LARP7_MACFA
ID LARP7_MACFA Reviewed; 581 AA.
AC Q4R627;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=QtsA-19289 {ECO:0000303|Ref.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) 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
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}.
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DR EMBL; AB169363; BAE01448.1; -; mRNA.
DR AlphaFoldDB; Q4R627; -.
DR SMR; Q4R627; -.
DR STRING; 9541.XP_005555766.1; -.
DR Ensembl; ENSMFAT00000029366; ENSMFAP00000001189; ENSMFAG00000036506.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000154949; -.
DR Proteomes; UP000233100; Chromosome 5.
DR Bgee; ENSMFAG00000036506; Expressed in heart and 13 other tissues.
DR GO; GO:0120259; C:7SK snRNP; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0097322; F:7SK snRNA binding; ISS:UniProtKB.
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:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0032897; P:negative regulation of viral transcription; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Acetylation; Differentiation; Isopeptide bond; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW Spermatogenesis; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..581
FT /note="La-related protein 7"
FT /id="PRO_0000281678"
FT DOMAIN 28..122
FT /note="HTH La-type RNA-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00332"
FT DOMAIN 125..203
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 449..562
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 188..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..353
FT /note="Basic and acidic 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 257
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT MOD_RES 338
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT CROSSLNK 237
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
FT CROSSLNK 410
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q4G0J3"
SQ SEQUENCE 581 AA; 66637 MW; 43D1CEDDA69F610D CRC64;
METESGNQKN VMEEESTEKK KEVEKKKRSR VKQVLADIAK QVDFWFGDAN LHKDRFLREQ
IEKSRDGYVD ISLLVSFNKM KKLTTDGKLI ARALRSSAVV ELDLEGTRIR RKKPLGERPK
DEDERTVYVE LLPKNVNHSW IERVFGKCGN VVYISIPHYK STGDPKGFAF VEFETKEQAA
KAIEFLNNPP EEAPRKPGIF PKTVKNKPIP ALRVVEEKKK KKKKKGRMKK EDNVQAKEEN
MDTTNTSISK MKRSRPTSEG SDIESTEPQK QSSKKKKKRD RVEASSLPEV RTGKRKRSSS
EDAESLGPRS KVKKIIQKDI IKEPSEASKE NRDIEISTEE EKDTGDLKDS SLLKTKRKHK
KKHKERHKMG EEVIPLRVLS KSEWMDLKKE YLALQKASMA SLKKTISQIK SESEMETDGG
VPQKTGMKNE KTNSEECPTQ EKVNATGPQF VSGVIVKIIS TEPLPGRKQV RDTLAAISEV
LYVDLLEGDT ECHARFKTPE DAQAVINAYT EISKKHCWKL EILSGDHEQR YWQKILVDRQ
AKLNQPREKK RGTEKLITKA EKIRLAKTQQ ASKHIRFSEY D
