TERF2_CHICK
ID TERF2_CHICK Reviewed; 718 AA.
AC Q9PU53;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Telomeric repeat-binding factor 2;
DE AltName: Full=TTAGGG repeat-binding factor 2;
DE AltName: Full=Telomeric DNA-binding protein;
GN Name=TERF2; Synonyms=TRF2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-718, AND VARIANT VAL-438.
RC STRAIN=White leghorn; TISSUE=Embryo;
RX PubMed=10571037; DOI=10.1016/s0378-1119(99)00374-1;
RA Konrad J.P., Mills W., Easty D.J., Farr C.J.;
RT "Cloning and characterisation of the chicken gene encoding the telomeric
RT protein TRF2.";
RL Gene 239:81-90(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-132.
RA Boardman P.E., Bonfield J.K., Brown W.R.A., Carder C., Chalk S.E.,
RA Croning M.D.R., Davies R.M., Francis M.D., Grafham D.V., Hubbard S.J.,
RA Humphray S.J., Hunt P.J., Maddison M., McLaren S.R., Niblett D.,
RA Overton I.M., Rogers J., Scott C.E., Taylor R.G., Tickle C., Wilson S.A.;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH TERF2IP.
RX PubMed=14659874; DOI=10.1016/j.gene.2003.08.026;
RA Tan M., Wei C., Price C.M.;
RT "The telomeric protein Rap1 is conserved in vertebrates and is expressed
RT from a bidirectional promoter positioned between the Rap1 and KARS genes.";
RL Gene 323:1-10(2003).
CC -!- FUNCTION: Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and
CC plays a central role in telomere maintenance and protection against
CC end-to-end fusion of chromosomes. Component of the shelterin complex
CC (telosome) that is involved in the regulation of telomere length and
CC protection. Shelterin associates with arrays of double-stranded 5'-
CC TTAGGG-3' repeats added by telomerase and protects chromosome ends;
CC without its protective activity, telomeres are no longer hidden from
CC the DNA damage surveillance and chromosome ends are inappropriately
CC processed by DNA repair pathways (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Component of the shelterin complex (telosome) (By
CC similarity). Interacts with TERF2IP/RAP1. {ECO:0000250,
CC ECO:0000269|PubMed:14659874}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC Chromosome, telomere {ECO:0000250}. Note=Colocalizes with telomeric DNA
CC in interphase cells and is located at chromosome ends during metaphase.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in embryo.
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DR EMBL; AJ133783; CAB56220.1; -; mRNA.
DR EMBL; CR406218; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001258821.1; NM_001271892.1.
DR AlphaFoldDB; Q9PU53; -.
DR SMR; Q9PU53; -.
DR BioGRID; 675877; 1.
DR STRING; 9031.ENSGALP00000000930; -.
DR PaxDb; Q9PU53; -.
DR PRIDE; Q9PU53; -.
DR GeneID; 395598; -.
DR KEGG; gga:395598; -.
DR CTD; 7014; -.
DR VEuPathDB; HostDB:geneid_395598; -.
DR eggNOG; ENOG502RYHN; Eukaryota.
DR InParanoid; Q9PU53; -.
DR OrthoDB; 605826at2759; -.
DR PhylomeDB; Q9PU53; -.
DR Reactome; R-GGA-418124; Telomere maintenance.
DR PRO; PR:Q9PU53; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0042162; F:telomeric DNA binding; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0031848; P:protection from non-homologous end joining at telomere; IEA:InterPro.
DR GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB.
DR CDD; cd11654; TRF2_RBM; 1.
DR Gene3D; 1.25.40.210; -; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR013867; Telomere_rpt-bd_fac_dimer_dom.
DR InterPro; IPR036507; Telomere_rpt-bd_fac_dimer_sf.
DR InterPro; IPR030657; TERF2.
DR InterPro; IPR031902; TERF2_RBM.
DR PANTHER; PTHR46833; PTHR46833; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF16772; TERF2_RBM; 1.
DR Pfam; PF08558; TRF; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF63600; SSF63600; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Chromosome; DNA-binding; Nucleus; Reference proteome; Repeat;
KW Telomere.
FT CHAIN 1..718
FT /note="Telomeric repeat-binding factor 2"
FT /id="PRO_0000197133"
FT REPEAT 257..269
FT /note="1"
FT REPEAT 270..282
FT /note="2"
FT REPEAT 283..295
FT /note="3"
FT REPEAT 296..308
FT /note="4"
FT REPEAT 309..321
FT /note="5"
FT REPEAT 322..334
FT /note="6"
FT REPEAT 335..347
FT /note="7"
FT REPEAT 348..360
FT /note="8"
FT REPEAT 361..373
FT /note="9"
FT REPEAT 374..386
FT /note="10"
FT REPEAT 387..399
FT /note="11"
FT REPEAT 400..412
FT /note="12"
FT REPEAT 413..425
FT /note="13"
FT REPEAT 426..438
FT /note="14"
FT REPEAT 439..451
FT /note="15"
FT DOMAIN 664..717
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 688..713
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 24..220
FT /note="TRFH dimerization"
FT REGION 219..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..451
FT /note="15 X 13 AA approximate tandem repeats"
FT REGION 342..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 545..550
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 237..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 438
FT /note="A -> V"
FT /evidence="ECO:0000269|PubMed:10571037"
FT CONFLICT 128..162
FT /note="IHKVLKEAAVIVCIKNKEFSKALAVLKRHMEKDTG -> LHSLWFQETEMDS
FT TGKRVDQRRSEEVWRREVEDHF (in Ref. 2; CR406218)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 718 AA; 80163 MW; DD61F253A6912551 CRC64;
MAAKRSRAAM EEQEKTSTRS DDREQAVNRW VLQFYFHQAV AAYRAGRNRD FRQLRDVMQA
LLVRPLEREP AVAQMLRVMQ FLSRIEEGEN LDCTFDKETE LTPLESAIGI LQLIAKEFSV
PEKKIELIHK VLKEAAVIVC IKNKEFSKAL AVLKRHMEKD TGNQKKRTEL QTIIREKNRA
HPIIRDFSYV NFQQYMFQFL KTYVDTSEPL LVTMMKSLNS ERAEEPKRSS VTPESPSRTE
DQEEAYEPLR RVKHSVGTLR RAETAGGVAG APSCPEMAKD PTGAPEHVGT VKDAVRAPCP
AESTEDSQGT PRCAETARDV MGAPSPSEMT KDLLGAPKCT ETARDVVRAP SPAESTKDPV
GTPGHAETAR DVARAPSPAE TTKNLPGAPE CADTVKNTVR APSPAERRKD LVRAPKRAET
ARDVVRAPSP AERVKDTAGA SEPMKSASYP TASQPRIAAV KSSKVFSVPV EISEQPAAAA
PVHAGVSSRD LERTPFRTVT TYGISVLREA FKMLSNSPDS DALFNKLDET DLPSPQQMSP
SVSHRTKRRK EEKNQGSETL DSPEIPHKSK RLFTISKMIM DQGSQCSKSS ESPDSSQERV
VSSAYRPVQE LPDQPVSTKR SSQQRWNSSY GEERKDSWSD EDELFTDAAL TETSSNNSTV
YGSKKQKWTV QESEWIKDGV RKYGEGRWKT ISEKYPFQNR TSVQIKDRYR TMKKLGIA
