RL401_CHLRE
ID RL401_CHLRE Reviewed; 128 AA.
AC P0CH11; P14624; P14695;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 59.
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=UBI1;
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].
RC STRAIN=2137;
RX PubMed=2554258; DOI=10.1093/nar/17.20.8377;
RA Callis J., Pollmann L., Shanklin J., Wettern M., Vierstra R.;
RT "Sequence of a cDNA from Chlamydomonas reinhardii encoding a ubiquitin 52
RT amino acid extension protein.";
RL Nucleic Acids Res. 17:8377-8377(1989).
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; X15427; CAA33466.1; -; mRNA.
DR PIR; S06598; UQKM.
DR RefSeq; XP_001700313.1; XM_001700261.1.
DR AlphaFoldDB; P0CH11; -.
DR SMR; P0CH11; -.
DR STRING; 3055.EDO98280; -.
DR EnsemblPlants; PNW87921; PNW87921; CHLRE_01g007051v5.
DR GeneID; 5725863; -.
DR Gramene; PNW87921; PNW87921; CHLRE_01g007051v5.
DR KEGG; cre:CHLRE_01g007051v5; -.
DR eggNOG; KOG0003; Eukaryota.
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_0000114837"
FT CHAIN 77..128
FT /note="60S ribosomal protein L40"
FT /id="PRO_0000138761"
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
