LARP7_RAT
ID LARP7_RAT Reviewed; 571 AA.
AC Q5XI01;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 25-MAY-2022, entry version 119.
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:0000312|RGD:1592474};
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=Testis;
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 PROTEIN SEQUENCE OF 8-15; 347-354 AND 409-418, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254 AND SER-257, 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-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
CC elongation. The 7SK RNP complex also promotes snRNA gene transcription
CC by RNA polymerase II via interaction with the little elongation complex
CC (LEC). LARP7 specifically binds to the highly conserved 3'-terminal U-
CC rich stretch of 7SK RNA; on stimulation, remains associated with 7SK
CC RNA, whereas P-TEFb is released from the complex. LARP7 also acts as a
CC regulator of mRNA splicing fidelity by promoting U6 snRNA processing.
CC Specifically binds U6 snRNAs and associates with a subset of box C/D
CC RNP complexes: promotes U6 snRNA 2'-O-methylation by facilitating U6
CC snRNA loading into box C/D RNP complexes. U6 snRNA 2'-O-methylation is
CC required for mRNA splicing fidelity. Binds U6 snRNAs with a 5'-CAGGG-3'
CC sequence motif (By similarity). U6 snRNA processing is required for
CC spermatogenesis (By similarity). {ECO:0000250|UniProtKB:Q05CL8,
CC ECO:0000250|UniProtKB:Q4G0J3}.
CC -!- SUBUNIT: Core component of the 7SK RNP complex, at least composed of
CC 7SK RNA, LARP7, MEPCE, HEXIM1 (or HEXIM2) and P-TEFb (composed of CDK9
CC and CCNT1/cyclin-T1). Interacts with METTL16. Interacts with RBM7; upon
CC genotoxic stress this interaction is enhanced, triggering the release
CC of inactive P-TEFb complex from the core, yielding to P-TEFb complex
CC activation. Associates with box C/D small nucleolar ribonucleoprotein
CC (snoRNP) complexes. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH83898.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC083898; AAH83898.1; ALT_INIT; mRNA.
DR RefSeq; NP_001037755.2; NM_001044290.2.
DR AlphaFoldDB; Q5XI01; -.
DR SMR; Q5XI01; -.
DR BioGRID; 601734; 2.
DR STRING; 10116.ENSRNOP00000065357; -.
DR iPTMnet; Q5XI01; -.
DR PhosphoSitePlus; Q5XI01; -.
DR jPOST; Q5XI01; -.
DR PaxDb; Q5XI01; -.
DR PRIDE; Q5XI01; -.
DR GeneID; 686883; -.
DR KEGG; rno:686883; -.
DR CTD; 51574; -.
DR RGD; 1592474; Larp7.
DR eggNOG; KOG0118; Eukaryota.
DR InParanoid; Q5XI01; -.
DR OrthoDB; 1499213at2759; -.
DR PhylomeDB; Q5XI01; -.
DR PRO; PR:Q5XI01; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0120259; C:7SK snRNP; ISO:RGD.
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:0036093; P:germ cell proliferation; ISO:RGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0035562; P:negative regulation of chromatin binding; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0032897; P:negative regulation of viral transcription; ISO:RGD.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:RGD.
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; 2.
DR PROSITE; PS50961; HTH_LA; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS51939; XRRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Differentiation; Direct protein sequencing; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Spermatogenesis; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..571
FT /note="La-related protein 7"
FT /id="PRO_0000281679"
FT DOMAIN 23..117
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT DOMAIN 120..198
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 439..552
FT /note="xRRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01288"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT MOD_RES 252
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q05CL8"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 261
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q05CL8"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT MOD_RES 336
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT CROSSLNK 232
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT CROSSLNK 408
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
SQ SEQUENCE 571 AA; 64949 MW; EB52574AB7D6E330 CRC64;
METENQKTME ESTEKRKEEK KKRSRVKQVL ADIAKQVDFW FGDANLHKDR FLREQIEKSR
DGYVDISLLV SFNKMKKLTT DGKLIARALK SSSVVELDLE GTRIRRKKPL GERPKDEEER
TVYVELLPKN VTHSWIERVF GKCGNVVYIS IPHYKSTGDP KGFAFVEFET KEQAAKAIEF
LNNPPEEAPR KPGIFPKTVK NKPIPSLRVA EEKKKKKKKK GRIKKEESVQ AKELVVDSSS
SGVSKATKRP RTASEGSEAE TPEAPKQPAK KKKKRDKVET GGLPESKAGK RERSSAEDED
CLPPRPKLKK RAQKDGGGPA ASEVSKEHRD LEFCSTEEEK EPGDRKGDSL SKGKRKHKKK
HKERHKMGEE VIPLRVLSKT EWMDLKKEYL ALQKASMASL KKTISQIKLE SEMETESKAP
PGSGQQCSTQ EKVSAQGPQF VTGVIVKILS EDPLPGRKQV KDILATISEV VYIDLLEGDT
ECHARFKTPE DAQAVMNAQT EIKKKHSWNL EILSGDHEQR YWQKILVDRQ AKLNQPREKK
RGTEKLITKA EKIRLAKTQQ ASQHIRFSEY D
