ID   RL403_CHLRE             Reviewed;         128 AA.
AC   P0CH10; P14624; P14695;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Ubiquitin-60S ribosomal protein L40;
DE   Contains:
DE     RecName: Full=Ubiquitin;
DE   Contains:
DE     RecName: Full=60S ribosomal protein L40;
DE     AltName: Full=CEP52;
DE   Flags: Precursor;
GN   Name=UBI3;
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1657605; DOI=10.1111/j.1432-1033.1991.tb16363.x;
RA   Pollmann L., von Kampen J., Wettern M.;
RT   "Ubiquitin in a lower plant. Characterization of ubiquitin-encoding DNA and
RT   RNA from Chlamydomonas reinhardii.";
RL   Eur. J. Biochem. 202:197-204(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-70 AND 75-76.
RC   STRAIN=cw15;
RX   PubMed=1312804; DOI=10.1016/0003-9861(92)90157-r;
RA   Shimogawara K., Muto S.;
RT   "Purification of Chlamydomonas 28-kDa ubiquitinated protein and its
RT   identification as ubiquitinated histone H2B.";
RL   Arch. Biochem. Biophys. 294:193-199(1992).
CC   -!- FUNCTION: [Ubiquitin]: Exists either covalently attached to another
CC       protein, or free (unanchored). When covalently bound, it is conjugated
CC       to target proteins via an isopeptide bond either as a monomer
CC       (monoubiquitin), a polymer linked via different Lys residues of the
CC       ubiquitin (polyubiquitin chains) or a linear polymer linked via the
CC       initiator Met of the ubiquitin (linear polyubiquitin chains).
CC       Polyubiquitin chains, when attached to a target protein, have different
CC       functions depending on the Lys residue of the ubiquitin that is linked:
CC       Lys-48-linked is involved in protein degradation via the proteasome.
CC       Linear polymer chains formed via attachment by the initiator Met lead
CC       to cell signaling. Ubiquitin is usually conjugated to Lys residues of
CC       target proteins, however, in rare cases, conjugation to Cys or Ser
CC       residues has been observed. When polyubiquitin is free (unanchored-
CC       polyubiquitin), it also has distinct roles, such as in activation of
CC       protein kinases, and in signaling (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: [60S ribosomal protein L40]: Component of the 60S subunit of
CC       the ribosome.
CC   -!- SUBUNIT: Ribosomal protein L40 is part of the 60S ribosomal subunit.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [60S ribosomal protein L40]: Cytoplasm
CC       {ECO:0000250}.
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 eL40 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X60826; CAA43216.1; -; mRNA.
DR   RefSeq; XP_001700313.1; XM_001700261.1.
DR   AlphaFoldDB; P0CH10; -.
DR   SMR; P0CH10; -.
DR   PRIDE; P0CH10; -.
DR   EnsemblPlants; PNW87921; PNW87921; CHLRE_01g007051v5.
DR   GeneID; 5725863; -.
DR   Gramene; PNW87921; PNW87921; CHLRE_01g007051v5.
DR   KEGG; cre:CHLRE_01g007051v5; -.
DR   HOGENOM; CLU_010412_3_4_1; -.
DR   OMA; AREYNQN; -.
DR   OrthoDB; 1536766at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IEA:UniProt.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 4.10.1060.50; -; 1.
DR   InterPro; IPR038587; L40e_sf.
DR   InterPro; IPR001975; Ribosomal_L40e.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   Pfam; PF01020; Ribosomal_L40e; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM01377; Ribosomal_L40e; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Isopeptide bond; Nucleus;
KW   Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT   CHAIN           1..76
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396457"
FT   CHAIN           77..128
FT                   /note="60S ribosomal protein L40"
FT                   /id="PRO_0000396458"
FT   DOMAIN          1..76
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CROSSLNK        48
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT   CROSSLNK        76
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
SQ   SEQUENCE   128 AA;  14700 MW;  CA59D3F07E1651C7 CRC64;
     MQIFVKTLTG KTITLEVESS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN
     IQKESTLHLV LRLRGGIIEP SLQALARKYN QEKMICRKCY ARLHPRAKNC RKKSCGHTNQ
     LRPKKKLK