RS30_MOUSE
ID RS30_MOUSE Reviewed; 59 AA.
AC P62862; Q05472; Q95261; Q9JJ24;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=40S ribosomal protein S30;
GN Name=Fau;
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].
RC STRAIN=SWR/J;
RX PubMed=8395683;
RA Michiels L., van der Rauwelaert E., van Hasselt F., Kas K., Merregaert J.;
RT "fau cDNA encodes a ubiquitin-like-S30 fusion protein and is expressed as
RT an antisense sequence in the Finkel-Biskis-Reilly murine sarcoma virus.";
RL Oncogene 8:2537-2546(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=7724584; DOI=10.1073/pnas.92.8.3463;
RA Nakamura M., Xavier R.M., Tsunematsu T., Tanigawa Y.;
RT "Molecular cloning and characterization of a cDNA encoding monoclonal
RT nonspecific suppressor factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3463-3467(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=7774934; DOI=10.1016/0888-7543(95)80140-h;
RA Casteels D., Poirier C., Guenet J.-L., Merregaert J.;
RT "The mouse Fau gene: genomic structure, chromosomal localization, and
RT characterization of two retropseudogenes.";
RL Genomics 25:291-294(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Swiss OB;
RA Nie G.-Y., Li Y., Salamonsen L.A., Clements J.A., Findlay J.K.;
RT "Identification of monoclonal non-specific suppressor factor beta as one of
RT the genes differentially expressed at implantation sites compared to
RT interimplantation sites in the mouse uterus.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Small intestine;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Pancreas, and Spleen;
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 [8]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-51, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- MISCELLANEOUS: This ribosomal protein is synthesized as a C-terminal
CC extension protein (CEP) of a ubiquitin-like protein.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS30 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA91564.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAF80246.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH58691.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH62873.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA05655.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB22034.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB25684.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA46715.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X65922; CAA46715.1; ALT_INIT; mRNA.
DR EMBL; D26610; BAA05655.1; ALT_INIT; mRNA.
DR EMBL; L33715; AAA91564.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF147745; AAF80246.1; ALT_INIT; mRNA.
DR EMBL; AK002355; BAB22034.1; ALT_INIT; mRNA.
DR EMBL; AK008466; BAB25684.1; ALT_INIT; mRNA.
DR EMBL; BC058691; AAH58691.1; ALT_INIT; mRNA.
DR EMBL; BC062873; AAH62873.1; ALT_INIT; mRNA.
DR PIR; I48346; I48346.
DR AlphaFoldDB; P62862; -.
DR SMR; P62862; -.
DR ComplexPortal; CPX-5261; 40S cytosolic small ribosomal subunit.
DR iPTMnet; P62862; -.
DR PhosphoSitePlus; P62862; -.
DR EPD; P62862; -.
DR jPOST; P62862; -.
DR MaxQB; P62862; -.
DR PeptideAtlas; P62862; -.
DR PRIDE; P62862; -.
DR ProteomicsDB; 260846; -.
DR TopDownProteomics; P62862; -.
DR MGI; MGI:102547; Fau.
DR ChiTaRS; Fau; mouse.
DR Proteomes; UP000000589; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0019731; P:antibacterial humoral response; ISO:MGI.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0002227; P:innate immune response in mucosa; ISO:MGI.
DR GO; GO:0000028; P:ribosomal small subunit assembly; ISO:MGI.
DR InterPro; IPR006846; Ribosomal_S30.
DR Pfam; PF04758; Ribosomal_S30; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..59
FT /note="40S ribosomal protein S30"
FT /id="PRO_0000174000"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 59 AA; 6648 MW; 012AC1FB555B01A4 CRC64;
KVHGSLARAG KVRGQTPKVA KQEKKKKKTG RAKRRMQYNR RFVNVVPTFG KKKGPNANS
