ID   UBIQ_LUMTE              Reviewed;          63 AA.
AC   P84589;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 2.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Ubiquitin;
DE   Flags: Fragment;
OS   Lumbricus terrestris (Common earthworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Oligochaeta; Crassiclitellata; Lumbricina; Lumbricidae; Lumbricinae;
OC   Lumbricus.
OX   NCBI_TaxID=6398;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RA   Koenig S., Mehlich A.-M., Buellesbach J., Michiels N.;
RT   "Allohormones in Lumbricus terrestris? Mass spectrometry of the setal gland
RT   product indicates role of ubiquitin.";
RL   Invertebr. Reprod. Dev. 49:103-111(2006).
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-6-linked may be involved in DNA repair; Lys-11-linked is involved
CC       in ERAD (endoplasmic reticulum-associated degradation) and in cell-
CC       cycle regulation; Lys-29-linked is involved in lysosomal degradation;
CC       Lys-33-linked is involved in kinase modification; Lys-48-linked is
CC       involved in protein degradation via the proteasome; Lys-63-linked is
CC       involved in endocytosis, DNA-damage responses as well as in signaling
CC       processes leading to activation of the transcription factor NF-kappa-B.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62990}. Nucleus
CC       {ECO:0000250|UniProtKB:P62990}.
CC   -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000255}.
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DR   AlphaFoldDB; P84589; -.
DR   SMR; P84589; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   Pfam; PF00240; ubiquitin; 1.
DR   PRINTS; PR00348; UBIQUITIN.
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   Ubl conjugation.
FT   CHAIN           <1..>63
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000114819"
FT   DOMAIN          <1..>63
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   SITE            43
FT                   /note="Interacts with activating enzyme"
FT                   /evidence="ECO:0000305"
FT   SITE            57
FT                   /note="Essential for function"
FT                   /evidence="ECO:0000305"
FT   SITE            61
FT                   /note="Interacts with activating enzyme"
FT                   /evidence="ECO:0000305"
FT   CROSSLNK        37
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|Ref.1"
FT   NON_TER         63
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   63 AA;  7203 MW;  3A3EB5E4332696F7 CRC64;
     TITLEVEPSD TIENVKAKIQ DKEGIPPDQQ RLIFAGKQLE DGRTLSDYNI QKESTLHLVL
     RLR