TCAB1_MOUSE
ID TCAB1_MOUSE Reviewed; 532 AA.
AC Q8VC51;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Telomerase Cajal body protein 1 {ECO:0000250|UniProtKB:Q9BUR4};
DE AltName: Full=WD repeat-containing protein 79 {ECO:0000250|UniProtKB:Q9BUR4};
DE AltName: Full=WD40 repeat-containing protein antisense to TP53 gene homolog {ECO:0000250|UniProtKB:Q9BUR4};
GN Name=Wrap53 {ECO:0000312|MGI:MGI:2384933};
GN Synonyms=Tcab1 {ECO:0000250|UniProtKB:Q9BUR4},
GN Wdr79 {ECO:0000250|UniProtKB:Q9BUR4};
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney, and Liver;
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 [3]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=29804836; DOI=10.1016/j.cell.2018.04.039;
RA Chen L., Roake C.M., Freund A., Batista P.J., Tian S., Yin Y.A.,
RA Gajera C.R., Lin S., Lee B., Pech M.F., Venteicher A.S., Das R.,
RA Chang H.Y., Artandi S.E.;
RT "An Activity Switch in Human Telomerase Based on RNA Conformation and
RT Shaped by TCAB1.";
RL Cell 0:0-0(2018).
CC -!- FUNCTION: RNA chaperone that plays a key role in telomere maintenance
CC and RNA localization to Cajal bodies (PubMed:29804836). Specifically
CC recognizes and binds the Cajal body box (CAB box) present in both small
CC Cajal body RNAs (scaRNAs) and telomerase RNA template component (TERC)
CC (PubMed:29804836). Essential component of the telomerase holoenzyme
CC complex, a ribonucleoprotein complex essential for the replication of
CC chromosome termini that elongates telomeres in most eukaryotes (By
CC similarity). In the telomerase holoenzyme complex, required to
CC stimulate the catalytic activity of the complex (PubMed:29804836). Acts
CC by specifically binding the CAB box of the TERC RNA and controlling the
CC folding of the CR4/CR5 region of the TERC RNA, a critical step for
CC telomerase activity (By similarity). In addition, also controls
CC telomerase holoenzyme complex localization to Cajal body (By
CC similarity). During S phase, required for delivery of TERC to telomeres
CC during S phase and for telomerase activity (By similarity). In addition
CC to its role in telomere maintenance, also required for Cajal body
CC formation, probably by mediating localization of scaRNAs to Cajal
CC bodies (By similarity). Also plays a role in DNA repair: phosphorylated
CC by ATM in response to DNA damage and relocalizes to sites of DNA
CC double-strand breaks to promote the repair of DNA double-strand breaks
CC (By similarity). Acts by recruiting the ubiquitin ligase RNF8 to DNA
CC breaks and promote both homologous recombination (HR) and non-
CC homologous end joining (NHEJ) (By similarity).
CC {ECO:0000250|UniProtKB:Q9BUR4, ECO:0000269|PubMed:29804836}.
CC -!- SUBUNIT: Component of the telomerase holoenzyme complex composed of one
CC molecule of TERT, one molecule of WRAP53/TCAB1, two molecules of H/ACA
CC ribonucleoprotein complex subunits DKC1, NOP10, NHP2 and GAR1, and a
CC telomerase RNA template component (TERC). The telomerase holoenzyme
CC complex is associated with TEP1, SMG6/EST1A and POT1. Interacts with
CC the chaperonin-containing T-complex (TRiC) complex; which mediates the
CC folding of WRAP53/TCAB1. Interacts with COIL. Interacts with SMN1.
CC Interacts with RNF8. Interacts with histone H2AX.
CC {ECO:0000250|UniProtKB:Q9BUR4}.
CC -!- SUBCELLULAR LOCATION: Nucleus, Cajal body
CC {ECO:0000250|UniProtKB:Q9BUR4}. Chromosome, telomere
CC {ECO:0000250|UniProtKB:Q9BUR4}. Chromosome
CC {ECO:0000250|UniProtKB:Q9BUR4}. Note=Released from telomerase RNA
CC template component (TERC) in mitotic cells coincident with
CC delocalization from Cajal bodies. In response to DNA damage, localizes
CC to sites of DNA double-strand breaks following phosphorylation by ATM.
CC {ECO:0000250|UniProtKB:Q9BUR4}.
CC -!- PTM: Phosphorylated at Ser-61 by ATM in response to DNA damage,
CC promoting its interaction with histone H2AX and localization to sites
CC of DNA double-strand breaks. {ECO:0000250|UniProtKB:Q9BUR4}.
CC -!- SIMILARITY: Belongs to the TCAB1 family. {ECO:0000305}.
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DR EMBL; AL731687; CAI52013.1; -; Genomic_DNA.
DR EMBL; BC021790; AAH21790.1; -; mRNA.
DR EMBL; BC069868; AAH69868.1; -; mRNA.
DR CCDS; CCDS24897.1; -.
DR RefSeq; NP_659073.1; NM_144824.2.
DR AlphaFoldDB; Q8VC51; -.
DR SMR; Q8VC51; -.
DR STRING; 10090.ENSMUSP00000047825; -.
DR iPTMnet; Q8VC51; -.
DR PhosphoSitePlus; Q8VC51; -.
DR EPD; Q8VC51; -.
DR jPOST; Q8VC51; -.
DR MaxQB; Q8VC51; -.
DR PaxDb; Q8VC51; -.
DR PeptideAtlas; Q8VC51; -.
DR PRIDE; Q8VC51; -.
DR ProteomicsDB; 297838; -.
DR Antibodypedia; 24336; 80 antibodies from 23 providers.
DR DNASU; 216853; -.
DR Ensembl; ENSMUST00000048139; ENSMUSP00000047825; ENSMUSG00000041346.
DR GeneID; 216853; -.
DR KEGG; mmu:216853; -.
DR UCSC; uc007jqj.1; mouse.
DR CTD; 55135; -.
DR MGI; MGI:2384933; Wrap53.
DR VEuPathDB; HostDB:ENSMUSG00000041346; -.
DR eggNOG; KOG2919; Eukaryota.
DR GeneTree; ENSGT00390000010169; -.
DR HOGENOM; CLU_022731_1_1_1; -.
DR InParanoid; Q8VC51; -.
DR OMA; FTKGCQW; -.
DR OrthoDB; 934297at2759; -.
DR PhylomeDB; Q8VC51; -.
DR TreeFam; TF315169; -.
DR Reactome; R-MMU-171319; Telomere Extension By Telomerase.
DR BioGRID-ORCS; 216853; 26 hits in 76 CRISPR screens.
DR ChiTaRS; Wrap53; mouse.
DR PRO; PR:Q8VC51; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8VC51; protein.
DR Bgee; ENSMUSG00000041346; Expressed in blastocyst and 183 other tissues.
DR ExpressionAtlas; Q8VC51; baseline and differential.
DR Genevisible; Q8VC51; MM.
DR GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0005697; C:telomerase holoenzyme complex; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0070034; F:telomerase RNA binding; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0030576; P:Cajal body organization; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; ISS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:1904851; P:positive regulation of establishment of protein localization to telomere; ISO:MGI.
DR GO; GO:0051973; P:positive regulation of telomerase activity; IDA:UniProtKB.
DR GO; GO:1904867; P:protein localization to Cajal body; ISS:UniProtKB.
DR GO; GO:0034337; P:RNA folding; ISS:UniProtKB.
DR GO; GO:0090666; P:scaRNA localization to Cajal body; ISS:UniProtKB.
DR GO; GO:0090671; P:telomerase RNA localization to Cajal body; ISO:MGI.
DR GO; GO:0032203; P:telomere formation via telomerase; ISS:UniProtKB.
DR GO; GO:0007004; P:telomere maintenance via telomerase; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Chaperone; Chromosome; DNA damage; DNA repair; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Telomere; WD repeat.
FT CHAIN 1..532
FT /note="Telomerase Cajal body protein 1"
FT /id="PRO_0000242697"
FT REPEAT 151..190
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 206..251
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 256..297
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 307..348
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 349..389
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 395..434
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUR4"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUR4"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUR4"
FT MOD_RES 474
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUR4"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUR4"
SQ SEQUENCE 532 AA; 58151 MW; 928FE02E7D74D235 CRC64;
MKTSEERLLA PDSLPPDLAP APVPQGSPAE KNTDFEPVPP PCGGDDQPQL ATDPVASLVV
SQELQQGDSV PLEVEFNTSS ELSPGIEEQD VSEHASLPGE ETNLPELESG EATEGVSEER
AEVDEGDTFW TYSFSQVPRY LSGSWSEFST RSENFLKGCK WAPDGSCILT NSADNVLRIY
NLPPELYSEQ EQVDYAEMVP VLRMVEGDTI YDYCWYSLMS STQPDTSYVA SSSRENPIHI
WDAFTGELRA SFRAYNHLDE LTAAHSLCFS PDGSQLFCGF NRTVRVFSTS RPGRDCEVRA
TFAKKQGQSG IISCIAFSPS QPLYACGSYG RTIGLYAWDD GSPLALLGGH QGGITHLCFH
PDGNLFFSGA RKDAELLCWD LRQPGHLLWS LSREVTTNQR IYFDLDPSGQ FLVSGNTSGV
VSVWDISGAL SDDSKLEPVV TFLPQKDCTN GVSLHPTLPL LATASGQRVF PEPTNSGDEG
ELELELPLLS LCHAHPECQL QLWWCGGGPD PSSPVDDQDE KGQRRTEAVG MS
