TERB1_DANRE
ID TERB1_DANRE Reviewed; 814 AA.
AC Q1LX29; A3KQ98;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Telomere repeats-binding bouquet formation protein 1 {ECO:0000250|UniProtKB:Q8C0V1};
DE AltName: Full=Coiled-coil domain-containing protein 79;
GN Name=ccdc79; Synonyms=terb1 {ECO:0000250|UniProtKB:Q8C0V1};
GN ORFNames=si:dkey-238c7.7, si:dkey-30c15.5;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
CC -!- FUNCTION: Meiosis-specific telomere-associated protein involved in
CC meiotic telomere attachment to the nucleus inner membrane, a crucial
CC step for homologous pairing and synapsis. Component of the MAJIN-TERB1-
CC TERB2 complex, which promotes telomere cap exchange by mediating
CC attachment of telomeric DNA to the inner nuclear membrane and
CC replacement of the protective cap of telomeric chromosomes: in early
CC meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA
CC and the shelterin/telosome complex. During prophase, the complex
CC matures and promotes release of the shelterin/telosome complex from
CC telomeric DNA. In the MAJIN-TERB1-TERB2 complex, TERB1 probably
CC mediates association with the shelterin/telosome complex.
CC {ECO:0000250|UniProtKB:Q8C0V1}.
CC -!- SUBUNIT: Component of the MAJIN-TERB1-TERB2 complex.
CC {ECO:0000250|UniProtKB:Q8C0V1}.
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000250|UniProtKB:Q8C0V1}. Nucleus inner membrane
CC {ECO:0000250|UniProtKB:Q8C0V1}. Note=Localizes to telomeres during
CC meiotic prophase. In leptotene spermatocytes, localizes to telomeres
CC that localize to the nucleus inner membrane.
CC {ECO:0000250|UniProtKB:Q8C0V1}.
CC -!- SIMILARITY: Belongs to the TERB1 family. {ECO:0000305}.
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DR EMBL; BX470218; CAK10982.2; -; Genomic_DNA.
DR EMBL; BX571879; CAM56625.1; -; Genomic_DNA.
DR RefSeq; NP_001082851.1; NM_001089382.1.
DR AlphaFoldDB; Q1LX29; -.
DR SMR; Q1LX29; -.
DR STRING; 7955.ENSDARP00000118262; -.
DR PaxDb; Q1LX29; -.
DR Ensembl; ENSDART00000081468; ENSDARP00000075909; ENSDARG00000058587.
DR Ensembl; ENSDART00000142270; ENSDARP00000118262; ENSDARG00000058587.
DR GeneID; 559140; -.
DR KEGG; dre:559140; -.
DR CTD; 283847; -.
DR ZFIN; ZDB-GENE-060503-732; terb1.
DR eggNOG; ENOG502QQER; Eukaryota.
DR GeneTree; ENSGT00390000005075; -.
DR HOGENOM; CLU_022991_1_0_1; -.
DR InParanoid; Q1LX29; -.
DR OMA; RENCQDN; -.
DR OrthoDB; 196162at2759; -.
DR PhylomeDB; Q1LX29; -.
DR TreeFam; TF335845; -.
DR PRO; PR:Q1LX29; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 18.
DR Bgee; ENSDARG00000058587; Expressed in testis and 7 other tissues.
DR ExpressionAtlas; Q1LX29; baseline.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0005637; C:nuclear inner membrane; ISS:UniProtKB.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; ISS:UniProtKB.
DR GO; GO:0070197; P:meiotic attachment of telomere to nuclear envelope; ISS:UniProtKB.
DR GO; GO:0045141; P:meiotic telomere clustering; ISS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR042359; TERB1.
DR PANTHER; PTHR14014; PTHR14014; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 3: Inferred from homology;
KW Chromosome; Coiled coil; Meiosis; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Telomere.
FT CHAIN 1..814
FT /note="Telomere repeats-binding bouquet formation protein
FT 1"
FT /id="PRO_0000320159"
FT REPEAT 93..136
FT /note="ARM 1"
FT REPEAT 327..368
FT /note="ARM 2"
FT DOMAIN 746..799
FT /note="Myb-like"
FT REGION 461..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 488..512
FT /evidence="ECO:0000255"
FT COMPBIAS 461..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 96
FT /note="R -> Q (in Ref. 1; CAM56625)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="S -> N (in Ref. 1; CAM56625)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="I -> T (in Ref. 1; CAM56625)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="T -> P (in Ref. 1; CAM56625)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="K -> E (in Ref. 1; CAM56625)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="F -> Y (in Ref. 1; CAM56625)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="T -> A (in Ref. 1; CAM56625)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="I -> N (in Ref. 1; CAM56625)"
FT /evidence="ECO:0000305"
FT CONFLICT 713
FT /note="R -> K (in Ref. 1; CAM56625)"
FT /evidence="ECO:0000305"
FT CONFLICT 723
FT /note="V -> M (in Ref. 1; CAM56625)"
FT /evidence="ECO:0000305"
FT CONFLICT 728
FT /note="D -> E (in Ref. 1; CAM56625)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="A -> T (in Ref. 1; CAM56625)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 814 AA; 92807 MW; 5DF0423DEFEDBE17 CRC64;
MEATKTDLRL LLECLKYQMK WPGSQKQALL TIISICKQND QYVEFLREIG GISFIYNLSK
SSTFSQVKET ALFTLASLAE LHESCKQALC REEMFRDFVQ HLEQEMPLTE KRVAVYMLSV
LVANNRCGQT LAKTSRCIEA LLRLFRQSFP VPGESYEQLQ LWITVSSALC GSVNNPQNEE
NQNVCMSVFP EIKPWLQEVA LPRAELAQPL CSFIGMTVAN NPCAQEYFVS VGGLDSLSDT
LTRVLSQSTH SASVCKMATI ITKTLSACIS NNELLGSSLS KLRVIPGLLR LLSSPNLDPQ
DQLAVVLTTG HLTDACVEQQ SQLLSAGGLP IIITLLTETS DEELKKAAIF VLHTCNRITE
SLGPGMSTID PNECDREGQW RSAGQILQRI QLLEKKIGKK LWERDPESQP HSMKRSDSHV
ECDDELWEGS VMRKVKGNHR VYGEFRAIPA GTPITSEILQ DQDSLQPDSS EEGLSPVQVN
LFKGPNWEKS KKRKHKQKRE NERSDNQETR REGVNKRELK RNVKSERVVK RLKMMNLESD
DDGYELLQNC STPTEGNRDT QGPDIFRHPD PVKRNQREPS LSDDNMSLCT ELLDKEINKF
LKPPSASKSN TLRCAGCVKH MNELNSRSFG AVLSSCRFQC DFHLTLREAE DRFRRSQPLK
RTSHTPTHTH INTHRKIREH STSAQEHKQK SKREKHKLSH QSSDRCYRLT PLRRPRETYS
PDVKQWTDHR HLKKSSEDAR SKNSSGRHRK RQNWSDKELC YLTKGVKRFG HSWNTILWKY
PFHPGRTNVD LAKKFYHMQK AKAQGVDLSV AKAL
