Overview
| Uniprot ID | P61011 |
|---|
| Protein Name | Signal recognition particle subunit SRP54 |
|---|
| Gene Name | SRP54 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 321 |
DNEALIEKLKHGQFT |
Function
Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (PubMed:34020957). As part of the SRP complex, associates with the SRP receptor (SR) component SRPRA to target secretory proteins to the endoplasmic reticulum membrane (PubMed:34020957). Binds to the signal sequence of presecretory proteins when they emerge from the ribosomes (PubMed:34020957). Displays basal GTPase activity, and stimulates reciprocal GTPase activation of the SR subunit SRPRA (PubMed:28972538, PubMed:34020957). Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SR subunit SRPRA (PubMed:34020957). SR compaction and GTPase mediated rearrangement of SR drive SRP-mediated cotranslational protein translocation into the ER (PubMed:34020957). Requires the presence of SRP9/SRP14 and/or SRP19 to stably interact with RNA (By similarity). Plays a role in proliferation and differentiation of granulocytic cells, neutrophils migration capacity and exocrine pancreas development (PubMed:28972538, PubMed:29914977)
Protein Sequence
10
MVLADLGRKI
20
TSALRSLSNA
30
TIINEEVLNA
40
MLKEVCTALL
50
EADVNIKLVK
60
QLRENVKSAI
70
DLEEMASGLN
80
KRKMIQHAVF
90
KELVKLVDPG
100
VKAWTPTKGK
110
QNVIMFVGLQ
120
GSGKTTTCSK
130
LAYYYQRKGW
140
KTCLICADTF
150
RAGAFDQLKQ
160
NATKARIPFY
170
GSYTEMDPVI
180
IASEGVEKFK
190
NENFEIIIVD
200
TSGRHKQEDS
210
LFEEMLQVAN
220
AIQPDNIVYV
230
MDASIGQACE
240
AQAKAFKDKV
250
DVASVIVTKL
260
DGHAKGGGAL
270
SAVAATKSPI
280
IFIGTGEHID
290
DFEPFKTQPF
300
ISKLLGMGDI
310
EGLIDKVNEL
320
KLDDNEALIE
330
KLKHGQFTLR
340
DMYEQFQNIM
350
KMGPFSQILG
360
MIPGFGTDFM
370
SKGNEQESMA
380
RLKKLMTIMD
390
SMNDQELDST
400
DGAKVFSKQP
410
GRIQRVARGS
420
GVSTRDVQEL
430
LTQYTKFAQM
440
VKKMGGIKGL
450
FKGGDMSKNV
460
SQSQMAKLNQ
470
QMAKMMDPRV
480
LHHMGGMAGL
490
QSMMRQFQQG
500
AAGNMKGMMG
FNNM
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0005783 |
endoplasmic reticulum |
| Cellular Component |
GO:0016607 |
nuclear speck |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0005786 |
signal recognition particle, endoplasmic reticulum targeting |
| Molecular Function |
GO:0008312 |
7S RNA binding |
| Molecular Function |
GO:0030942 |
endoplasmic reticulum signal peptide binding |
| Molecular Function |
GO:0019003 |
GDP binding |
| Molecular Function |
GO:0005525 |
GTP binding |
| Molecular Function |
GO:0003924 |
GTPase activity |
| Molecular Function |
GO:0043021 |
ribonucleoprotein complex binding |
| Molecular Function |
GO:0003723 |
RNA binding |
| Biological Process |
GO:0031017 |
exocrine pancreas development |
| Biological Process |
GO:0030851 |
granulocyte differentiation |
| Biological Process |
GO:0030593 |
neutrophil chemotaxis |
| Biological Process |
GO:0045047 |
protein targeting to ER |
| Biological Process |
GO:0006614 |
SRP-dependent cotranslational protein targeting to membrane |
| Biological Process |
GO:0006617 |
SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition |
| Biological Process |
GO:0006616 |
SRP-dependent cotranslational protein targeting to membrane, translocation |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.