TCAB1_MESAU
ID TCAB1_MESAU Reviewed; 538 AA.
AC Q60525;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Telomerase Cajal body protein 1 {ECO:0000250|UniProtKB:Q9BUR4};
DE AltName: Full=Guanine nucleotide-binding protein beta 5 {ECO:0000303|PubMed:7613025};
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:0000250|UniProtKB:Q9BUR4};
GN Synonyms=Gnb5 {ECO:0000303|PubMed:7613025},
GN Tcab1 {ECO:0000250|UniProtKB:Q9BUR4}, Wdr79 {ECO:0000250|UniProtKB:Q9BUR4};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=7613025; DOI=10.1007/bf00352407;
RA Albor A., Notario V.;
RT "The Gnb5 gene is a novel beta-transducin homolog transcribed from a
RT divergent promoter located immediately upstream of the Syrian hamster p53
RT P1 promoter.";
RL Mamm. Genome 6:236-241(1995).
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: relocalizes to sites of DNA double-strand breaks in
CC response to DNA damage and promotes the repair of DNA double-strand
CC breaks. Acts by recruiting the ubiquitin ligase RNF8 to DNA breaks and
CC promote both homologous recombination (HR) and non-homologous end
CC 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. {ECO:0000250|UniProtKB:Q9BUR4}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in testis.
CC {ECO:0000269|PubMed:7613025}.
CC -!- SIMILARITY: Belongs to the TCAB1 family. {ECO:0000305}.
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DR EMBL; U13152; AAA85261.1; -; mRNA.
DR RefSeq; NP_001268518.1; NM_001281589.1.
DR AlphaFoldDB; Q60525; -.
DR SMR; Q60525; -.
DR STRING; 10036.XP_005067607.1; -.
DR GeneID; 101834343; -.
DR CTD; 55135; -.
DR eggNOG; KOG2919; Eukaryota.
DR OrthoDB; 934297at2759; -.
DR Proteomes; UP000189706; Unplaced.
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; IEA:Ensembl.
DR GO; GO:0042393; F:histone binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
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; IEA:Ensembl.
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; IEA:Ensembl.
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; IEA:Ensembl.
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; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 4.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Chromosome; DNA damage; DNA repair; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Telomere; WD repeat.
FT CHAIN 1..538
FT /note="Telomerase Cajal body protein 1"
FT /id="PRO_0000367317"
FT REPEAT 154..194
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 210..255
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 260..301
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 311..352
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 353..393
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 399..438
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUR4"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUR4"
FT MOD_RES 478
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUR4"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUR4"
SQ SEQUENCE 538 AA; 58501 MW; EEA6C6955693E04E CRC64;
MKTSEERLVV PDSLSSDQAP APVPQGSPVD ENTDSEPVPQ PCGGDDRSQV AADSVAGSVV
FQEPQQGHPL PLSAPLEVEF NTPGELSPRI EEQELSENVS LPVEDTNQPE LASGEDVEGV
SEEPGPVDEG DAFWSYNFSQ VPRYLSGSWS EFRAHSENFL KGCKWAPDGS CILTNSADNT
LRIYNLPPEL YSATEQVDYA EMVPVLRMVE GDTIYDYCWY SLMSSSQPDT SYVASSSREN
PIHIWDAFTG ELRASFRAYN HLDELTAAHS LCFSPDGSQL FCGFNRTVRV FSTSRPGRDC
EVRATFAKKQ GQSGIISCIA FSPSQPLYAC GSYGRTLGLY AWDDGSPLAL LGGHQGGITH
LCFHPDGNLF FSGARKDAEL LCWDLRQPGH LLWSLSREVT TNQRIYFDLD PSGQFLVSGN
TNGMVSVWDI SGAFGDSSKL GPVMTFLPQK DCTNGVSLHP SLPLLATASG QRMFPEPTNS
GDEGEPEGDL PLLSLCHAHP EWQLQLWWCG GGPDPSSPND PQDEKGQGRA EGCGDGLI
