(data stored in ACNUC13479 zone)

SWISSPROT: 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   05-JUL-2017, entry version 138.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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
RT   membrane 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: 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)
RT   receptor as prototype for the interaction of small GTPases with Longin
RT   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
RP   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)
CC       receptor. Ensures, in conjunction with the signal recognition
CC       particle, the correct targeting of the nascent secretory proteins
CC       to the endoplasmic reticulum membrane system. Has GTPase activity.
CC       May mediate the membrane association of SRPR.
CC   -!- SUBUNIT: Heterodimer with SRPRA. {ECO:0000269|PubMed:16439358}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SRP receptor beta subunit family.
CC       {ECO:0000305}.
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   UniGene; Mm.273053; -.
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   ProteinModelPortal; P47758; -.
DR   SMR; P47758; -.
DR   IntAct; P47758; 1.
DR   MINT; MINT-1844750; -.
DR   STRING; 10090.ENSMUSP00000035157; -.
DR   iPTMnet; P47758; -.
DR   PhosphoSitePlus; P47758; -.
DR   SwissPalm; P47758; -.
DR   EPD; P47758; -.
DR   MaxQB; P47758; -.
DR   PaxDb; P47758; -.
DR   PeptideAtlas; P47758; -.
DR   PRIDE; P47758; -.
DR   TopDownProteomics; P47758; -.
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   eggNOG; KOG0090; Eukaryota.
DR   eggNOG; COG2229; LUCA.
DR   GeneTree; ENSGT00510000048347; -.
DR   HOGENOM; HOG000241847; -.
DR   HOVERGEN; HBG054206; -.
DR   InParanoid; P47758; -.
DR   KO; K12272; -.
DR   OrthoDB; EOG091G0242; -.
DR   PhylomeDB; P47758; -.
DR   TreeFam; TF106190; -.
DR   EvolutionaryTrace; P47758; -.
DR   PRO; PR:P47758; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   Bgee; ENSMUSG00000032553; -.
DR   CleanEx; MM_SRPRB; -.
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:0005047; F:signal recognition particle binding; IBA:GO_Central.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   CDD; cd04105; SR_beta; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR024156; Small_GTPase_ARF.
DR   InterPro; IPR019009; SRP_receptor_beta_su.
DR   Pfam; PF09439; SRPRB; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P47758.
DR   SWISS-2DPAGE; P47758.
KW   3D-structure; Complete proteome; Endoplasmic reticulum; GTP-binding;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN         1    269       Signal recognition particle receptor
FT                                subunit beta.
FT                                /FTId=PRO_0000101228.
FT   TRANSMEM     35     55       Helical. {ECO:0000255}.
FT   NP_BIND      69     77       GTP. {ECO:0000269|PubMed:16439358}.
FT   NP_BIND      90     93       GTP. {ECO:0000269|PubMed:16439358}.
FT   NP_BIND     178    181       GTP. {ECO:0000269|PubMed:16439358}.
FT   BINDING     118    118       GTP; via amide nitrogen.
FT                                {ECO:0000269|PubMed:16439358}.
FT   BINDING     246    246       GTP; via amide nitrogen.
FT                                {ECO:0000269|PubMed:16439358}.
FT   MOD_RES     110    110       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9Y5M8}.
FT   MOD_RES     212    212       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q9Y5M8}.
FT   CONFLICT     16     16       A -> P (in Ref. 2; BAB25638).
FT                                {ECO:0000305}.
FT   STRAND       64     68       {ECO:0000244|PDB:2FH5}.
FT   HELIX        75     84       {ECO:0000244|PDB:2FH5}.
FT   STRAND       97    102       {ECO:0000244|PDB:2FH5}.
FT   STRAND      110    115       {ECO:0000244|PDB:2FH5}.
FT   HELIX       120    130       {ECO:0000244|PDB:2FH5}.
FT   HELIX       131    133       {ECO:0000244|PDB:2FH5}.
FT   STRAND      134    142       {ECO:0000244|PDB:2FH5}.
FT   TURN        143    145       {ECO:0000244|PDB:2FH5}.
FT   HELIX       146    165       {ECO:0000244|PDB:2FH5}.
FT   STRAND      172    178       {ECO:0000244|PDB:2FH5}.
FT   HELIX       188    205       {ECO:0000244|PDB:2FH5}.
FT   HELIX       232    234       {ECO:0000244|PDB:2FH5}.
FT   STRAND      235    237       {ECO:0000244|PDB:2FH5}.
FT   STRAND      239    243       {ECO:0000244|PDB:2FH5}.
FT   HELIX       259    268       {ECO:0000244|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
//

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