TCAB1_RAT
ID TCAB1_RAT Reviewed; 532 AA.
AC Q5XII5;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
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|RGD:1359624};
GN Synonyms=Tcab1 {ECO:0000250|UniProtKB:Q9BUR4},
GN Wdr79 {ECO:0000250|UniProtKB:Q9BUR4};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-476, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: RNA chaperone that plays a key role in telomere maintenance
CC and RNA localization to Cajal bodies. Specifically recognizes and binds
CC the Cajal body box (CAB box) present in both small Cajal body RNAs
CC (scaRNAs) and telomerase RNA template component (TERC). Essential
CC component of the telomerase holoenzyme complex, a ribonucleoprotein
CC complex essential for the replication of chromosome termini that
CC elongates telomeres in most eukaryotes. In the telomerase holoenzyme
CC complex, required to stimulate the catalytic activity of the complex.
CC Acts by specifically binding the CAB box of the TERC RNA and
CC controlling the folding of the CR4/CR5 region of the TERC RNA, a
CC critical step for telomerase activity. In addition, also controls
CC telomerase holoenzyme complex localization to Cajal body. During S
CC phase, required for delivery of TERC to telomeres during S phase and
CC for telomerase activity. In addition to its role in telomere
CC maintenance, also required for Cajal body formation, probably by
CC mediating localization of scaRNAs to Cajal bodies. Also plays a role in
CC DNA repair: phosphorylated by ATM in response to DNA damage and
CC relocalizes to sites of DNA double-strand breaks to promote the repair
CC of DNA double-strand breaks. Acts by recruiting the ubiquitin ligase
CC RNF8 to DNA breaks and promote both homologous recombination (HR) and
CC non-homologous end joining (NHEJ). {ECO:0000250|UniProtKB:Q9BUR4}.
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; BC083696; AAH83696.1; -; mRNA.
DR RefSeq; NP_001007611.1; NM_001007610.1.
DR AlphaFoldDB; Q5XII5; -.
DR SMR; Q5XII5; -.
DR STRING; 10116.ENSRNOP00000014261; -.
DR iPTMnet; Q5XII5; -.
DR PhosphoSitePlus; Q5XII5; -.
DR PaxDb; Q5XII5; -.
DR Ensembl; ENSRNOT00000014261; ENSRNOP00000014261; ENSRNOG00000010520.
DR GeneID; 287432; -.
DR KEGG; rno:287432; -.
DR UCSC; RGD:1359624; rat.
DR CTD; 55135; -.
DR RGD; 1359624; Wrap53.
DR eggNOG; KOG2919; Eukaryota.
DR GeneTree; ENSGT00390000010169; -.
DR HOGENOM; CLU_022731_1_1_1; -.
DR InParanoid; Q5XII5; -.
DR OMA; FTKGCQW; -.
DR OrthoDB; 934297at2759; -.
DR PhylomeDB; Q5XII5; -.
DR TreeFam; TF315169; -.
DR Reactome; R-RNO-171319; Telomere Extension By Telomerase.
DR PRO; PR:Q5XII5; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000010520; Expressed in thymus and 20 other tissues.
DR Genevisible; Q5XII5; RN.
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; IEA:Ensembl.
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:RGD.
DR GO; GO:0042393; F:histone binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
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:RGD.
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:RGD.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISS: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:RGD.
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_0000242698"
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..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
SQ SEQUENCE 532 AA; 58195 MW; 5A0A44F0CB08D84D CRC64;
MKTSEELRLA PDSLPSDLVP APVLQASPAD KNTDSEPVPP PCGGDDQLQV ATDAVASSVV
SQELQQGDSA PLEVEFNISS ELSPRIEEQE VPENASLPVE ETNRPELESG EAMEGVSEEP
AAVDEGDIFW SYSFSQVPQY LSGSWSEFST RSENFLKGCK WAPDGSCILT NSADNVLRIY
NLPPELYSES EQVDYAEMVP VLRMVEGDTI YDYCWYSLMS STQPDTSYVA SSSRENPIHI
WDAFTGELRA SFRAYNHLDE LTAAHSLCFS PDGSQLFCGF NRTVRVFSTS RPGRDCEVRT
TFAKKQGQSG IISCLAFSPA QPLYACGSYG RTLGLYAWDD GSPLALLGGH QGGITHLCFH
PDGNLFFSGA RKDAELLCWD LRQPGHLLWS LSREVTTNQR IYFDLDPSGQ FLVSGNTSGV
VSVWDISGAF SDCKQLEPVM TFLPQDDCTN GVSLHPTLPL LATASGQRMF PEPTNSGDEG
EPELDLPLLS LRHAHPECQL QLWWCGGGPD PSNPDEDQDE KGQGRTEAVG MS
