SRP14_MOUSE
ID SRP14_MOUSE Reviewed; 110 AA.
AC P16254; Q3TIK2;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Signal recognition particle 14 kDa protein;
DE Short=SRP14;
GN Name=Srp14;
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 PROTEIN SEQUENCE OF 1-19 AND 77-95.
RX PubMed=2557625; DOI=10.1073/pnas.86.24.9747;
RA Strub K., Walter P.;
RT "Isolation of a cDNA clone of the 14-kDa subunit of the signal recognition
RT particle by cross-hybridization of differently primed polymerase chain
RT reactions.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:9747-9751(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Hippocampus, and Spleen;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [6]
RP X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) IN COMPLEX WITH SRP9.
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:P37108}.
CC -!- SUBUNIT: Heterodimer with SRP9; binds RNA as heterodimer (By
CC similarity). Component of a signal recognition particle (SRP) complex
CC that 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:P16255, ECO:0000269|PubMed:9233785}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the SRP14 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M29264; AAA40136.1; -; mRNA.
DR EMBL; AK019310; BAB31658.1; -; mRNA.
DR EMBL; AK156845; BAE33873.1; -; mRNA.
DR EMBL; AK167821; BAE39844.1; -; mRNA.
DR EMBL; AK168144; BAE40110.1; -; mRNA.
DR EMBL; BC021537; AAH21537.1; -; mRNA.
DR CCDS; CCDS16577.1; -.
DR PIR; B34501; B34501.
DR RefSeq; NP_033299.1; NM_009273.4.
DR PDB; 1914; X-ray; 2.53 A; A=1-110.
DR PDBsum; 1914; -.
DR AlphaFoldDB; P16254; -.
DR SMR; P16254; -.
DR BioGRID; 203501; 12.
DR IntAct; P16254; 1.
DR STRING; 10090.ENSMUSP00000009693; -.
DR iPTMnet; P16254; -.
DR PhosphoSitePlus; P16254; -.
DR EPD; P16254; -.
DR jPOST; P16254; -.
DR MaxQB; P16254; -.
DR PaxDb; P16254; -.
DR PeptideAtlas; P16254; -.
DR PRIDE; P16254; -.
DR ProteomicsDB; 263345; -.
DR Antibodypedia; 5798; 157 antibodies from 26 providers.
DR DNASU; 20813; -.
DR Ensembl; ENSMUST00000009693; ENSMUSP00000009693; ENSMUSG00000009549.
DR GeneID; 20813; -.
DR KEGG; mmu:20813; -.
DR UCSC; uc008lsa.1; mouse.
DR CTD; 6727; -.
DR MGI; MGI:107169; Srp14.
DR VEuPathDB; HostDB:ENSMUSG00000009549; -.
DR eggNOG; KOG1761; Eukaryota.
DR GeneTree; ENSGT00390000008496; -.
DR HOGENOM; CLU_094309_2_1_1; -.
DR InParanoid; P16254; -.
DR OMA; RFNGHNK; -.
DR OrthoDB; 1634105at2759; -.
DR PhylomeDB; P16254; -.
DR TreeFam; TF106247; -.
DR Reactome; R-MMU-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 20813; 18 hits in 57 CRISPR screens.
DR ChiTaRS; Srp14; mouse.
DR EvolutionaryTrace; P16254; -.
DR PRO; PR:P16254; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P16254; protein.
DR Bgee; ENSMUSG00000009549; Expressed in saccule of membranous labyrinth and 262 other tissues.
DR ExpressionAtlas; P16254; baseline and differential.
DR Genevisible; P16254; MM.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; ISO:MGI.
DR GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
DR GO; GO:0030942; F:endoplasmic reticulum signal peptide binding; IEA:InterPro.
DR GO; GO:0045047; P:protein targeting to ER; ISO:MGI.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR Gene3D; 3.30.720.10; -; 1.
DR InterPro; IPR003210; Signal_recog_particle_SRP14.
DR InterPro; IPR009018; Signal_recog_particle_SRP9/14.
DR PANTHER; PTHR12013; PTHR12013; 1.
DR Pfam; PF02290; SRP14; 1.
DR SUPFAM; SSF54762; SSF54762; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; RNA-binding;
KW Signal recognition particle.
FT CHAIN 1..110
FT /note="Signal recognition particle 14 kDa protein"
FT /id="PRO_0000135191"
FT REGION 90..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT HELIX 6..19
FT /evidence="ECO:0007829|PDB:1914"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1914"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:1914"
FT STRAND 55..64
FT /evidence="ECO:0007829|PDB:1914"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:1914"
FT HELIX 76..90
FT /evidence="ECO:0007829|PDB:1914"
SQ SEQUENCE 110 AA; 12510 MW; 95EB062DBC0CCA25 CRC64;
MVLLESEQFL TELTRLFQKC RSSGSVFITL KKYDGRTKPI PRKSSVEGLE PAENKCLLRA
TDGKRKISTV VSSKEVNKFQ MAYSNLLRAN MDGLKKRDKK NKSKKSKPAQ
