ID E3UKG7_ERISI Unreviewed; 129 AA.
AC E3UKG7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Ubiquitin-ribosomal protein eL40 fusion protein {ECO:0000256|ARBA:ARBA00035298};
OS Eriocheir sinensis (Chinese mitten crab).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC Eubrachyura; Grapsoidea; Varunidae; Eriocheir.
OX NCBI_TaxID=95602 {ECO:0000313|EMBL:ADO32980.1};
RN [1] {ECO:0000313|EMBL:ADO32980.1}
RP NUCLEOTIDE SEQUENCE.
RA Deng Y.F., Xia A.J., Pan J.L., Bo R.F., Zhu Q.S.;
RT "Cloning, characterization and expression of ubiquitin from Eriocheir
RT sinensis.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADW27185.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22297692; DOI=10.1007/s11033-012-1474-6;
RA Wang Q., Chen L., Wang Y., Li W., He L., Jiang H.;
RT "Expression characteristics of two ubiquitin/ribosomal fusion protein genes
RT in the developing testis, accessory gonad and ovary of Chinese mitten crab,
RT Eriocheir sinensis.";
RL Mol. Biol. Rep. 39:6683-6692(2012).
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; HM449082; ADO32980.1; -; mRNA.
DR EMBL; HM177457; ADW27185.1; -; mRNA.
DR AlphaFoldDB; E3UKG7; -.
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; 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 2: Evidence at transcript level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
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 129 AA; 14717 MW; A622238878A7BB96 CRC64;
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGVIEP SLKLLAEKYN CNKMICRKCY ARLHPRATNC RKKKCGHTSN
IRPKKKIKG
//
