LARP7_DANRE
ID LARP7_DANRE Reviewed; 555 AA.
AC Q7ZWE3;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=zgc:56476 {ECO:0000303|Ref.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=SJD;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=26542022; DOI=10.1242/jcs.175018;
RA Matrone G., Wilson K.S., Maqsood S., Mullins J.J., Tucker C.S.,
RA Denvir M.A.;
RT "CDK9 and its repressor LARP7 modulate cardiomyocyte proliferation and
RT response to injury in the zebrafish heart.";
RL J. Cell Sci. 128:4560-4571(2015).
CC -!- FUNCTION: RNA-binding protein that specifically binds distinct small
CC nuclear RNA (snRNAs) and regulates their processing and function
CC (PubMed:26542022). Specifically binds the 7SK snRNA (7SK RNA) and acts
CC as a core component of the 7SK ribonucleoprotein (RNP) complex, thereby
CC acting as a negative regulator of transcription elongation by RNA
CC polymerase II (PubMed:26542022). The 7SK RNP complex sequesters the
CC positive transcription elongation factor b (P-TEFb) in a large inactive
CC 7SK RNP complex preventing RNA polymerase II phosphorylation and
CC subsequent transcriptional elongation (PubMed:26542022). The 7SK RNP
CC complex also promotes snRNA gene transcription by RNA polymerase II via
CC interaction with the little elongation complex (LEC) (By similarity).
CC LARP7 specifically binds to the highly conserved 3'-terminal U-rich
CC stretch of 7SK RNA; on stimulation, remains associated with 7SK RNA,
CC whereas P-TEFb is released from the complex (By similarity). LARP7 also
CC acts as a regulator of mRNA splicing fidelity by promoting U6 snRNA
CC processing. Specifically binds U6 snRNAs and associates with a subset
CC of box C/D RNP complexes: promotes U6 snRNA 2'-O-methylation by
CC facilitating U6 snRNA loading into box C/D RNP complexes (By
CC similarity). U6 snRNA 2'-O-methylation is required for mRNA splicing
CC fidelity (By similarity). {ECO:0000250|UniProtKB:Q4G0J3,
CC ECO:0000269|PubMed:26542022}.
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 -!- DEVELOPMENTAL STAGE: Expression reaches a peak at 48 hours post-
CC fertilization (hpf) and then decreases at 72, 96 and 120 hpf
CC (PubMed:26542022). In embryonic hearts, expression slightly increases
CC between 48 and 96 hpf, and then decreases at 120 hpf (PubMed:26542022).
CC Expressed in the adult heart (PubMed:26542022).
CC {ECO:0000269|PubMed:26542022}.
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 -!- DISRUPTION PHENOTYPE: Mild cardiac phenotype with increased
CC phosphorylation of 'Ser-2' on RNA polymerase II.
CC {ECO:0000269|PubMed:26542022}.
CC -!- SIMILARITY: Belongs to the LARP7 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC049455; AAH49455.1; -; mRNA.
DR RefSeq; NP_956224.1; NM_199930.2.
DR AlphaFoldDB; Q7ZWE3; -.
DR SMR; Q7ZWE3; -.
DR STRING; 7955.ENSDARP00000013520; -.
DR PaxDb; Q7ZWE3; -.
DR GeneID; 334956; -.
DR KEGG; dre:334956; -.
DR CTD; 51574; -.
DR ZFIN; ZDB-GENE-030131-6896; larp7.
DR eggNOG; KOG0118; Eukaryota.
DR InParanoid; Q7ZWE3; -.
DR PhylomeDB; Q7ZWE3; -.
DR PRO; PR:Q7ZWE3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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:0061026; P:cardiac muscle tissue regeneration; IGI:ZFIN.
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:0060043; P:regulation of cardiac muscle cell proliferation; IGI:ZFIN.
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; 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; 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 Coiled coil; Differentiation; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; RNA-binding; Spermatogenesis; Transcription;
KW Transcription regulation.
FT CHAIN 1..555
FT /note="La-related protein 7"
FT /id="PRO_0000281680"
FT DOMAIN 36..127
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT DOMAIN 133..211
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 425..538
FT /note="xRRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01288"
FT REGION 218..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 295..356
FT /evidence="ECO:0000255"
FT COMPBIAS 220..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 555 AA; 64063 MW; CAE4BF92EBB3111C CRC64;
MKVCQRKTID TEKMSSVGDT ACADLSEKKD NEKKKRSRVK QLLSDVKKQV EFWFGDVNLH
KDRFMKSIIE QSRDGYIDIA VLTTFNRMKN LTADVKLIAR ALKNSTIVEV NDEGTRIRRK
EPLGETPKDV DSRTVYVELL PKTVTHIWLE RVFSKCGHVV YISIPRYKST RHSKGFAFVE
FETQEQAQKA VEMLNNPPED APRKPGIFPK TCRKKAVPFD AVTQDNDEDG KKKKTELKNS
TSEETGSNNM DQDGMLESTV TSEPNLATLT STVSKKAKKK RLRSQSFEAS SGEDQFEMSS
KMRKVEEEKS ELKDLSSENK DEELNSLKKK DDSVLKAKRK RKKKLKERLK VGEEVIPLRV
LSKKEWLDLK QEYLTLQKRC MAHLKQSVFQ INQKPTNYHI VKLKEDDTNA FYKDTPKKEL
TSGPEFLSGV IVKISYNQPL PSKRCIKDML SELSPVAYVD LLDGDTEGHV RFKSSEDAQK
VIKARFEFQK KYNWNLELLS GDHERRYWQK ILVDRQAKLN TPREKKRGTE KLISKAEKII
IAKAKEASNH IRFDD
