ID   RS30_MOUSE              Reviewed;         133 AA.
AC   P62862; P35545; Q05472; Q642K5; Q95261; Q9JJ24;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2023, sequence version 2.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=Ubiquitin-like FUBI-ribosomal protein eS30 fusion protein {ECO:0000305};
DE   AltName: Full=FAU ubiquitin-like and ribosomal protein S30 {ECO:0000305};
DE   Contains:
DE     RecName: Full=Ubiquitin-like protein FUBI;
DE   Contains:
DE     RecName: Full=Small ribosomal subunit protein eS30;
DE     AltName: 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;
RC   TISSUE=Bone marrow, Kidney, 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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [7]
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   [8]
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   [9]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-125, 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).
RN   [10] {ECO:0007744|PDB:7CPU, ECO:0007744|PDB:7CPV}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS) OF 75-133 (40S RIBOSOMAL
RP   PROTEIN S30).
RX   PubMed=36517592; DOI=10.1038/s41586-022-05508-0;
RA   Li H., Huo Y., He X., Yao L., Zhang H., Cui Y., Xiao H., Xie W., Zhang D.,
RA   Wang Y., Zhang S., Tu H., Cheng Y., Guo Y., Cao X., Zhu Y., Jiang T.,
RA   Guo X., Qin Y., Sha J.;
RT   "A male germ-cell-specific ribosome controls male fertility.";
RL   Nature 0:0-0(2022).
CC   -!- FUNCTION: [Ubiquitin-like protein FUBI]: May have pro-apoptotic
CC       activity. {ECO:0000250|UniProtKB:P62861}.
CC   -!- FUNCTION: [Small ribosomal subunit protein eS30]: Component of the 40S
CC       subunit of the ribosome (PubMed:36517592). Contributes to the assembly
CC       and function of 40S ribosomal subunits (By similarity).
CC       {ECO:0000250|UniProtKB:P62861, ECO:0000269|PubMed:36517592}.
CC   -!- SUBUNIT: [Small ribosomal subunit protein eS30]: Component of the 40S
CC       subunit of the ribosome. {ECO:0000269|PubMed:36517592}.
CC   -!- INTERACTION:
CC       P62862; Q9CPT0: Bcl2l14; NbExp=4; IntAct=EBI-309546, EBI-8296066;
CC       P62862; Q62419: Sh3gl1; NbExp=3; IntAct=EBI-309546, EBI-642935;
CC   -!- SUBCELLULAR LOCATION: [Small ribosomal subunit protein eS30]: Nucleus
CC       {ECO:0000250|UniProtKB:P62861}. Cytoplasm
CC       {ECO:0000269|PubMed:36517592}.
CC   -!- PTM: FUBI is cleaved from ribosomal protein S30 by the deubiquitinase
CC       USP36 before the assembly of ribosomal protein S30 into pre-40S
CC       ribosomal particles. FUBI removal from ribosomal protein S30 is a
CC       crucial event for the final maturation of pre-40S particles.
CC       {ECO:0000250|UniProtKB:P62861}.
CC   -!- MISCELLANEOUS: FAU encodes a fusion protein consisting of the
CC       ubiquitin-like protein FUBI at the N terminus and ribosomal protein S30
CC       at the C terminus. {ECO:0000250|UniProtKB:P62861}.
CC   -!- MISCELLANEOUS: [Ubiquitin-like protein FUBI]: Lacks the typical lysine
CC       residues that participate in Ub's polyubiquitination. However contains
CC       a C-terminal di-glycine signature after its proteolytic separation from
CC       ribosomal protein S30 and could theoretically be conjugated onto target
CC       proteins. {ECO:0000250|UniProtKB:P62861}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic
CC       ribosomal protein eS30 family. {ECO:0000305}.
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DR   EMBL; X65922; CAA46715.1; -; mRNA.
DR   EMBL; D26610; BAA05655.1; -; mRNA.
DR   EMBL; L33715; AAA91564.1; -; Genomic_DNA.
DR   EMBL; AF147745; AAF80246.1; -; mRNA.
DR   EMBL; AK002355; BAB22034.1; -; mRNA.
DR   EMBL; AK008466; BAB25684.1; -; mRNA.
DR   EMBL; AK132752; BAE21333.1; -; mRNA.
DR   EMBL; AK151211; BAE30206.1; -; mRNA.
DR   EMBL; AK151465; BAE30423.1; -; mRNA.
DR   EMBL; AK152738; BAE31458.1; -; mRNA.
DR   EMBL; BC058691; AAH58691.1; -; mRNA.
DR   EMBL; BC062873; AAH62873.1; -; mRNA.
DR   EMBL; BC081463; AAH81463.1; -; mRNA.
DR   CCDS; CCDS29489.1; -.
DR   PIR; I48346; I48346.
DR   RefSeq; NP_001153711.1; NM_001160239.2.
DR   RefSeq; NP_001177365.1; NM_001190436.1.
DR   RefSeq; NP_032016.1; NM_007990.3.
DR   PDB; 7CPU; EM; 2.82 A; Se=75-133.
DR   PDB; 7CPV; EM; 3.03 A; Se=75-133.
DR   PDB; 7LS1; EM; 3.30 A; T3=1-133.
DR   PDB; 7LS2; EM; 3.10 A; T3=1-133.
DR   PDBsum; 7CPU; -.
DR   PDBsum; 7CPV; -.
DR   PDBsum; 7LS1; -.
DR   PDBsum; 7LS2; -.
DR   AlphaFoldDB; P62862; -.
DR   EMDB; EMD-23500; -.
DR   EMDB; EMD-23501; -.
DR   EMDB; EMD-30432; -.
DR   EMDB; EMD-30433; -.
DR   SMR; P62862; -.
DR   BioGRID; 199600; 8.
DR   ComplexPortal; CPX-5261; 40S cytosolic small ribosomal subunit.
DR   IntAct; P62862; 3.
DR   MINT; P62862; -.
DR   STRING; 10090.ENSMUSP00000136358; -.
DR   GlyGen; P62862; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P62862; -.
DR   PhosphoSitePlus; P62862; -.
DR   EPD; P62862; -.
DR   jPOST; P62862; -.
DR   MaxQB; P62862; -.
DR   PaxDb; 10090-ENSMUSP00000128416; -.
DR   PeptideAtlas; P62862; -.
DR   ProteomicsDB; 260846; -.
DR   ProteomicsDB; 298353; -.
DR   ProteomicsDB; 339100; -.
DR   Pumba; P62862; -.
DR   TopDownProteomics; P62862; -.
DR   Antibodypedia; 29676; 417 antibodies from 31 providers.
DR   DNASU; 14109; -.
DR   Ensembl; ENSMUST00000043074.14; ENSMUSP00000042835.6; ENSMUSG00000038274.14.
DR   Ensembl; ENSMUST00000178310.9; ENSMUSP00000136803.2; ENSMUSG00000038274.14.
DR   Ensembl; ENSMUST00000179142.2; ENSMUSP00000136358.2; ENSMUSG00000038274.14.
DR   Ensembl; ENSMUST00000236217.2; ENSMUSP00000157416.2; ENSMUSG00000038274.14.
DR   Ensembl; ENSMUST00000237840.2; ENSMUSP00000157878.2; ENSMUSG00000038274.14.
DR   GeneID; 14109; -.
DR   KEGG; mmu:14109; -.
DR   AGR; MGI:102547; -.
DR   CTD; 2197; -.
DR   MGI; MGI:102547; Fau.
DR   VEuPathDB; HostDB:ENSMUSG00000038274; -.
DR   eggNOG; KOG0001; Eukaryota.
DR   eggNOG; KOG0009; Eukaryota.
DR   GeneTree; ENSGT00390000007479; -.
DR   HOGENOM; CLU_010412_5_0_1; -.
DR   OMA; HCTLEVV; -.
DR   OrthoDB; 177691at2759; -.
DR   TreeFam; TF313779; -.
DR   BioGRID-ORCS; 14109; 28 hits in 62 CRISPR screens.
DR   ChiTaRS; Fau; mouse.
DR   PRO; PR:Q642K5; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   Bgee; ENSMUSG00000038274; Expressed in spleen and 65 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; NAS:ComplexPortal.
DR   GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0031386; F:protein tag activity; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
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; NAS: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:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0000028; P:ribosomal small subunit assembly; ISO:MGI.
DR   CDD; cd01793; Ubl_FUBI; 1.
DR   InterPro; IPR039415; FUBI.
DR   InterPro; IPR006846; Ribosomal_eS30.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   PANTHER; PTHR12650; 40S RIBOSOMAL PROTEIN S30/UBIQUITIN-LIKE PROTEIN FUBI; 1.
DR   PANTHER; PTHR12650:SF15; SIMILAR TO UBIQUITIN-LIKE_S30 RIBOSOMAL FUSION PROTEIN-RELATED; 1.
DR   Pfam; PF04758; Ribosomal_S30; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Nucleus; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein.
FT   CHAIN           1..133
FT                   /note="Ubiquitin-like FUBI-ribosomal protein eS30 fusion
FT                   protein"
FT                   /id="PRO_0000174000"
FT   CHAIN           1..74
FT                   /note="Ubiquitin-like protein FUBI"
FT                   /id="PRO_0000457810"
FT   CHAIN           75..133
FT                   /note="Small ribosomal subunit protein eS30"
FT                   /id="PRO_0000457811"
FT   REGION          84..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..110
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         125
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
SQ   SEQUENCE   133 AA;  14416 MW;  20B7C774A022AB16 CRC64;
     MQLFVRAQEL HTLEVTGQET VAQIKDHVAS LEGIAPEDQV VLLAGSPLED EATLGQCGVE
     ALTTLEVAGR MLGGKVHGSL ARAGKVRGQT PKVAKQEKKK KKTGRAKRRM QYNRRFVNVV
     PTFGKKKGPN ANS
//