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Protein

Signal recognition particle receptor subunit beta

Gene

Srprb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the SRP (signal recognition particle) receptor. Ensures, in conjunction with the signal recognition particle, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system. Has GTPase activity. May mediate the membrane association of SRPR.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei118 – 1181GTP; via amide nitrogen1 Publication
Binding sitei246 – 2461GTP; via amide nitrogen1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi69 – 779GTP1 Publication
Nucleotide bindingi90 – 934GTP1 Publication
Nucleotide bindingi178 – 1814GTP1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Signal recognition particle receptor subunit beta
Short name:
SR-beta
Gene namesi
Name:Srprb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:102964. Srprb.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei35 – 5521HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 269269Signal recognition particle receptor subunit betaPRO_0000101228Add
BLAST

Proteomic databases

EPDiP47758.
MaxQBiP47758.
PaxDbiP47758.
PRIDEiP47758.
TopDownProteomicsiP47758.

PTM databases

iPTMnetiP47758.
PhosphoSiteiP47758.
SwissPalmiP47758.

Expressioni

Gene expression databases

BgeeiP47758.
CleanExiMM_SRPRB.
GenevisibleiP47758. MM.

Interactioni

Subunit structurei

Heterodimer with SRPRA.1 Publication

Protein-protein interaction databases

IntActiP47758. 1 interaction.
MINTiMINT-1844750.
STRINGi10090.ENSMUSP00000035157.

Structurei

Secondary structure

1
269
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi64 – 685Combined sources
Helixi75 – 8410Combined sources
Beta strandi97 – 1026Combined sources
Beta strandi110 – 1156Combined sources
Helixi120 – 13011Combined sources
Helixi131 – 1333Combined sources
Beta strandi134 – 1429Combined sources
Turni143 – 1453Combined sources
Helixi146 – 16520Combined sources
Beta strandi172 – 1787Combined sources
Helixi188 – 20518Combined sources
Helixi232 – 2343Combined sources
Beta strandi235 – 2373Combined sources
Beta strandi239 – 2435Combined sources
Helixi259 – 26810Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FH5X-ray2.45B58-269[»]
2GO5electron microscopy7.40258-269[»]
ProteinModelPortaliP47758.
SMRiP47758. Positions 63-269.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP47758.

Family & Domainsi

Sequence similaritiesi

Belongs to the SRP receptor beta subunit family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0090. Eukaryota.
COG2229. LUCA.
GeneTreeiENSGT00510000048347.
HOGENOMiHOG000241847.
HOVERGENiHBG054206.
InParanoidiP47758.
KOiK12272.
OrthoDBiEOG7D59N7.
PhylomeDBiP47758.
TreeFamiTF106190.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR024156. Small_GTPase_ARF.
IPR019009. SRP_receptor_beta_su.
[Graphical view]
PfamiPF09439. SRPRB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequencei

Sequence statusi: Complete.

P47758-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASANTRRVG DGAGGAFQPY LDSLRQELQQ RDPTLLSVAV ALLAVLLTLV
60 70 80 90 100
FWKFIWSRKS SQRAVLFVGL CDSGKTLLFV RLLTGQYRDT QTSITDSSAI
110 120 130 140 150
YKVNNNRGNS LTLIDLPGHE SLRFQLLDRF KSSARAVVFV VDSAAFQREV
160 170 180 190 200
KDVAEFLYQV LIDSMALKNS PSLLIACNKQ DIAMAKSAKL IQQQLEKELN
210 220 230 240 250
TLRVTRSAAP STLDSSSTAP AQLGKKGKEF EFSQLPLKVE FLECSAKGGR
260
GDTGSADIQD LEKWLAKIA
Length:269
Mass (Da):29,579
Last modified:February 1, 1996 - v1
Checksum:i041175FA6891DA37
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161A → P in BAB25638 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17343 mRNA. Translation: AAA69976.1.
AK004854 mRNA. Translation: BAB23618.1.
AK007859 mRNA. Translation: BAB25311.1.
AK008383 mRNA. Translation: BAB25638.1.
AK015469 mRNA. Translation: BAB29860.1.
AK030437 mRNA. Translation: BAC26963.1.
AK167039 mRNA. Translation: BAE39207.1.
BC003798 mRNA. Translation: AAH03798.1.
CCDSiCCDS23450.1.
PIRiA56487.
RefSeqiNP_033301.1. NM_009275.4.
UniGeneiMm.273053.

Genome annotation databases

EnsembliENSMUST00000035157; ENSMUSP00000035157; ENSMUSG00000032553.
GeneIDi20818.
KEGGimmu:20818.
UCSCiuc009rgg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17343 mRNA. Translation: AAA69976.1.
AK004854 mRNA. Translation: BAB23618.1.
AK007859 mRNA. Translation: BAB25311.1.
AK008383 mRNA. Translation: BAB25638.1.
AK015469 mRNA. Translation: BAB29860.1.
AK030437 mRNA. Translation: BAC26963.1.
AK167039 mRNA. Translation: BAE39207.1.
BC003798 mRNA. Translation: AAH03798.1.
CCDSiCCDS23450.1.
PIRiA56487.
RefSeqiNP_033301.1. NM_009275.4.
UniGeneiMm.273053.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FH5X-ray2.45B58-269[»]
2GO5electron microscopy7.40258-269[»]
ProteinModelPortaliP47758.
SMRiP47758. Positions 63-269.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP47758. 1 interaction.
MINTiMINT-1844750.
STRINGi10090.ENSMUSP00000035157.

PTM databases

iPTMnetiP47758.
PhosphoSiteiP47758.
SwissPalmiP47758.

Proteomic databases

EPDiP47758.
MaxQBiP47758.
PaxDbiP47758.
PRIDEiP47758.
TopDownProteomicsiP47758.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035157; ENSMUSP00000035157; ENSMUSG00000032553.
GeneIDi20818.
KEGGimmu:20818.
UCSCiuc009rgg.1. mouse.

Organism-specific databases

CTDi58477.
MGIiMGI:102964. Srprb.

Phylogenomic databases

eggNOGiKOG0090. Eukaryota.
COG2229. LUCA.
GeneTreeiENSGT00510000048347.
HOGENOMiHOG000241847.
HOVERGENiHBG054206.
InParanoidiP47758.
KOiK12272.
OrthoDBiEOG7D59N7.
PhylomeDBiP47758.
TreeFamiTF106190.

Miscellaneous databases

EvolutionaryTraceiP47758.
PROiP47758.
SOURCEiSearch...

Gene expression databases

BgeeiP47758.
CleanExiMM_SRPRB.
GenevisibleiP47758. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR024156. Small_GTPase_ARF.
IPR019009. SRP_receptor_beta_su.
[Graphical view]
PfamiPF09439. SRPRB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The beta subunit of the signal recognition particle receptor is a transmembrane GTPase that anchors the alpha subunit, a peripheral membrane GTPase, to the endoplasmic reticulum membrane."
    Miller J.D., Tajima S., Lauffer L., Walter P.
    J. Cell Biol. 128:273-282(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver, Pancreas, Pituitary, Small intestine and Testis.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  4. "The structure of the mammalian signal recognition particle (SRP) receptor as prototype for the interaction of small GTPases with Longin domains."
    Schlenker O., Hendricks A., Sinning I., Wild K.
    J. Biol. Chem. 281:8898-8906(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 58-269 IN COMPLEX WITH SRPR; MAGNESIUM IONS AND GTP, SUBUNIT.
  5. "Signal recognition particle receptor exposes the ribosomal translocon binding site."
    Halic M., Gartmann M., Schlenker O., Mielke T., Pool M.R., Sinning I., Beckmann R.
    Science 312:745-747(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF 58-269 OF SIGNAL RECOGNITION PARTICLE IN COMPLEX WITH THE 80S RIBOSOME AND THE SRP RECEPTOR.

Entry informationi

Entry nameiSRPRB_MOUSE
AccessioniPrimary (citable) accession number: P47758
Secondary accession number(s): Q544X9, Q9D872
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 8, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.