SRPRB_MOUSE
ID SRPRB_MOUSE Reviewed; 269 AA.
AC P47758; Q544X9; Q9D872;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Signal recognition particle receptor subunit beta;
DE Short=SR-beta;
GN Name=Srprb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=7844142; DOI=10.1083/jcb.128.3.273;
RA Miller J.D., Tajima S., Lauffer L., Walter P.;
RT "The beta subunit of the signal recognition particle receptor is a
RT transmembrane GTPase that anchors the alpha subunit, a peripheral membrane
RT GTPase, to the endoplasmic reticulum membrane.";
RL J. Cell Biol. 128:273-282(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Liver, Pancreas, Pituitary, Small intestine, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 58-269 IN COMPLEX WITH SRPR;
RP MAGNESIUM IONS AND GTP, AND SUBUNIT.
RX PubMed=16439358; DOI=10.1074/jbc.m512415200;
RA Schlenker O., Hendricks A., Sinning I., Wild K.;
RT "The structure of the mammalian signal recognition particle (SRP) receptor
RT as prototype for the interaction of small GTPases with Longin domains.";
RL J. Biol. Chem. 281:8898-8906(2006).
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF 58-269 OF SIGNAL
RP RECOGNITION PARTICLE IN COMPLEX WITH THE 80S RIBOSOME AND THE SRP RECEPTOR.
RX PubMed=16675701; DOI=10.1126/science.1124864;
RA Halic M., Gartmann M., Schlenker O., Mielke T., Pool M.R., Sinning I.,
RA Beckmann R.;
RT "Signal recognition particle receptor exposes the ribosomal translocon
RT binding site.";
RL Science 312:745-747(2006).
CC -!- FUNCTION: Component of the SRP (signal recognition particle) receptor
CC (PubMed:7844142). Ensures, in conjunction with the signal recognition
CC particle, the correct targeting of the nascent secretory proteins to
CC the endoplasmic reticulum membrane system (PubMed:7844142). May mediate
CC the membrane association of SR (PubMed:7844142).
CC {ECO:0000269|PubMed:7844142}.
CC -!- SUBUNIT: Heterodimer with SRPRA. {ECO:0000269|PubMed:16439358}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O13950}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the SRP receptor beta subunit family.
CC {ECO:0000305}.
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DR EMBL; U17343; AAA69976.1; -; mRNA.
DR EMBL; AK004854; BAB23618.1; -; mRNA.
DR EMBL; AK007859; BAB25311.1; -; mRNA.
DR EMBL; AK008383; BAB25638.1; -; mRNA.
DR EMBL; AK015469; BAB29860.1; -; mRNA.
DR EMBL; AK030437; BAC26963.1; -; mRNA.
DR EMBL; AK167039; BAE39207.1; -; mRNA.
DR EMBL; BC003798; AAH03798.1; -; mRNA.
DR CCDS; CCDS23450.1; -.
DR PIR; A56487; A56487.
DR RefSeq; NP_033301.1; NM_009275.4.
DR PDB; 2FH5; X-ray; 2.45 A; B=58-269.
DR PDB; 2GO5; EM; 7.40 A; 2=58-269.
DR PDBsum; 2FH5; -.
DR PDBsum; 2GO5; -.
DR AlphaFoldDB; P47758; -.
DR SMR; P47758; -.
DR BioGRID; 203504; 7.
DR ComplexPortal; CPX-4622; Signal recognition particle receptor complex.
DR STRING; 10090.ENSMUSP00000035157; -.
DR iPTMnet; P47758; -.
DR PhosphoSitePlus; P47758; -.
DR SwissPalm; P47758; -.
DR EPD; P47758; -.
DR jPOST; P47758; -.
DR MaxQB; P47758; -.
DR PaxDb; P47758; -.
DR PeptideAtlas; P47758; -.
DR PRIDE; P47758; -.
DR TopDownProteomics; P47758; -.
DR Antibodypedia; 2504; 365 antibodies from 24 providers.
DR DNASU; 20818; -.
DR Ensembl; ENSMUST00000035157; ENSMUSP00000035157; ENSMUSG00000032553.
DR GeneID; 20818; -.
DR KEGG; mmu:20818; -.
DR UCSC; uc009rgg.1; mouse.
DR CTD; 58477; -.
DR MGI; MGI:102964; Srprb.
DR VEuPathDB; HostDB:ENSMUSG00000032553; -.
DR eggNOG; KOG0090; Eukaryota.
DR GeneTree; ENSGT00940000154388; -.
DR HOGENOM; CLU_046625_2_0_1; -.
DR InParanoid; P47758; -.
DR OMA; NKQDVAM; -.
DR OrthoDB; 1503159at2759; -.
DR PhylomeDB; P47758; -.
DR TreeFam; TF106190; -.
DR BRENDA; 3.6.5.4; 3474.
DR BioGRID-ORCS; 20818; 9 hits in 41 CRISPR screens.
DR ChiTaRS; Srprb; mouse.
DR EvolutionaryTrace; P47758; -.
DR PRO; PR:P47758; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P47758; protein.
DR Bgee; ENSMUSG00000032553; Expressed in saccule of membranous labyrinth and 259 other tissues.
DR ExpressionAtlas; P47758; baseline and differential.
DR Genevisible; P47758; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005785; C:signal recognition particle receptor complex; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0045047; P:protein targeting to ER; IBA:GO_Central.
DR GO; GO:0006617; P:SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition; IC:ComplexPortal.
DR CDD; cd04105; SR_beta; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR019009; SRP_receptor_beta_su.
DR PANTHER; PTHR11485:SF34; PTHR11485:SF34; 1.
DR Pfam; PF09439; SRPRB; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; GTP-binding; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..269
FT /note="Signal recognition particle receptor subunit beta"
FT /id="PRO_0000101228"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 69..77
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16439358"
FT BINDING 90..93
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16439358"
FT BINDING 118
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16439358"
FT BINDING 178..181
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16439358"
FT BINDING 246
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:16439358"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5M8"
FT MOD_RES 212
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5M8"
FT CONFLICT 16
FT /note="A -> P (in Ref. 2; BAB25638)"
FT /evidence="ECO:0000305"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:2FH5"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:2FH5"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:2FH5"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:2FH5"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:2FH5"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:2FH5"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:2FH5"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:2FH5"
FT HELIX 146..165
FT /evidence="ECO:0007829|PDB:2FH5"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:2FH5"
FT HELIX 188..205
FT /evidence="ECO:0007829|PDB:2FH5"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:2FH5"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:2FH5"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:2FH5"
FT HELIX 259..268
FT /evidence="ECO:0007829|PDB:2FH5"
SQ SEQUENCE 269 AA; 29579 MW; 041175FA6891DA37 CRC64;
MASANTRRVG DGAGGAFQPY LDSLRQELQQ RDPTLLSVAV ALLAVLLTLV FWKFIWSRKS
SQRAVLFVGL CDSGKTLLFV RLLTGQYRDT QTSITDSSAI YKVNNNRGNS LTLIDLPGHE
SLRFQLLDRF KSSARAVVFV VDSAAFQREV KDVAEFLYQV LIDSMALKNS PSLLIACNKQ
DIAMAKSAKL IQQQLEKELN TLRVTRSAAP STLDSSSTAP AQLGKKGKEF EFSQLPLKVE
FLECSAKGGR GDTGSADIQD LEKWLAKIA
