Overview
| Uniprot ID | Q5XI01 |
| Protein Name | La-related protein 7 |
| Gene Name | Larp7 |
| Organism | Rattus norvegicus |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 245 |
SSSSGVSKATKRPRT |
| 277 |
KKKKKRDKVETGGLP |
| 287 |
TGGLPESKAGKRERS |
| 314 |
KLKKRAQKDGGGPAA |
| 549 |
GTEKLITKAEKIRLA |
| 557 |
AEKIRLAKTQQASQH |
Function
RNA-binding protein that specifically binds distinct small nuclear RNA (snRNAs) and regulates their processing and function. Specifically binds the 7SK snRNA (7SK RNA) and acts as a core component of the 7SK ribonucleoprotein (RNP) complex, thereby acting as a negative regulator of transcription elongation by RNA polymerase II. The 7SK RNP complex sequesters the positive transcription elongation factor b (P-TEFb) in a large inactive 7SK RNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation. The 7SK RNP complex also promotes snRNA gene transcription by RNA polymerase II via interaction with the little elongation complex (LEC). LARP7 specifically binds to the highly conserved 3'-terminal U-rich stretch of 7SK RNA; on stimulation, remains associated with 7SK RNA, whereas P-TEFb is released from the complex. LARP7 also acts as a regulator of mRNA splicing fidelity by promoting U6 snRNA processing. Specifically binds U6 snRNAs and associates with a subset of box C/D RNP complexes: promotes U6 snRNA 2'-O-methylation by facilitating U6 snRNA loading into box C/D RNP complexes. U6 snRNA 2'-O-methylation is required for mRNA splicing fidelity. Binds U6 snRNAs with a 5'-CAGGG-3' sequence motif (By similarity). U6 snRNA processing is required for spermatogenesis (By similarity)
Protein Sequence
10
METENQKTME
20
ESTEKRKEEK
30
KKRSRVKQVL
40
ADIAKQVDFW
50
FGDANLHKDR
60
FLREQIEKSR
70
DGYVDISLLV
80
SFNKMKKLTT
90
DGKLIARALK
100
SSSVVELDLE
110
GTRIRRKKPL
120
GERPKDEEER
130
TVYVELLPKN
140
VTHSWIERVF
150
GKCGNVVYIS
160
IPHYKSTGDP
170
KGFAFVEFET
180
KEQAAKAIEF
190
LNNPPEEAPR
200
KPGIFPKTVK
210
NKPIPSLRVA
220
EEKKKKKKKK
230
GRIKKEESVQ
240
AKELVVDSSS
250
SGVSKATKRP
260
RTASEGSEAE
270
TPEAPKQPAK
280
KKKKRDKVET
290
GGLPESKAGK
300
RERSSAEDED
310
CLPPRPKLKK
320
RAQKDGGGPA
330
ASEVSKEHRD
340
LEFCSTEEEK
350
EPGDRKGDSL
360
SKGKRKHKKK
370
HKERHKMGEE
380
VIPLRVLSKT
390
EWMDLKKEYL
400
ALQKASMASL
410
KKTISQIKLE
420
SEMETESKAP
430
PGSGQQCSTQ
440
EKVSAQGPQF
450
VTGVIVKILS
460
EDPLPGRKQV
470
KDILATISEV
480
VYIDLLEGDT
490
ECHARFKTPE
500
DAQAVMNAQT
510
EIKKKHSWNL
520
EILSGDHEQR
530
YWQKILVDRQ
540
AKLNQPREKK
550
RGTEKLITKA
560
EKIRLAKTQQ
570
ASQHIRFSEY
D
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0120259 |
7SK snRNP |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:1990904 |
ribonucleoprotein complex |
| Molecular Function |
GO:0097322 |
7SK snRNA binding |
| Molecular Function |
GO:0003723 |
RNA binding |
| Molecular Function |
GO:0017070 |
U6 snRNA binding |
| Biological Process |
GO:0000494 |
box C/D sno(s)RNA 3'-end processing |
| Biological Process |
GO:0030154 |
cell differentiation |
| Biological Process |
GO:0006351 |
DNA-templated transcription |
| Biological Process |
GO:0036093 |
germ cell proliferation |
| Biological Process |
GO:0006397 |
mRNA processing |
| Biological Process |
GO:0000122 |
negative regulation of transcription by RNA polymerase II |
| Biological Process |
GO:0032897 |
negative regulation of viral transcription |
| Biological Process |
GO:1900087 |
positive regulation of G1/S transition of mitotic cell cycle |
| Biological Process |
GO:1904871 |
positive regulation of protein localization to Cajal body |
| Biological Process |
GO:1905382 |
positive regulation of snRNA transcription by RNA polymerase II |
| Biological Process |
GO:0048024 |
regulation of mRNA splicing, via spliceosome |
| Biological Process |
GO:0008380 |
RNA splicing |
| Biological Process |
GO:0007283 |
spermatogenesis |
| Biological Process |
GO:1990438 |
U6 2'-O-snRNA methylation |
Reference
[1] Sheng L, Xu H, Wang Y, Ni J, Xiang T et al.. Systematic analysis of lysine lactylation in nucleus pulposus cells.. iScience 27(11):111157. 2024 Nov 15. PMID: 39524337.