ID   RLA2_ARTSA              Reviewed;         111 AA.
AC   P02399;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=60S acidic ribosomal protein P2;
DE   AltName: Full=EL12;
OS   Artemia salina (Brine shrimp).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Anostraca; Artemiidae; Artemia.
OX   NCBI_TaxID=85549;
RN   [1]
RP   PROTEIN SEQUENCE, AND PHOSPHORYLATION AT SER-98.
RX   PubMed=477981; DOI=10.1016/0014-5793(79)81089-3;
RA   Amons R., Pluijms W.J.M., Moeller W.;
RT   "The primary structure of ribosomal protein eL12/eL12-P from Artemia salina
RT   80 S ribosomes.";
RL   FEBS Lett. 104:85-89(1979).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-108.
RX   PubMed=3839187; DOI=10.1111/j.1432-1033.1985.tb08968.x;
RA   Maassen J.A., Schop E.N., Brands J.H.G.M., van Hemert F.J., Lenstra J.A.,
RA   Moeller W.;
RT   "Molecular cloning and analysis of cDNA sequences for two ribosomal
RT   proteins from Artemia. The coordinate expression of genes for ribosomal
RT   proteins and elongation factor 1 during embryogenesis of Artemia.";
RL   Eur. J. Biochem. 149:609-616(1985).
RN   [3]
RP   SUBUNIT, STOICHIOMETRY, AND MASS SPECTROMETRY.
RX   PubMed=20467040; DOI=10.1074/mcp.m000072-mcp201;
RA   Gordiyenko Y., Videler H., Zhou M., McKay A.R., Fucini P., Biegel E.,
RA   Muller V., Robinson C.V.;
RT   "Mass spectrometry defines the stoichiometry of ribosomal stalk complexes
RT   across the phylogenetic tree.";
RL   Mol. Cell. Proteomics 9:1774-1783(2010).
CC   -!- FUNCTION: Plays an important role in the elongation step of protein
CC       synthesis.
CC   -!- SUBUNIT: Part of the ribosomal stalk of the large ribosomal subunit; P1
CC       and P2 exist as dimers which assemble on the P0 scaffold.
CC       {ECO:0000269|PubMed:20467040}.
CC   -!- MASS SPECTROMETRY: Mass=80479.25; Mass_error=9.3; Method=Electrospray;
CC       Note=Isolated P0(P1/P2)4.; Evidence={ECO:0000269|PubMed:20467040};
CC   -!- MASS SPECTROMETRY: Mass=11522.16; Mass_error=0.7; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:20467040};
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC       {ECO:0000305}.
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DR   EMBL; X02632; CAA26479.1; -; mRNA.
DR   PIR; A25208; R8SS12.
DR   AlphaFoldDB; P02399; -.
DR   SMR; P02399; -.
DR   iPTMnet; P02399; -.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0002182; P:cytoplasmic translational elongation; IEA:InterPro.
DR   CDD; cd05833; Ribosomal_P2; 1.
DR   Gene3D; 1.10.10.1410; -; 1.
DR   HAMAP; MF_01478; Ribosomal_L12_arch; 1.
DR   InterPro; IPR038716; P1/P2_N_sf.
DR   InterPro; IPR027534; Ribosomal_L12/P1/P2.
DR   InterPro; IPR044076; Ribosomal_P2.
DR   InterPro; IPR001859; T.cruzi_P2-like.
DR   PANTHER; PTHR21141; PTHR21141; 1.
DR   PRINTS; PR00456; RIBOSOMALP2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Phosphoprotein; Ribonucleoprotein;
KW   Ribosomal protein.
FT   CHAIN           1..111
FT                   /note="60S acidic ribosomal protein P2"
FT                   /id="PRO_0000157645"
FT   REGION          63..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..111
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         98
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:477981"
FT   CONFLICT        19
FT                   /note="S -> T (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        80
FT                   /note="T -> A (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   111 AA;  11503 MW;  69C4241E1FAF4E01 CRC64;
     MRYVAAYLLA ALSGNADPST ADIEKILSSV GIECNPSQLQ KVMNELKGKD LEALIAEGQT
     KLASMPTGGA PAAAAGGAAT APAAEAKEAK KEEKKEESEE EDEDMGFGLF D