Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for P20424

Entry ID Method Resolution Chain Position Source
AF-P20424-F1 Predicted AlphaFoldDB

6 variants for P20424

Variant ID(s) Position Change Description Diseaes Association Provenance
s16-712849 60 Q>K No SGRP
s16-712750 93 T>S No SGRP
s16-712726 101 A>T No SGRP
s16-712712 105 K>N No SGRP
s16-711685 448 P>S No SGRP
s16-711629 466 M>I No SGRP

No associated diseases with P20424

4 regional properties for P20424

Type Name Position InterPro Accession
domain Signal recognition particle, SRP54 subunit, GTPase domain 109 - 304 IPR000897
domain AAA+ ATPase domain 108 - 294 IPR003593
domain Signal recognition particle, SRP54 subunit, M-domain 335 - 436 IPR004125
domain Signal recognition particle SRP54, helical bundle 2 - 92 IPR013822

Functions

Description
EC Number 3.6.5.4 Acting on GTP; involved in cellular and subcellular movement
Subcellular Localization
  • Cytoplasm
  • Endoplasmic reticulum
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
signal recognition particle, endoplasmic reticulum targeting A ribonucleoprotein particle of 325 kDa composed of a 7S (300 nucleotide) RNA molecule and a complex of six different polypeptides. This binds both to the N-terminal signal peptide for proteins destined for the endoplasmic reticulum as they emerge from the large ribosomal subunit and also to the ribosome. This binding arrests further translation thereby preventing the proteins from being released into the cytosol. The SRP-ribosome complex then diffuses to the endoplasmic reticulum where it is bound to the signal recognition particle receptor, which allows resumption of protein synthesis and facilitates the passage of the growing polypeptide chain through the translocon. Through a process involving GTP hydrolysis, the SRP-SRP receptor complex dissociates and SRP returns to the cytosol. Of the six polypeptides of SRP the 54 kDa subunit (SRP54) is the central player. It contains an N-terminal GTPase domain and a C-terminal domain that binds directly to the signal peptide and the SRP RNA. Examples of this component are found in Mus musculus, Saccharomyces cerevisiae and Arabidopsis thaliana.

5 GO annotations of molecular function

Name Definition
7S RNA binding Binding to a 7S RNA, the RNA component of the signal recognition particle (SRP).
endoplasmic reticulum signal peptide binding Binding to an endoplasmic reticulum signal peptide, a specific peptide sequence that acts as a signal to localize the protein within the endoplasmic reticulum.
GTP binding Binding to GTP, guanosine triphosphate.
GTPase activator activity Binds to and increases the activity of a GTPase, an enzyme that catalyzes the hydrolysis of GTP.
GTPase activity Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate.

3 GO annotations of biological process

Name Definition
SRP-dependent cotranslational protein targeting to membrane The targeting of proteins to a membrane that occurs during translation and is dependent upon two key components, the signal-recognition particle (SRP) and the SRP receptor. SRP is a cytosolic particle that transiently binds to the endoplasmic reticulum (ER) signal sequence in a nascent protein, to the large ribosomal unit, and to the SRP receptor in the ER membrane.
SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition The process in which SRP binds to the signal peptide in a nascent protein, causing protein elongation to pause, during cotranslational membrane targeting.
SRP-dependent cotranslational protein targeting to membrane, translocation The process during cotranslational membrane targeting wherein proteins move across a membrane. SRP and its receptor initiate the transfer of the nascent chain across the endoplasmic reticulum (ER) membrane; they then dissociate from the chain, which is transferred to a set of transmembrane proteins, collectively called the translocon. Once the nascent chain translocon complex is assembled, the elongating chain passes directly from the large ribosomal subunit into the centers of the translocon, a protein-lined channel within the membrane. The growing chain is never exposed to the cytosol and does not fold until it reaches the ER lumen.

8 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q2T9U1 SRP54 Signal recognition particle 54 kDa protein Bos taurus (Bovine) PR
P61010 SRP54 Signal recognition particle 54 kDa protein Canis lupus familiaris (Dog) (Canis familiaris) PR
P61011 SRP54 Signal recognition particle 54 kDa protein Homo sapiens (Human) PR
P14576 Srp54 Signal recognition particle 54 kDa protein Mus musculus (Mouse) PR
Q6AYB5 Srp54 Signal recognition particle 54 kDa protein Rattus norvegicus (Rat) PR
P49966 SRP-54B Signal recognition particle 54 kDa protein 2 Arabidopsis thaliana (Mouse-ear cress) PR
P49971 Signal recognition particle 54 kDa protein 1 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) PR
P49972 Signal recognition particle 54 kDa protein 2 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) PR
10 20 30 40 50 60
MVLADLGKRI NSAVNNAISN TQDDFTTSVD VMLKGIVTAL LESDVNIALV SKLRNNIRSQ
70 80 90 100 110 120
LLSENRSEKS TTNAQTKKLI QKTVFDELCK LVTCEGSEEK AFVPKKRKTN IIMFVGLQGS
130 140 150 160 170 180
GKTTSCTKLA VYYSKRGFKV GLVCADTFRA GAFDQLKQNA IRARIPFYGS YTETDPAKVA
190 200 210 220 230 240
EEGINKFKKE KFDIIIVDTS GRHHQEEELF QEMIEISNVI KPNQTIMVLD ASIGQAAEQQ
250 260 270 280 290 300
SKAFKESSDF GAIILTKMDG HARGGGAISA VAATNTPIIF IGTGEHIHDL EKFSPKSFIS
310 320 330 340 350 360
KLLGIGDIES LFEQLQTVSN KEDAKATMEN IQKGKFTLLD FKKQMQTIMK MGPLSNIAQM
370 380 390 400 410 420
IPGMSNMMNQ VGEEETSQKM KKMVYVLDSM TKEELESDGR MFIEEPTRMV RVAKGSGTSV
430 440 450 460 470 480
FEVEMILMQQ QMMARMAQTA TQQQPGAPGA NARMPGMPNM PGMPNMPGMP NMPGMPKVTP
490 500 510 520 530 540
QMMQQAQQKL KQNPGLMQNM MNMFGGGMGG GMGGGMPDMN EMMKMMQDPQ MQQMAKQFGM
G