ID RS27A_DAUCA Reviewed; 143 AA.
AC P59272; O82079; P03993; P69312;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Ubiquitin-ribosomal protein eS31 fusion protein {ECO:0000305};
DE Contains:
DE RecName: Full=Ubiquitin;
DE Contains:
DE RecName: Full=Small ribosomal subunit protein eS31 {ECO:0000305};
DE AltName: Full=40S ribosomal protein S27a;
DE Flags: Precursor; Fragment;
OS Daucus carota (Wild carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=4039;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Lunga di Amsterdam;
RA Balestrazzi A., Cella R., Carbonera D.;
RT "Cloning and expression analysis of a cDNA for carrot ubiquitin carboxyl
RT extension protein.";
RL (er) Plant Gene Register PGR98-109(1998).
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: [Small ribosomal subunit protein eS31]: Component of the 40S
CC subunit of the ribosome.
CC -!- SUBUNIT: [Small ribosomal subunit protein eS31]: Part of the 40S
CC ribosomal subunit. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Ubiquitin is generally synthesized as a polyubiquitin
CC precursor with tandem head to tail repeats. Often, there are one to
CC three additional amino acids after the last repeat, removed in the
CC mature protein. Alternatively, ubiquitin extension protein is
CC synthesized as a single copy of ubiquitin fused to a ribosomal protein
CC (either eL40 or eS31) or to an ubiquitin-related protein (either RUB1
CC or RUB2). Following translation, extension protein is cleaved from
CC ubiquitin.
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 eS31 family. {ECO:0000305}.
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DR EMBL; U68751; AAC26159.1; -; mRNA.
DR AlphaFoldDB; P59272; -.
DR SMR; P59272; -.
DR EnsemblPlants; KZM87323; KZM87323; DCAR_024457.
DR Gramene; KZM87323; KZM87323; DCAR_024457.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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:0046872; F:metal ion binding; 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 CDD; cd01803; Ubl_ubiquitin; 1.
DR Gene3D; 6.20.50.150; -; 1.
DR InterPro; IPR002906; Ribosomal_eS31.
DR InterPro; IPR038582; Ribosomal_eS31_euk-type_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:SF468; POLYUBIQUITIN-LIKE; 1.
DR PANTHER; PTHR10666; UBIQUITIN; 1.
DR Pfam; PF01599; Ribosomal_S27; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM01402; Ribosomal_S27; 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; Isopeptide bond; Metal-binding; Nucleus; Ribonucleoprotein;
KW Ribosomal protein; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000114838"
FT CHAIN 77..>143
FT /note="Small ribosomal subunit protein eS31"
FT /id="PRO_0000137678"
FT DOMAIN 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT ZN_FING 121..>143
FT /note="C4-type"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT NON_TER 143
SQ SEQUENCE 143 AA; 16356 MW; 8FAD6DC9681338F1 CRC64;
MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN
IQKESTLHLV LRLRGGGKKR KKKTYTKPKK TKHKHRKVKL AVLQFYKVDE SGKVQRLRKE
CPNGECGAGT FMANHFDRHY CGK
//
