ID   UBIQP_HORVU             Reviewed;         171 AA.
AC   P0CG83; O82079; P03993; P69314;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 29.
DE   RecName: Full=Polyubiquitin;
DE   Contains:
DE     RecName: Full=Ubiquitin;
DE   Flags: Precursor; Fragment;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Bomi; TISSUE=Leaf;
RX   PubMed=2426105; DOI=10.1111/j.1432-1033.1986.tb09720.x;
RA   Gausing K., Barkardottir R.;
RT   "Structure and expression of ubiquitin genes in higher plants.";
RL   Eur. J. Biochem. 158:57-62(1986).
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}. Nucleus {ECO:0000250}.
CC   -!- MISCELLANEOUS: Ubiquitin is generally synthesized as a polyubiquitin
CC       precursor with tandem head to tail repeats. Often, there is 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 L40 or S27A) or to an ubiquitin-related protein (either RUB1 or
CC       RUB2). Following translation, extension protein is cleaved from
CC       ubiquitin.
CC   -!- MISCELLANEOUS: For the sake of clarity sequence features are annotated
CC       only for the first chain, and are not repeated for each of the
CC       following chains.
CC   -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR   EMBL; X04133; CAA27751.1; -; mRNA.
DR   PIR; A25062; A25062.
DR   AlphaFoldDB; P0CG83; -.
DR   SMR; P0CG83; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003729; F:mRNA binding; IEA:UniProt.
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; 2.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 2.
DR   SUPFAM; SSF54236; SSF54236; 2.
DR   PROSITE; PS00299; UBIQUITIN_1; 2.
DR   PROSITE; PS50053; UBIQUITIN_2; 2.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Isopeptide bond; Nucleus; Repeat; Ubl conjugation.
FT   CHAIN           <1..18
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396387"
FT   CHAIN           19..94
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396388"
FT   CHAIN           95..170
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396389"
FT   PROPEP          171
FT                   /id="PRO_0000396390"
FT   DOMAIN          <1..18
FT                   /note="Ubiquitin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          19..94
FT                   /note="Ubiquitin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          95..170
FT                   /note="Ubiquitin-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CROSSLNK        66
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        94
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   NON_TER         1
SQ   SEQUENCE   171 AA;  19239 MW;  AF412572ECB892CA CRC64;
     YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT ITLEVESSDT IDNVKAKIQD KEGIPPDQQR
     LIFAGKQLED GRTLADYNIQ KESTLHLVLR LRGGMQIFVK TLTGKTITLE VESSDTIDNV
     KAKIQDKEGI PPDQQRLIFA GKQLEDGRTL ADYNIQKEST LHLVLRLRGG K