LARP7_XENTR
ID LARP7_XENTR Reviewed; 593 AA.
AC Q28G87;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=La-related protein 7 {ECO:0000250|UniProtKB:Q4G0J3};
DE AltName: Full=La ribonucleoprotein domain family member 7 {ECO:0000250|UniProtKB:Q4G0J3};
GN Name=larp7 {ECO:0000250|UniProtKB:Q4G0J3};
GN ORFNames=TGas080c15.1 {ECO:0000303|Ref.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA-binding protein that specifically binds distinct small
CC nuclear RNA (snRNAs) and regulates their processing and function.
CC Specifically binds the 7SK snRNA (7SK RNA) and acts as a core component
CC of the 7SK ribonucleoprotein (RNP) complex, thereby acting as a
CC negative regulator of transcription elongation by RNA polymerase II.
CC The 7SK RNP complex sequesters the positive transcription elongation
CC factor b (P-TEFb) in a large inactive 7SK RNP complex preventing RNA
CC polymerase II phosphorylation and subsequent transcriptional elongation
CC (By similarity). The 7SK RNP complex also promotes snRNA gene
CC transcription by RNA polymerase II via interaction with the little
CC elongation complex (LEC). LARP7 specifically binds to the highly
CC conserved 3'-terminal U-rich stretch of 7SK RNA; on stimulation,
CC remains associated with 7SK RNA, whereas P-TEFb is released from the
CC complex. LARP7 also acts as a regulator of mRNA splicing fidelity by
CC promoting U6 snRNA processing. Specifically binds U6 snRNAs and
CC associates with a subset of box C/D RNP complexes: promotes U6 snRNA
CC 2'-O-methylation by facilitating U6 snRNA loading into box C/D RNP
CC complexes. U6 snRNA 2'-O-methylation is required for mRNA splicing
CC fidelity (By similarity). {ECO:0000250|UniProtKB:Q4G0J3,
CC ECO:0000250|UniProtKB:Q7ZWE3}.
CC -!- SUBUNIT: Core component of the 7SK RNP complex. Associates with box C/D
CC small nucleolar ribonucleoprotein (snoRNP) complexes.
CC {ECO:0000250|UniProtKB:Q4G0J3}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q4G0J3}.
CC -!- DOMAIN: The xRRM domain binds the 3' end of 7SK snRNA (7SK RNA) at the
CC top of stem-loop 4. {ECO:0000250|UniProtKB:Q4G0J3}.
CC -!- SIMILARITY: Belongs to the LARP7 family. {ECO:0000305}.
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DR EMBL; CR761502; CAJ83882.1; -; mRNA.
DR RefSeq; NP_001039168.1; NM_001045703.1.
DR AlphaFoldDB; Q28G87; -.
DR SMR; Q28G87; -.
DR STRING; 8364.ENSXETP00000051994; -.
DR PaxDb; Q28G87; -.
DR GeneID; 734000; -.
DR KEGG; xtr:734000; -.
DR CTD; 51574; -.
DR Xenbase; XB-GENE-984850; larp7.
DR eggNOG; KOG0118; Eukaryota.
DR InParanoid; Q28G87; -.
DR OrthoDB; 1499213at2759; -.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000024097; Expressed in gastrula and 12 other tissues.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0097322; F:7SK snRNA binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0017070; F:U6 snRNA binding; ISS:UniProtKB.
DR GO; GO:0000494; P:box C/D RNA 3'-end processing; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1904871; P:positive regulation of protein localization to Cajal body; ISS:UniProtKB.
DR GO; GO:1905382; P:positive regulation of snRNA transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR GO; GO:1990438; P:U6 2'-O-snRNA methylation; ISS:UniProtKB.
DR CDD; cd08032; LARP_7; 1.
DR CDD; cd12290; RRM1_LARP7; 1.
DR CDD; cd12542; RRM2_LARP7; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR045180; La_dom_prot.
DR InterPro; IPR006630; La_HTH.
DR InterPro; IPR014886; La_xRRM.
DR InterPro; IPR034946; LARP7_La.
DR InterPro; IPR034887; LARP7_RRM1.
DR InterPro; IPR034910; LARP7_RRM2.
DR InterPro; IPR002344; Lupus_La.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR22792; PTHR22792; 1.
DR Pfam; PF05383; La; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF08777; RRM_3; 1.
DR PRINTS; PR00302; LUPUSLA.
DR SMART; SM00715; LA; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50961; HTH_LA; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS51939; XRRM; 1.
PE 2: Evidence at transcript level;
KW Differentiation; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; RNA-binding; Spermatogenesis; Transcription;
KW Transcription regulation.
FT CHAIN 1..593
FT /note="La-related protein 7"
FT /id="PRO_0000281681"
FT DOMAIN 30..121
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT DOMAIN 127..205
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 461..574
FT /note="xRRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01288"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 593 AA; 68069 MW; 2276225F53104857 CRC64;
MTAIETDTPS NKVKEDESTD LRKDREKKKR SRVKQLLADI AKQVDFWFGD VNLHKDRFLR
EQIEKTRDGY IDISLLASFN KMKKITTDSK LIARAVKNSS VVEINLSGTK IRRRFPLGEK
PQDVDSRTVY VELLPKNVTH SWIERVFGKY GMVVYVSIPR YKSTGDPKGF AFIEFETQEQ
AAKAIEVLNN PPEEAPRKAG MFPKTVKNKH LPPVEVTEHS ITEGCGTEEK KKKKKKKSKA
RKDSVEKAEE DTKEQDMDII SEGVPKRRKT VSESSVPDVQ EADKQTAKKE KKKKERAESF
DQSEKVRQGK RKCSSSEEHD CSSAKQKKSD TKDLPQDEKP MVTQEVLQEC KELSTEEEKD
AVDKKEISVP KVKRKRKKKH KERHRVGEEV IPLRVLSKTE WLVLKAEYLT LQRASMASLK
KSMSEMNHIS EEEMQTQPSM QSFDIKNGKV ETVKNEPLGP QFVCGVIGKI TSSDPLQGRK
YVKDAFSGVC EVVYVDMLEG DTECHVRFKS PEDAQTAVKT RSDLQGKHNW KLQILAGDNE
QRYWQKILVD RQAKLNRPRE KKRGTEKLIA KAEKMRLAKT QEASKHIRFS DGF
