LARP7_EUPAE
ID LARP7_EUPAE Reviewed; 437 AA.
AC Q9GSF8;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=La-related protein 7 homolog {ECO:0000305};
DE AltName: Full=La ribonucleoprotein domain family member 7 homolog {ECO:0000305};
DE AltName: Full=Telomerase subunit p43 {ECO:0000303|PubMed:11080168};
OS Euplotes aediculatus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Hypotrichia; Euplotida; Euplotidae; Euplotes.
OX NCBI_TaxID=5940;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, RIBOSOMAL
RP FRAMESHIFTING, FUNCTION, RNA-BINDING, IDENTIFICATION IN THE TELOMERASE
RP HOLOENZYME COMPLEX, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=11080168; DOI=10.1093/emboj/19.22.6230;
RA Aigner S., Lingner J., Goodrich K.J., Grosshans C.A., Shevchenko A.,
RA Mann M., Cech T.R.;
RT "Euplotes telomerase contains an La motif protein produced by apparent
RT translational frameshifting.";
RL EMBO J. 19:6230-6239(2000).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=12741831; DOI=10.1021/bi034121y;
RA Aigner S., Postberg J., Lipps H.J., Cech T.R.;
RT "The Euplotes La motif protein p43 has properties of a telomerase-specific
RT subunit.";
RL Biochemistry 42:5736-5747(2003).
RN [3]
RP FUNCTION, RNA-BINDING, IDENTIFICATION IN THE TELOMERASE HOLOENZYME COMPLEX,
RP AND SUBCELLULAR LOCATION.
RX PubMed=12665556; DOI=10.1242/jcs.00351;
RA Moellenbeck M., Postberg J., Paeschke K., Rossbach M., Joensson F.,
RA Lipps H.J.;
RT "The telomerase-associated protein p43 is involved in anchoring telomerase
RT in the nucleus.";
RL J. Cell Sci. 116:1757-1761(2003).
RN [4]
RP FUNCTION.
RX PubMed=15208446; DOI=10.1261/rna.7400704;
RA Aigner S., Cech T.R.;
RT "The Euplotes telomerase subunit p43 stimulates enzymatic activity and
RT processivity in vitro.";
RL RNA 10:1108-1118(2004).
RN [5]
RP IDENTIFICATION OF THE XRRM DOMAIN.
RX PubMed=22705372; DOI=10.1016/j.molcel.2012.05.018;
RA Singh M., Wang Z., Koo B.K., Patel A., Cascio D., Collins K., Feigon J.;
RT "Structural basis for telomerase RNA recognition and RNP assembly by the
RT holoenzyme La family protein p65.";
RL Mol. Cell 47:16-26(2012).
CC -!- FUNCTION: RNA-binding protein required for assembly of the holoenzyme
CC telomerase ribonucleoprotein (RNP) complex (PubMed:11080168,
CC PubMed:12665556, PubMed:15208446). Specifically binds telomerase RNA
CC and promotes its assembly with catalytic subunit p123, thereby
CC stimulating enzymatic activity and processivity of p123
CC (PubMed:15208446). Telomerase is a ribonucleoprotein enzyme essential
CC that copies new telomeric repeats onto chromosome ends and functions to
CC maintain cell division (PubMed:11080168, PubMed:12665556).
CC {ECO:0000269|PubMed:11080168, ECO:0000269|PubMed:12665556,
CC ECO:0000269|PubMed:15208446}.
CC -!- SUBUNIT: Component of the telomerase holoenzyme complex composed
CC minimally of the catalytic subunit p123 and the telomerase RNA template
CC component. {ECO:0000269|PubMed:11080168, ECO:0000269|PubMed:12665556}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12665556,
CC ECO:0000269|PubMed:12741831}. Chromosome, telomere {ECO:0000305}.
CC Note=Localizes to the macronucleus. {ECO:0000269|PubMed:12665556,
CC ECO:0000269|PubMed:12741831}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=1;
CC Comment=A ribosomal frameshift occurs between the codons for Met-86
CC and Lys-88. {ECO:0000269|PubMed:11080168};
CC Name=1;
CC IsoId=Q9GSF8-1; Sequence=Displayed;
CC -!- PTM: The mature form of the protein is a protein of 43 kDa, which is
CC derived from a 51 kDa precursor by proteolytic cleavage.
CC {ECO:0000269|PubMed:11080168}.
CC -!- SIMILARITY: Belongs to the LARP7 family. {ECO:0000305}.
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DR EMBL; AF307939; AAG33619.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9GSF8; -.
DR SMR; Q9GSF8; -.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0031039; C:macronucleus; IDA:UniProtKB.
DR GO; GO:0005697; C:telomerase holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0070034; F:telomerase RNA binding; IDA:UniProtKB.
DR GO; GO:1904868; P:telomerase catalytic core complex assembly; IDA:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR006630; La_HTH.
DR InterPro; IPR014886; La_xRRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF05383; La; 1.
DR SMART; SM00715; LA; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50961; HTH_LA; 1.
DR PROSITE; PS51939; XRRM; 1.
PE 1: Evidence at protein level;
KW Chromosome; Direct protein sequencing; Nucleus; Ribosomal frameshifting;
KW RNA-binding; Telomere.
FT CHAIN 1..437
FT /note="La-related protein 7 homolog"
FT /id="PRO_0000449906"
FT DOMAIN 38..145
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT DOMAIN 279..397
FT /note="xRRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01288,
FT ECO:0000303|PubMed:22705372"
FT REGION 417..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 437 AA; 50722 MW; F8661001AF96A11C CRC64;
MEMDIDLDDI ENLLPNTFNK YSSSCSDKKG CKTLKSGSKS PSLTIPKLQK QLEFYFSDAN
LYNDSFLRKL VLKSGEQRVE IETLLMFKKI RSLLKEHYGE NYLILKANND EYIKFICECV
KGSRYIRLTK DKLAIKRKKK FDNRTAEELI AFTIRIDGEL PSLETIEKAV YNCRNRSSES
SDVNKPNKPC KFNGIYVKSF GTNAHCIYIG FLKHRYTECF RDCFSLQQIT CFDYSCSSLI
SLKEAGEMKR RLKKEISKFV DSSVTGINNK NISNEKEEEL SQSCFLKISK IPAGSKKYQI
REALDCDRPS YIQYDDKETA VIRFKNSAMR TKFLESRNGA EILIKKNCVD IAKESNSKSF
VNKYYQSCLI EEIDEATAQK IIKEIKDQRS SIDEIKAELK LDNKKYKPWS KYCGRKRRPV
SKRKNKAINK MSTEVKK
