UBIQ_WHEAT
ID UBIQ_WHEAT Reviewed; 77 AA.
AC P69326; O82079; P03993;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Ubiquitin;
DE Flags: Precursor;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Mustang; TISSUE=Leaf;
RX PubMed=1650258; DOI=10.1007/bf00015082;
RA Joshi C.P., Weng J., Nguyen H.T.;
RT "Wheat ubiquitin gene exhibits a conserved protein coding region and a
RT diverged 3' non-coding region.";
RL Plant Mol. Biol. 16:907-908(1991).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR EMBL; X56601; CAA39938.1; -; mRNA.
DR PDB; 5TTE; X-ray; 3.50 A; F=1-76.
DR PDB; 6NYA; X-ray; 2.06 A; B/E=1-76.
DR PDB; 7K5J; X-ray; 3.42 A; M/N/O/P/Q/R/W/X=1-76.
DR PDBsum; 5TTE; -.
DR PDBsum; 6NYA; -.
DR PDBsum; 7K5J; -.
DR AlphaFoldDB; P69326; -.
DR SMR; P69326; -.
DR STRING; 4565.Traes_1AS_36865F81C.2; -.
DR EnsemblPlants; TraesCAD_scaffold_050574_01G000200.1; TraesCAD_scaffold_050574_01G000200.1; TraesCAD_scaffold_050574_01G000200.
DR EnsemblPlants; TraesCLE_scaffold_060412_01G000200.1; TraesCLE_scaffold_060412_01G000200.1; TraesCLE_scaffold_060412_01G000200.
DR EnsemblPlants; TraesCS7D02G454100.1; TraesCS7D02G454100.1.cds1; TraesCS7D02G454100.
DR EnsemblPlants; TraesPAR_scaffold_047021_01G000100.1; TraesPAR_scaffold_047021_01G000100.1; TraesPAR_scaffold_047021_01G000100.
DR EnsemblPlants; TraesPAR_scaffold_156029_01G000300.1; TraesPAR_scaffold_156029_01G000300.1; TraesPAR_scaffold_156029_01G000300.
DR EnsemblPlants; TraesROB_scaffold_086305_01G000200.1; TraesROB_scaffold_086305_01G000200.1; TraesROB_scaffold_086305_01G000200.
DR EnsemblPlants; TraesROB_scaffold_183018_01G000300.1; TraesROB_scaffold_183018_01G000300.1; TraesROB_scaffold_183018_01G000300.
DR EnsemblPlants; TraesWEE_scaffold_049341_01G000300.1; TraesWEE_scaffold_049341_01G000300.1; TraesWEE_scaffold_049341_01G000300.
DR Gramene; TraesCAD_scaffold_050574_01G000200.1; TraesCAD_scaffold_050574_01G000200.1; TraesCAD_scaffold_050574_01G000200.
DR Gramene; TraesCLE_scaffold_060412_01G000200.1; TraesCLE_scaffold_060412_01G000200.1; TraesCLE_scaffold_060412_01G000200.
DR Gramene; TraesCS7D02G454100.1; TraesCS7D02G454100.1.cds1; TraesCS7D02G454100.
DR Gramene; TraesPAR_scaffold_047021_01G000100.1; TraesPAR_scaffold_047021_01G000100.1; TraesPAR_scaffold_047021_01G000100.
DR Gramene; TraesPAR_scaffold_156029_01G000300.1; TraesPAR_scaffold_156029_01G000300.1; TraesPAR_scaffold_156029_01G000300.
DR Gramene; TraesROB_scaffold_086305_01G000200.1; TraesROB_scaffold_086305_01G000200.1; TraesROB_scaffold_086305_01G000200.
DR Gramene; TraesROB_scaffold_183018_01G000300.1; TraesROB_scaffold_183018_01G000300.1; TraesROB_scaffold_183018_01G000300.
DR Gramene; TraesWEE_scaffold_049341_01G000300.1; TraesWEE_scaffold_049341_01G000300.1; TraesWEE_scaffold_049341_01G000300.
DR eggNOG; KOG0004; Eukaryota.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P69326; baseline and differential.
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; 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 3D-structure; Cytoplasm; Isopeptide bond; Nucleus; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000114853"
FT PROPEP 77
FT /id="PRO_0000396431"
FT DOMAIN 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
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 STRAND 1..7
FT /evidence="ECO:0007829|PDB:6NYA"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:6NYA"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:6NYA"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:6NYA"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:6NYA"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:6NYA"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:7K5J"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:6NYA"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:6NYA"
SQ SEQUENCE 77 AA; 8653 MW; 53152936277CD840 CRC64;
MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN
IQKESTLHLV LRLRGGQ
