ID K4G045_CALMI Unreviewed; 128 AA.
AC K4G045;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Ubiquitin-ribosomal protein eL40 fusion protein {ECO:0000256|ARBA:ARBA00035298};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFK10626.1};
RN [1] {ECO:0000313|EMBL:AFK10626.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Gills {ECO:0000313|EMBL:AFK10626.1};
RX PubMed=23056606;
RA Tan Y.Y., Kodzius R., Tay B.H., Tay A., Brenner S., Venkatesh B.;
RT "Sequencing and Analysis of Full-Length cDNAs, 5'-ESTs and 3'-ESTs from a
RT Cartilaginous Fish, the Elephant Shark (Callorhinchus milii).";
RL PLoS ONE 7:E47174-E47174(2012).
CC -!- FUNCTION: Component of the 60S subunit of the ribosome.
CC {ECO:0000256|ARBA:ARBA00002241}.
CC -!- FUNCTION: Exists either covalently attached to another protein, or free
CC (unanchored). When covalently bound, it is conjugated to target
CC proteins via an isopeptide bond either as a monomer (monoubiquitin), a
CC polymer linked via different Lys residues of the ubiquitin
CC (polyubiquitin chains) or a linear polymer linked via the initiator Met
CC of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains,
CC when attached to a target protein, have different functions depending
CC on the Lys residue of the ubiquitin that is linked: Lys-48-linked is
CC involved in protein degradation via the proteasome. Linear polymer
CC chains formed via attachment by the initiator Met lead to cell
CC signaling. Ubiquitin is usually conjugated to Lys residues of target
CC proteins, however, in rare cases, conjugation to Cys or Ser residues
CC 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. {ECO:0000256|ARBA:ARBA00029384}.
CC -!- SUBUNIT: Part of the 60S ribosomal subunit.
CC {ECO:0000256|ARBA:ARBA00035124}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic
CC ribosomal protein eL40 family. {ECO:0000256|ARBA:ARBA00010570}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin family.
CC {ECO:0000256|ARBA:ARBA00008373}.
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DR EMBL; JX052398; AFK10626.1; -; mRNA.
DR EMBL; JX207239; AFM85553.1; -; mRNA.
DR AlphaFoldDB; K4G045; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0015934; C:large ribosomal subunit; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd01803; Ubl_ubiquitin; 1.
DR Gene3D; 4.10.1060.50; -; 1.
DR InterPro; IPR001975; Ribosomal_eL40_dom.
DR InterPro; IPR038587; Ribosomal_eL40_sf.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
DR PANTHER; PTHR10666:SF515; POLYUBIQUITIN-B; 1.
DR PANTHER; PTHR10666; UBIQUITIN; 1.
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; Ubiquitin-like; 1.
DR SUPFAM; SSF57829; Zn-binding ribosomal proteins; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW ECO:0000313|EMBL:AFK10626.1}.
FT DOMAIN 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
SQ SEQUENCE 128 AA; 14681 MW; 7BC592ADAFAC9883 CRC64;
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGGMDP SLRLLAMKYN CEKMICRKCY ARLHPRASNC RKKKCGHTNN
LRPKKELK
//
