RSSA_CANAL
ID RSSA_CANAL Reviewed; 261 AA.
AC O42817; A0A1D8PK64; Q59YU8; Q9P8C6;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=40S ribosomal protein S0 {ECO:0000255|HAMAP-Rule:MF_03015};
GN Name=RPS0 {ECO:0000255|HAMAP-Rule:MF_03015}; Synonyms=YST1;
GN OrderedLocusNames=CAALFM_C305370CA; ORFNames=CaO19.6975;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 26555;
RX PubMed=9579059; DOI=10.1099/00221287-144-4-839;
RA Montero M., Marcilla A., Sentandreu R., Valentin E.;
RT "A Candida albicans 37 kDa polypeptide with homology to the laminin
RT receptor is a component of the translational machinery.";
RL Microbiology 144:839-847(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RA Montero M., Ramon A.M., Valentin-Gomez E., Sentandreu R.;
RT "Characterization of CaYST1,a gene of Candida albicans implicated in
RT filamentation.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [6]
RP FUNCTION.
RX PubMed=8300236; DOI=10.1128/iai.62.2.742-746.1994;
RA Lopez-Ribot J.L., Casanova M., Monteagudo C., Sepulveda P., Martinez J.P.;
RT "Evidence for the presence of a high-affinity laminin receptor-like
RT molecule on the surface of Candida albicans yeast cells.";
RL Infect. Immun. 62:742-746(1994).
CC -!- FUNCTION: Required for the assembly and/or stability of the 40S
CC ribosomal subunit. Required for the processing of the 20S rRNA-
CC precursor to mature 18S rRNA in a late step of the maturation of 40S
CC ribosomal subunits. {ECO:0000255|HAMAP-Rule:MF_03015,
CC ECO:0000269|PubMed:8300236, ECO:0000269|Ref.2}.
CC -!- SUBUNIT: Component of the small ribosomal subunit. Mature ribosomes
CC consist of a small (40S) and a large (60S) subunit. The 40S subunit
CC contains about 33 different proteins and 1 molecule of RNA (18S). The
CC 60S subunit contains about 49 different proteins and 3 molecules of RNA
CC (25S, 5.8S and 5S). Interacts with RPS21. {ECO:0000255|HAMAP-
CC Rule:MF_03015}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: This protein appears to have acquired a second function
CC as a laminin receptor specifically in the vertebrate lineage. A 67 kDa
CC form similar to the human laminin receptor (67LR) has been isolated
CC from the cell walls of blastoconidia, but it does not bind laminin.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC {ECO:0000255|HAMAP-Rule:MF_03015}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA72242.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Y11434; CAA72242.1; ALT_FRAME; mRNA.
DR EMBL; AJ251858; CAB77627.1; -; Genomic_DNA.
DR EMBL; CP017625; AOW28551.1; -; Genomic_DNA.
DR RefSeq; XP_019330874.1; XM_019475329.1.
DR AlphaFoldDB; O42817; -.
DR SMR; O42817; -.
DR BioGRID; 1226772; 2.
DR STRING; 237561.O42817; -.
DR PRIDE; O42817; -.
DR GeneID; 3643678; -.
DR KEGG; cal:CAALFM_C305370CA; -.
DR CGD; CAL0000191976; YST1.
DR VEuPathDB; FungiDB:C3_05370C_A; -.
DR eggNOG; KOG0830; Eukaryota.
DR HOGENOM; CLU_058171_2_0_1; -.
DR InParanoid; O42817; -.
DR OMA; ENKMKRY; -.
DR OrthoDB; 1129610at2759; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:CGD.
DR GO; GO:0005840; C:ribosome; IDA:CGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IGI:CGD.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR GO; GO:0006412; P:translation; IGI:CGD.
DR CDD; cd01425; RPS2; 1.
DR HAMAP; MF_03015; Ribosomal_S2_euk; 1.
DR InterPro; IPR001865; Ribosomal_S2.
DR InterPro; IPR018130; Ribosomal_S2_CS.
DR InterPro; IPR027498; Ribosomal_S2_euk.
DR InterPro; IPR005707; Ribosomal_S2_euk/arc.
DR InterPro; IPR023591; Ribosomal_S2_flav_dom_sf.
DR PANTHER; PTHR11489; PTHR11489; 1.
DR Pfam; PF00318; Ribosomal_S2; 2.
DR PRINTS; PR00395; RIBOSOMALS2.
DR SUPFAM; SSF52313; SSF52313; 1.
DR TIGRFAMs; TIGR01012; uS2_euk_arch; 1.
DR PROSITE; PS00962; RIBOSOMAL_S2_1; 1.
DR PROSITE; PS00963; RIBOSOMAL_S2_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03015"
FT CHAIN 2..261
FT /note="40S ribosomal protein S0"
FT /id="PRO_0000134365"
FT REGION 217..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..241
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03015"
FT CONFLICT 150
FT /note="D -> Q (in Ref. 1; CAA72242)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="S -> C (in Ref. 1; CAA72242)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="E -> G (in Ref. 1; CAA72242)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="E -> G (in Ref. 1; CAA72242)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="N -> I (in Ref. 1; CAA72242)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 261 AA; 28730 MW; 17886B880D1A191C CRC64;
MSLPASFDLT PEDAKLLLAA NVHLGAKNVQ VHNKPYVYKT RPDGMNIINI GKTWEKIVLA
ARIIAAVPNA SDVAVCSSRT FGQRAVLKFA AHTGATAIAG RFTPGNFTNY ITRSFKEPRL
VVVTDPRTDA QAIKESSYVN IPVIALTDMD SPSEYVDVAI PCNNKGKHSI GLIWWLLARE
VLRLRGIIPD RTTEWSVMPD LYFYRDPEEI EQNAVEEAKT EEVEEAPVAE AETEWTGETE
DVDWADSGAT PAAEDAAASN W
