TERB1_MOUSE
ID TERB1_MOUSE Reviewed; 768 AA.
AC Q8C0V1; A1L2Z9; E9QPF2; Q14CI1; Q8C0N5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Telomere repeats-binding bouquet formation protein 1 {ECO:0000303|PubMed:24413433};
DE AltName: Full=Coiled-coil domain-containing protein 79;
GN Name=Terb1 {ECO:0000303|PubMed:24413433};
GN Synonyms=Ccdc79 {ECO:0000312|MGI:MGI:2443187};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=24885367; DOI=10.1186/1471-2121-15-17;
RA Daniel K., Traenkner D., Wojtasz L., Shibuya H., Watanabe Y., Alsheimer M.,
RA Toth A.;
RT "Mouse CCDC79 (TERB1) is a meiosis-specific telomere associated protein.";
RL BMC Cell Biol. 15:17-17(2014).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, PHOSPHORYLATION AT
RP THR-648, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF THR-648,
RP AND INTERACTION WITH TERF1; STAG3 AND SUN1.
RX PubMed=24413433; DOI=10.1038/ncb2896;
RA Shibuya H., Ishiguro K.I., Watanabe Y.;
RT "The TRF1-binding protein TERB1 promotes chromosome movement and telomere
RT rigidity in meiosis.";
RL Nat. Cell Biol. 16:145-156(2014).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE MAJIN-TERB1-TERB2
RP COMPLEX, PHOSPHORYLATION AT THR-648, AND MUTAGENESIS OF THR-648.
RX PubMed=26548954; DOI=10.1016/j.cell.2015.10.030;
RA Shibuya H., Hernandez-Hernandez A., Morimoto A., Negishi L., Hoeoeg C.,
RA Watanabe Y.;
RT "MAJIN links telomeric DNA to the nuclear membrane by exchanging telomere
RT cap.";
RL Cell 163:1252-1266(2015).
RN [7]
RP STRUCTURE BY NMR OF 712-764.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structures of the myb-like DNA binding domain of 4930532d21rik
RT protein.";
RL Submitted (NOV-2005) to the PDB data bank.
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 (PubMed:24885367,
CC PubMed:24413433, PubMed:26548954). Component of the MAJIN-TERB1-TERB2
CC complex, which promotes telomere cap exchange by mediating attachment
CC of telomeric DNA to the inner nuclear membrane and replacement of the
CC protective cap of telomeric chromosomes: in early meiosis, the MAJIN-
CC TERB1-TERB2 complex associates with telomeric DNA and the
CC shelterin/telosome complex. During prophase, the complex matures and
CC promotes release of the shelterin/telosome complex from telomeric DNA
CC (PubMed:26548954). In the MAJIN-TERB1-TERB2 complex, TERB1 probably
CC mediates association with the shelterin/telosome complex via
CC interaction with TERF1, promoting priming telomeric DNA attachment'
CC (PubMed:26548954). Promotes telomere association with the nuclear
CC envelope and deposition of the SUN-KASH/LINC complex (PubMed:24885367,
CC PubMed:24413433). Also recruits cohesin to telomeres to develop
CC structural rigidity (PubMed:24413433). {ECO:0000269|PubMed:24413433,
CC ECO:0000269|PubMed:26548954, ECO:0000305|PubMed:24885367}.
CC -!- SUBUNIT: Component of the MAJIN-TERB1-TERB2 complex, composed of MAJIN,
CC TERB1 and TERB2 (PubMed:26548954). Interacts with TERF1, STAG3 and SUN1
CC (PubMed:24413433). Interacts (via Myb-like domain) with the cohesin
CC complex; probably mediated via interaction with STAG3
CC (PubMed:24413433). {ECO:0000269|PubMed:24413433,
CC ECO:0000269|PubMed:26548954}.
CC -!- INTERACTION:
CC Q8C0V1; Q9D666: Sun1; NbExp=2; IntAct=EBI-11707325, EBI-6752574;
CC Q8C0V1-1; P70371: Terf1; NbExp=4; IntAct=EBI-16089839, EBI-6919183;
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000269|PubMed:24413433, ECO:0000269|PubMed:24885367}. Nucleus
CC inner membrane {ECO:0000269|PubMed:26548954}. Note=Localizes to
CC telomeres during meiotic prophase (PubMed:24413433). In leptotene
CC spermatocytes, localizes to telomeres that localize to the nucleus
CC inner membrane (PubMed:26548954). {ECO:0000269|PubMed:24413433,
CC ECO:0000269|PubMed:26548954}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8C0V1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C0V1-2; Sequence=VSP_031617, VSP_031623;
CC Name=3;
CC IsoId=Q8C0V1-3; Sequence=VSP_031616, VSP_031618, VSP_031620,
CC VSP_031622;
CC Name=4;
CC IsoId=Q8C0V1-4; Sequence=VSP_031616, VSP_031618, VSP_031619,
CC VSP_031621;
CC -!- TISSUE SPECIFICITY: Expressed in testis and fetal oocytes.
CC {ECO:0000269|PubMed:24413433}.
CC -!- DEVELOPMENTAL STAGE: Expressed during meiotic prophase and becomes
CC undetectable in metaphase I in spermatocytes and oocytes (at protein
CC level). {ECO:0000269|PubMed:24413433, ECO:0000269|PubMed:24885367}.
CC -!- PTM: Phosphorylated by CDK (PubMed:24413433, PubMed:26548954).
CC Phosphorylation by CDK takes place in late prophase when the cap
CC exchange is prominent (PubMed:26548954). is important for the
CC stabilization of telomere attachment but dispenable for the cap
CC exchange (PubMed:26548954). {ECO:0000269|PubMed:24413433,
CC ECO:0000269|PubMed:26548954}.
CC -!- DISRUPTION PHENOTYPE: Mice develop normally, exhibit no overt
CC phenotype, but are infertile (both males and females). Testis lack
CC postmeiotic cells due to massive elimination of spermatocytes, while
CC females show degeneration of the ovaries, lacking growing follicles and
CC mature oocytes. {ECO:0000269|PubMed:24413433}.
CC -!- SIMILARITY: Belongs to the TERB1 family. {ECO:0000305}.
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DR EMBL; AK029754; BAC26599.1; -; mRNA.
DR EMBL; AK030157; BAC26814.1; -; mRNA.
DR EMBL; AC130543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC113771; AAI13772.1; -; mRNA.
DR EMBL; BC129814; AAI29815.1; -; mRNA.
DR CCDS; CCDS22580.1; -. [Q8C0V1-1]
DR RefSeq; NP_851289.2; NM_180958.3. [Q8C0V1-1]
DR RefSeq; XP_006531157.1; XM_006531094.2. [Q8C0V1-1]
DR RefSeq; XP_017168345.1; XM_017312856.1. [Q8C0V1-1]
DR PDB; 1X58; NMR; -; A=712-760.
DR PDBsum; 1X58; -.
DR AlphaFoldDB; Q8C0V1; -.
DR SMR; Q8C0V1; -.
DR DIP; DIP-60728N; -.
DR IntAct; Q8C0V1; 8.
DR STRING; 10090.ENSMUSP00000067324; -.
DR iPTMnet; Q8C0V1; -.
DR PhosphoSitePlus; Q8C0V1; -.
DR jPOST; Q8C0V1; -.
DR PaxDb; Q8C0V1; -.
DR PRIDE; Q8C0V1; -.
DR ProteomicsDB; 262753; -. [Q8C0V1-1]
DR ProteomicsDB; 262754; -. [Q8C0V1-2]
DR ProteomicsDB; 262755; -. [Q8C0V1-3]
DR ProteomicsDB; 262756; -. [Q8C0V1-4]
DR Antibodypedia; 72088; 47 antibodies from 9 providers.
DR DNASU; 320022; -.
DR Ensembl; ENSMUST00000064576; ENSMUSP00000067324; ENSMUSG00000052616. [Q8C0V1-1]
DR GeneID; 320022; -.
DR KEGG; mmu:320022; -.
DR UCSC; uc009naq.1; mouse. [Q8C0V1-1]
DR UCSC; uc009nar.1; mouse. [Q8C0V1-2]
DR CTD; 283847; -.
DR MGI; MGI:2443187; Terb1.
DR VEuPathDB; HostDB:ENSMUSG00000052616; -.
DR eggNOG; ENOG502QQER; Eukaryota.
DR GeneTree; ENSGT00390000005075; -.
DR InParanoid; Q8C0V1; -.
DR OMA; RENCQDN; -.
DR OrthoDB; 196162at2759; -.
DR PhylomeDB; Q8C0V1; -.
DR TreeFam; TF335845; -.
DR BioGRID-ORCS; 320022; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Terb1; mouse.
DR EvolutionaryTrace; Q8C0V1; -.
DR PRO; PR:Q8C0V1; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8C0V1; protein.
DR Bgee; ENSMUSG00000052616; Expressed in spermatocyte and 49 other tissues.
DR ExpressionAtlas; Q8C0V1; baseline and differential.
DR Genevisible; Q8C0V1; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:UniProtKB.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:UniProtKB.
DR GO; GO:0070197; P:meiotic attachment of telomere to nuclear envelope; IMP:UniProtKB.
DR GO; GO:0045141; P:meiotic telomere clustering; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
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.
DR PROSITE; PS50176; ARM_REPEAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; Coiled coil; Meiosis;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Repeat; Telomere.
FT CHAIN 1..768
FT /note="Telomere repeats-binding bouquet formation protein
FT 1"
FT /id="PRO_0000320157"
FT REPEAT 101..145
FT /note="ARM 1"
FT REPEAT 341..384
FT /note="ARM 2"
FT DOMAIN 707..760
FT /note="Myb-like"
FT REGION 422..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..700
FT /note="Interaction with TERF1"
FT /evidence="ECO:0000269|PubMed:24413433"
FT COILED 399..448
FT /evidence="ECO:0000255"
FT COMPBIAS 457..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 648
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:26548954,
FT ECO:0000305|PubMed:24413433"
FT VAR_SEQ 1..401
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031616"
FT VAR_SEQ 1..48
FT /note="MESEKPKKTQEMKTDLKLLLECLKYHMGNPLSQKEVLITIHSVCKQNS ->
FT MSEVSHGQPFVTKG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031617"
FT VAR_SEQ 402..424
FT /note="REHWKAAKEILCRIKQFEKGGKE -> MKVLIQEKNLASYLPLVTAQRIV
FT (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031618"
FT VAR_SEQ 594..650
FT /note="GCIVARKLLNSRNFSKFLHSCAYQCVHHKVIMEAEDKYKNELRKTFICAKKI
FT LLTPC -> VCLYSYVGGFSYIEPPLHLARARLARKNDAATGSFCTRLLGELDCRGEKT
FT SSPELVA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031619"
FT VAR_SEQ 644..651
FT /note="KILLTPCR -> SNSFSNFN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031620"
FT VAR_SEQ 651..768
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031621"
FT VAR_SEQ 652..768
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031622"
FT VAR_SEQ 707..768
FT /note="KKRRIRKDFTKEEVNYLFHGVKTMGNHWNSILWSFPFQKGRRAVDLAHKYHR
FT LIKGPSCAAL -> SEFEATPGYIGKAHLKKRKRKKKENLQTSFSMM (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031623"
FT MUTAGEN 648
FT /note="T->A: Telomere-attachment defects."
FT /evidence="ECO:0000269|PubMed:26548954"
FT MUTAGEN 648
FT /note="T->D: Mimics phosphorylation state; impairs
FT interaction with TERF1."
FT /evidence="ECO:0000269|PubMed:24413433"
FT CONFLICT 211
FT /note="L -> V (in Ref. 1; BAC26599)"
FT /evidence="ECO:0000305"
FT STRAND 712..714
FT /evidence="ECO:0007829|PDB:1X58"
FT HELIX 717..730
FT /evidence="ECO:0007829|PDB:1X58"
FT HELIX 734..740
FT /evidence="ECO:0007829|PDB:1X58"
FT HELIX 749..760
FT /evidence="ECO:0007829|PDB:1X58"
SQ SEQUENCE 768 AA; 86835 MW; EEA1F16E6258BFA6 CRC64;
MESEKPKKTQ EMKTDLKLLL ECLKYHMGNP LSQKEVLITI HSVCKQNSDA GIYFREIGGL
MFIINLAKSS EQSLVKEAAL YTLGSIAEEN VYCQQSLCTS ELFQDLTGLL TNDDSNTNLK
RMSVYVLLVL VSNNRNGQTL VREVGCIEVL SQMFRTVLSN YELNLSDNSV FQSYLLWSSV
CSTLCVCVNN PQNDENQMLC CSLFPCVNEW LMNCMRPEVI RPICSFIGLT LANNTHAQNC
FVSSGGLDVL CQVLVQLESD SHNTLSSAKL AVIVTKTMDA CITDNSAAFT VVLSKYHIVS
TLLALLLHES LDSREKFSII LAIGHCTEDC EKNQYELLKN NGLPLMIQAL TEFKNEDLSK
AATYVLHNCK KITGKLSLSL GQNSFGENEI ELKDISEKET LREHWKAAKE ILCRIKQFEK
GGKEEKQQNR SGHYKDNTPS MKVNIQTNLK RLCADSTGGT RAEDKDINQS RELRSYKPSE
IMSKACANEN QLTTRKKNTN PVHPFCKEKG QSKIVHETTP SCAQNLDKEK TFDQKDSVSQ
SSDQVLKHLP HTVKNRKQVP ETDPFTLCLD IIDREVGIQA TDSCSRMLKY TCSGCIVARK
LLNSRNFSKF LHSCAYQCVH HKVIMEAEDK YKNELRKTFI CAKKILLTPC RRRQLCKEST
ASEELKIVHQ KPDSKKLPGL EAQALNTSIP EAMERRSPVP GQSGLHKKRR IRKDFTKEEV
NYLFHGVKTM GNHWNSILWS FPFQKGRRAV DLAHKYHRLI KGPSCAAL
