TCAB1_BOVIN
ID TCAB1_BOVIN Reviewed; 540 AA.
AC Q3SWZ7;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
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:0000250|UniProtKB:Q9BUR4};
GN Synonyms=TCAB1 {ECO:0000250|UniProtKB:Q9BUR4},
GN WDR79 {ECO:0000250|UniProtKB:Q9BUR4};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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-64 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; BC104583; AAI04584.1; -; mRNA.
DR RefSeq; NP_001030245.1; NM_001035073.1.
DR AlphaFoldDB; Q3SWZ7; -.
DR SMR; Q3SWZ7; -.
DR STRING; 9913.ENSBTAP00000001421; -.
DR PaxDb; Q3SWZ7; -.
DR GeneID; 509631; -.
DR KEGG; bta:509631; -.
DR CTD; 55135; -.
DR eggNOG; KOG2919; Eukaryota.
DR InParanoid; Q3SWZ7; -.
DR OrthoDB; 934297at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
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:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0070034; F:telomerase RNA binding; ISS:UniProtKB.
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: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: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; 3.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 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..540
FT /note="Telomerase Cajal body protein 1"
FT /id="PRO_0000242695"
FT REPEAT 158..197
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 213..258
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 263..304
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 314..355
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 356..396
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 402..441
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUR4"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUR4"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUR4"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUR4"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUR4"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUR4"
FT MOD_RES 480
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUR4"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUR4"
SQ SEQUENCE 540 AA; 59108 MW; 1353CB00638AE959 CRC64;
MKTPEAPPLA PDCLPSDQAP APARLSRQAS PMDKNTDPEL MPTPRDGDDP PQVSSDPMVG
LALSQELEEG VPASLPTPLE SGFGSPSELS SRVEEKELSE NVSLPAEETN RPELGPGEDV
EGVSEELTPE DEGYTIWNYN FSQVPRFLSG SWSEFITQPE NFLKGCKWAP DGSCILTNSA
DNILRIYNLP PELYNEGEQL EYAEMAPVLR MVEGDTIYDY CWYSLMSSAQ PDTSYVASSS
RENPIHIWDA FTGELRASFR SYNHLDELTA AHSLCFSPDG SQLFCGFNRT VRVFSTSRPG
RDCEVRTTFA KRQGQSGIIS CIAFSPTQPL YACGSYGRSL GLYTWEDGSP LALLGGHQGG
ITHLCFHPDG NCFFSGARKD AELLCWDLRQ LGHPLWSLSR EVTTNQRIYF DLDPTGQFLV
SGSTSGAVSV WDTGGAGLES KPEPVLSFQP QKDCTNGVSL HPSLPLLATA SGQRVFPEPT
ESGDEREEEV DLPLLSMRHV HLECQLQLWW CGGGPDTSIS DAHQEEMGQG RTEGGGGEFT
