ID E4WUZ1_OIKDI Unreviewed; 128 AA.
AC E4WUZ1;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Ubiquitin-ribosomal protein eL40 fusion protein {ECO:0000256|ARBA:ARBA00035298};
GN ORFNames=GSOID_T00009447001 {ECO:0000313|EMBL:CBY21673.1},
GN GSOID_T00030668001 {ECO:0000313|EMBL:CBY32249.1};
OS Oikopleura dioica (Tunicate).
OC Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC Oikopleuridae; Oikopleura.
OX NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY21673.1};
RN [1] {ECO:0000313|EMBL:CBY21673.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21097902; DOI=10.1126/science.1194167;
RA Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA Roest Crollius H., Wincker P., Chourrout D.;
RT "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT pelagic tunicate.";
RL Science 330:1381-1385(2010).
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 -!- 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; FN653017; CBY21673.1; -; Genomic_DNA.
DR EMBL; FN654340; CBY32249.1; -; Genomic_DNA.
DR AlphaFoldDB; E4WUZ1; -.
DR InParanoid; E4WUZ1; -.
DR Proteomes; UP000001307; Unassembled WGS sequence.
DR Proteomes; UP000011014; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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; 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 PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001307};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980}.
FT DOMAIN 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
SQ SEQUENCE 128 AA; 14650 MW; D1E316D96A46CE50 CRC64;
MQIFVKTLTG KTITLEVEAS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGVIEP SLKVLAQKYN CEKMICRKCY ARNHARATNC RKKKCGHTNQ
LRPKKKLK
//
