RUB1_DESAN
ID RUB1_DESAN Reviewed; 153 AA.
AC P0C073; P0C072; Q8LPV5;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Ubiquitin-NEDD8-like protein RUB1;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Contains:
DE RecName: Full=NEDD8-like protein RUB1;
DE AltName: Full=DaRUB1;
DE AltName: Full=Ubiquitin-related protein 1;
DE Flags: Precursor;
GN Name=RUB1;
OS Deschampsia antarctica (Antarctic hair grass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Poodae; Poeae; Poeae Chloroplast Group 2 (Poeae type); Holcinae;
OC Deschampsia.
OX NCBI_TaxID=159298;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Leaf;
RX PubMed=12955601; DOI=10.1007/s00792-003-0345-4;
RA Gidekel M., Destefano-Beltran L., Garcia P., Mujica L., Leal P., Cuba M.,
RA Fuentes L., Bravo L.A., Corcuera L.J., Alberdi M., Concha I., Gutierrez A.;
RT "Identification and characterization of three novel cold acclimation-
RT responsive genes from the extremophile hair grass Deschampsia antarctica
RT Desv.";
RL Extremophiles 7:459-469(2003).
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 Lys-63-linked is involved in endocytosis, and DNA-damage responses.
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: [NEDD8-like protein RUB1]: Probably function as a stable
CC post-translational protein modifier. May be involved during cold
CC acclimation. {ECO:0000269|PubMed:12955601}.
CC -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: At 13 degrees Celsius, expressed in roots and to a
CC lower extent in old leaves and crown. When transferred at 4 degrees
CC Celsius, levels increase in leaves and crown but decrease in roots.
CC {ECO:0000269|PubMed:12955601}.
CC -!- INDUCTION: By cold and PEG, but not by NaCl.
CC {ECO:0000269|PubMed:12955601}.
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 -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR EMBL; AY090541; AAM22748.1; -; mRNA.
DR AlphaFoldDB; P0C073; -.
DR SMR; P0C073; -.
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 CDD; cd01806; Ubl_NEDD8; 1.
DR InterPro; IPR038738; Nedd8-like.
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;
KW Ubl conjugation pathway.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000396912"
FT CHAIN 77..152
FT /note="NEDD8-like protein RUB1"
FT /id="PRO_0000035971"
FT PROPEP 153
FT /evidence="ECO:0000305"
FT /id="PRO_0000035972"
FT DOMAIN 1..76
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 77..152
FT /note="Ubiquitin-like 2"
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 63
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 CROSSLNK 152
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
SQ SEQUENCE 153 AA; 17116 MW; 1929C1A4A59A6B19 CRC64;
MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN
IQKESTLHLV LRLRGGTMIK VKTLTGKEIE IDIEPTDTID RVKERVEEKE GIPPVQQRLI
YAGKQLADDK TAKDYNIEGG SVLHLVLALR GGY
