ID A0A3B4YAY0_SERLL Unreviewed; 667 AA.
AC A0A3B4YAY0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, 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 Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000020284.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000020284.1}
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 AlphaFoldDB; A0A3B4YAY0; -.
DR STRING; 1841481.ENSSLDP00000020284; -.
DR Ensembl; ENSSLDT00000020957.1; ENSSLDP00000020284.1; ENSSLDG00000015857.1.
DR GeneTree; ENSGT00390000005351; -.
DR OrthoDB; 2920206at2759; -.
DR Proteomes; UP000261360; 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; 1.10.10.60; 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 185..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 575..602
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 185..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..226
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 279..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 667 AA; 73289 MW; 44879D074DF6FA1F CRC64;
MPLKEEDVAK SNISSVLFMT AEGEPMSFFL RPGLVKSKLQ PLITSGGGML CNVQQPGAIL
LIDPEERGSL RETTAHWYVS TQYIYDCIEK EERLNIEEYR LNPEVVPRHS ARLFNNYKEG
FFKLLGGRAA YTPEEDAAIL NYVSNHKSET GGNRLWQAME KQCVTSHSWQ SMKYRYKVQL
AKKKPEVEKV KTAEGEIKEA GSQETDVQKS PNEDAASPQK HSASTDLTQI DTQLLPAEST
QPENVEAETS NSPQPGEPCL DPQTDAHPIP AESPEPARAE PQTTVSPQKE SAPEDSLQSL
PNTPTPKNTK QPKQRASPEL EQPQRRLTRT HLELELSSSP QPYSKKLRSS STSPEKLSSS
PQPVNNTKSA VKLAAQKHTA TDPPPSKRAR GKSVAPVAES RQEESEEAAV SEIQQTDEES
TSSPQKAEKK KEKRKLGILE LATKEFEDES ESAEDEAPDL RNPTETAAIQ PTSTEPLSSV
TAADPASTQS NPEPGPSLQG KAQLTQSPSS NRVPETGCPE PAASEAVHAA SRPHLFIFDR
ESQEEDSQSL DGNSAAALSE PQPPVNKDAA LSLTQVALEE DMQQIRELMN RTNQDLASVT
KALLKTSGDF SAALDLLLDP SSISGPFWNR RDDSLLLSAD PVVLLHLQEK YSEEEVAKRI
VFLEVER
//
