGGGIL SNVQQPGVIL
LMDPEERSSI PESTSHWYVS IQYIHDCIEK NEQLDLEDYK LNPGVVQRSS PRLNRSKESS
PRLSRGRLLY TPEEDAAILS HVSKHKTEVG GNRLWQQMEK QRVTSHSWQS MKSHYKVLAE
KQSQVVNLET TEDNKATEEE TEVENNQGTD APKHPCEEDV VPPQTHSADL DFTQIDLQSL
LDECKAENAD AETSISAQEE EQQMNQQTDE PPAEGIQTET VEAETSNPPQ NDWLCPDVQT
DIQLITAENT ERDGPQTTVS PQKQSLLEES QPSQPESTPK TTSSKKPKEK QKTSSSLEQP
QRRITRRQLE LEMSLSPEPY AKKLRSSLNS AEQPTSSPQC TKKTKSAVKS ALRKDTTPNE
PPSKKARGGS VEAAAESQPE QNGDAAVSGT APADESDSVP QKAEKKKEKR KLGILELATK
EFEDESESDE APDLPPETEA TSTEPSVPPP LDTAADPASP QSSPEPASSL QENVQEAHAS
SSNFVAETSC PKPAATEPAA VSEAVNAQFN AHLFIFDSES QEEDSQSIVG DRPAAASNPE
PLVNKDTAFS LTQTQLEEDK QRIRELMNQT DQDLVSVTKA LLKTSGDFTA ALDLLLNPSS
ISGPFWNRCD DNLLLSTDPV VRQQLQEKYG EEEVAKRIVF LEVV
//
