ID   RLA1_ARTSA              Reviewed;         110 AA.
AC   P02402;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=60S acidic ribosomal protein P1;
DE   AltName: Full=eL12'/ eL12'-P;
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 OF 2-110.
RA   Amons R., Pluijms W.J.M., Kriek J., Moeller W.;
RT   "The primary structure of protein eL12'/eL12'-P from the large subunit of
RT   Artemia salina ribosomes.";
RL   FEBS Lett. 146:143-147(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-107, AND PHOSPHORYLATION AT SER-97.
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   -!- PTM: Phosphorylation of Ser-97 converts eL12' to eL12'-P.
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=11440.38; Mass_error=1.39; 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; X02633; CAA26480.1; -; mRNA.
DR   PIR; B25208; R6SSP2.
DR   AlphaFoldDB; P02402; -.
DR   SMR; P02402; -.
DR   iPTMnet; P02402; -.
DR   GO; GO:0022626; C:cytosolic ribosome; IEA:UniProt.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006414; P:translational elongation; IEA:InterPro.
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; IPR001859; T.cruzi_P2-like.
DR   PRINTS; PR00456; RIBOSOMALP2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Phosphoprotein; Ribonucleoprotein;
KW   Ribosomal protein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.1"
FT   CHAIN           2..110
FT                   /note="60S acidic ribosomal protein P1"
FT                   /id="PRO_0000157689"
FT   REGION          69..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..110
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="Blocked amino end (Ala)"
FT                   /evidence="ECO:0000269|Ref.1"
FT   MOD_RES         97
FT                   /note="Phosphoserine; in form eL12'-P"
FT                   /evidence="ECO:0000269|PubMed:3839187"
FT   CONFLICT        9
FT                   /note="Missing (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        22
FT                   /note="D -> V (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        43
FT                   /note="W -> S (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   110 AA;  11538 MW;  639769BA2EC65E8D CRC64;
     MASKDELACV YAALILLDDD VDITTEKVNT ILRAAGVSVE PYWPGLFTKA LEGLDLKSMI
     TNVGSGVGAA PAAGGAAAAT EAPAAKEEKK EEKKEESEEE DEDMGFGLFD