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SRP09_MOUSE
ID   SRP09_MOUSE             Reviewed;          86 AA.
AC   P49962; Q9D085;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 168.
DE   RecName: Full=Signal recognition particle 9 kDa protein;
DE            Short=SRP9;
GN   Name=Srp9;
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].
RX   PubMed=7518078; DOI=10.1093/nar/22.11.2028;
RA   Bovia F., Bui N., Strub K.;
RT   "The heterodimeric subunit SRP9/14 of the signal recognition particle
RT   functions as permuted single polypeptide chain.";
RL   Nucleic Acids Res. 22:2028-2035(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Urinary bladder;
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=FVB/N; 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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) IN COMPLEX WITH SRP14.
RX   PubMed=9233785; DOI=10.1093/emboj/16.13.3757;
RA   Birse D.E., Kapp U., Strub K., Cusack S., Aaberg A.;
RT   "The crystal structure of the signal recognition particle Alu RNA binding
RT   heterodimer, SRP9/14.";
RL   EMBO J. 16:3757-3766(1997).
CC   -!- FUNCTION: Component of the signal recognition particle (SRP) complex, a
CC       ribonucleoprotein complex that mediates the cotranslational targeting
CC       of secretory and membrane proteins to the endoplasmic reticulum (ER)
CC       (By similarity). SRP9 together with SRP14 and the Alu portion of the
CC       SRP RNA, constitutes the elongation arrest domain of SRP (By
CC       similarity). The complex of SRP9 and SRP14 is required for SRP RNA
CC       binding (By similarity). {ECO:0000250|UniProtKB:P21262}.
CC   -!- SUBUNIT: Heterodimer with SRP14; binds RNA as heterodimer (By
CC       similarity). Component of a signal recognition particle complex that
CC       consists of a 7SL RNA molecule of 300 nucleotides and six protein
CC       subunits: SRP72, SRP68, SRP54, SRP19, SRP14 and SRP9 (PubMed:9233785).
CC       {ECO:0000250|UniProtKB:P21262, ECO:0000269|PubMed:9233785}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the SRP9 family. {ECO:0000305}.
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DR   EMBL; X78304; CAA55114.1; -; mRNA.
DR   EMBL; AK011720; BAB27800.1; -; mRNA.
DR   EMBL; AK020583; BAB32138.1; -; mRNA.
DR   EMBL; AK020620; BAB32151.1; -; mRNA.
DR   EMBL; BC039648; AAH39648.1; -; mRNA.
DR   CCDS; CCDS35812.1; -.
DR   PIR; S57500; S57500.
DR   RefSeq; NP_036188.1; NM_012058.3.
DR   PDB; 1914; X-ray; 2.53 A; A=1-86.
DR   PDBsum; 1914; -.
DR   AlphaFoldDB; P49962; -.
DR   SMR; P49962; -.
DR   BioGRID; 205113; 10.
DR   IntAct; P49962; 1.
DR   STRING; 10090.ENSMUSP00000027792; -.
DR   iPTMnet; P49962; -.
DR   PhosphoSitePlus; P49962; -.
DR   SwissPalm; P49962; -.
DR   EPD; P49962; -.
DR   jPOST; P49962; -.
DR   PaxDb; P49962; -.
DR   PeptideAtlas; P49962; -.
DR   PRIDE; P49962; -.
DR   ProteomicsDB; 263344; -.
DR   Antibodypedia; 47125; 90 antibodies from 19 providers.
DR   DNASU; 27058; -.
DR   Ensembl; ENSMUST00000027792; ENSMUSP00000027792; ENSMUSG00000026511.
DR   GeneID; 27058; -.
DR   KEGG; mmu:27058; -.
DR   UCSC; uc007dxu.2; mouse.
DR   CTD; 6726; -.
DR   MGI; MGI:1350930; Srp9.
DR   VEuPathDB; HostDB:ENSMUSG00000026511; -.
DR   eggNOG; KOG3465; Eukaryota.
DR   GeneTree; ENSGT00390000018505; -.
DR   InParanoid; P49962; -.
DR   OMA; YINSWEE; -.
DR   OrthoDB; 1623953at2759; -.
DR   PhylomeDB; P49962; -.
DR   TreeFam; TF106246; -.
DR   Reactome; R-MMU-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   BioGRID-ORCS; 27058; 21 hits in 71 CRISPR screens.
DR   ChiTaRS; Srp9; mouse.
DR   EvolutionaryTrace; P49962; -.
DR   PRO; PR:P49962; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; P49962; protein.
DR   Bgee; ENSMUSG00000026511; Expressed in supraoptic nucleus and 257 other tissues.
DR   ExpressionAtlas; P49962; baseline and differential.
DR   Genevisible; P49962; MM.
DR   GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IBA:GO_Central.
DR   GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
DR   GO; GO:0045900; P:negative regulation of translational elongation; IEA:InterPro.
DR   GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IBA:GO_Central.
DR   Gene3D; 3.30.720.10; -; 1.
DR   InterPro; IPR008832; Signal_recog_particle_SRP9.
DR   InterPro; IPR009018; Signal_recog_particle_SRP9/14.
DR   InterPro; IPR039914; SRP9.
DR   InterPro; IPR039432; SRP9_dom.
DR   PANTHER; PTHR12834; PTHR12834; 1.
DR   Pfam; PF05486; SRP9-21; 1.
DR   PIRSF; PIRSF017029; Signal_recog_particle_SRP9; 1.
DR   SUPFAM; SSF54762; SSF54762; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Reference proteome; Ribonucleoprotein;
KW   RNA-binding; Signal recognition particle.
FT   CHAIN           1..86
FT                   /note="Signal recognition particle 9 kDa protein"
FT                   /id="PRO_0000135183"
FT   CONFLICT        22
FT                   /note="P -> S (in Ref. 2; BAB27800)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   86 AA;  10194 MW;  655860497132AD2C CRC64;
     MPQFQTWEEF SRAAEKLYLA DPMKVRVVLK YRHVDGNLCI KVTDDLVCLV YRTDQAQDVK
     KIEKFHSQLM RLMVAKESRN VTMETE
 
 
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