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 Q9U5L1

Entry ID Method Resolution Chain Position Source
AF-Q9U5L1-F1 Predicted AlphaFoldDB

No variants for Q9U5L1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9U5L1

No associated diseases with Q9U5L1

4 regional properties for Q9U5L1

Type Name Position InterPro Accession
domain Signal recognition particle, SRP54 subunit, GTPase domain 395 - 614 IPR000897
domain AAA+ ATPase domain 394 - 547 IPR003593
domain Signal recognition particle receptor, alpha subunit, N-terminal 27 - 267 IPR007222
domain Signal recognition particle SRP54, helical bundle 293 - 374 IPR013822

Functions

Description
EC Number
Subcellular Localization
  • Endoplasmic reticulum membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Thought to be anchored in the membrane through an interaction with SrpRbeta, which contains a bona fide transmembrane domain
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
endomembrane system A collection of membranous structures involved in transport within the cell. The main components of the endomembrane system are endoplasmic reticulum, Golgi bodies, vesicles, cell membrane and nuclear envelope. Members of the endomembrane system pass materials through each other or though the use of vesicles.
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
signal recognition particle receptor complex A transmembrane heterodimeric protein located in the membrane of the rough endoplasmic reticulum. Both subunits contain GTPase domains with which signal recognition particle interacts. In the presence of GTP and SRP receptor, SRP is released from the ribosome-nascent chain complex.

4 GO annotations of molecular function

Name Definition
GTP binding Binding to GTP, guanosine triphosphate.
GTPase activity Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate.
RNA binding Binding to an RNA molecule or a portion thereof.
signal recognition particle binding Binding to a signal recognition particle.

5 GO annotations of biological process

Name Definition
axonogenesis De novo generation of a long process of a neuron, including the terminal branched region. Refers to the morphogenesis or creation of shape or form of the developing axon, which carries efferent (outgoing) action potentials from the cell body towards target cells.
protein targeting The process of targeting specific proteins to particular regions of the cell, typically membrane-bounded subcellular organelles. Usually requires an organelle specific protein sequence motif.
protein targeting to ER The process of directing proteins towards the endoplasmic reticulum (ER) using signals contained within the protein. One common mechanism uses a 16- to 30-residue signal sequence, typically located at the N-terminus of the protein and containing positively charged amino acids followed by a continuous stretch of hydrophobic residues, which directs the ribosome to the ER membrane and initiates transport of the growing polypeptide across the ER membrane.
regulation of protein secretion Any process that modulates the frequency, rate or extent of the controlled release of a protein from a cell.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLDFVVIFTK GGVVLWHSNA SGNSFASCIN SLIRGVILEE RNTEAKYYEE DHLAVQFKLD
70 80 90 100 110 120
NELDLVYAAI FQKVIKLNYL DGFLADMQAA FKEKYGDIRL GDDYDFDREY RRVLSAAEEA
130 140 150 160 170 180
SAKQVKAPKT MRSYNESQKS KKTVASMIQD DKKPVEKRVN IQEAPPPSKS QPSSPPTGSP
190 200 210 220 230 240
MDKIIMEKRR KLREKLTPTK KTSPSDSKSS KPEKAGKKPR VWDLGGNSKD AALLDRSRDS
250 260 270 280 290 300
PDDVQYQNIN SELVGTMQGV IRDLDVESED EADNEDASSE GEAEEQVQSK KGKRGGLLSY
310 320 330 340 350 360
FKGIVGAKTM SLADLQPALE KMRDHLISKN VASEIAAKLC DSVAASLDGK QMGTFDSIAS
370 380 390 400 410 420
QVKEALTESL VRILSPKRRI DIIRDALESK RNGRPYTIIF CGVNGVGKST NLAKICFWLI
430 440 450 460 470 480
ENDFNVLIAA CDTFRAGAVE QLRTHTRHLN ALHPAAKHDG RNMVQLYEKG YGKDAAGIAM
490 500 510 520 530 540
EAIKFAHDTR VDVVLVDTAG RMQDNEPLMR SLSKLIKVNN PDLVLFVGEA LVGNEAVDQL
550 560 570 580 590 600
VKFNQSLADY SSNENPHIID GIVLTKFDTI DDKVGAAISM TYITGQPIVF VGTGQTYADL
610
KAINVNAVVN SLMK