ID A0A3B4US36_SERDU Unreviewed; 667 AA.
AC A0A3B4US36;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000021157.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000021157.1}
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 STRING; 41447.ENSSDUP00000021176; -.
DR Ensembl; ENSSDUT00000021542.1; ENSSDUP00000021157.1; ENSSDUG00000015403.1.
DR Ensembl; ENSSDUT00000021563.1; ENSSDUP00000021176.1; ENSSDUG00000015403.1.
DR GeneTree; ENSGT00390000005351; -.
DR OMA; MRFFIRP; -.
DR OrthoDB; 2920206at2759; -.
DR Proteomes; UP000261420; 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.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367107};
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 36..101
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 191..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 571..602
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 205..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 667 AA; 73337 MW; 1F516F6917DEAB36 CRC64;
MPFKEEDVAK SNISSVLFKT AEGEPMSFFL RPGLVKSKLQ PLITSGGGML CSVQQPGAIL
LIDPEERGSL RETTAHWYVS TQYIYDCIEK EERLNIEDYR LSPEEVPRHS GRLFNNYKEC
FLKVLGGRAA YTPEEDAAIL NYVSNHKSET GGNRLWQAME KQCVTSHSWQ SMKYRYKVQL
AKKNPEVEKV KTAEEEIKEA GSQETDVQKP PSEDAASPQT HSAATDLTQI DTQLLPAEST
QPENVEAETS NSPQPGEPCL DPQTDAHPIP AESTEPATAE PQTTASPQKE SAPEDSLQSL
PNTPTPKNRK QPKQRASPEL QQPQRRLTRR HLELEMSSSP KPYSKKLRSS STSPKKLSSS
PQPVNNTKSA VKLAAQKHTA TDPPPSKRAR GKSVAPVAES RQEESEEAAV SEIQQTDEES
TSSPQKVETK KEKRKLGILE LATKEFEDES ESAEDEAPDL RNPAETAAIQ PTSTEPLSSV
TAADPVSTQS NPEPGPSLQG KAQQTQSPSS NRVPETGCPE PAASEAVHAA SRPHLFIFDR
ESQEEDSQSL VGNSAAAPSE PQPPVNNDAA LSLTQVELEE DMQQIRELMN RTNQDLASVT
KALLKTSGDF SAALDLLLDP SSISGPFWNR RDDSLLLSAD PVVLLHLQEK YSEEEVAKRI
VFLEVER
//
