ID   UBIQP_LINUS             Reviewed;         305 AA.
AC   P69315; O82079; P03993;
DT   23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Polyubiquitin;
DE   Contains:
DE     RecName: Full=Ubiquitin;
DE   Contains:
DE     RecName: Full=Ubiquitin-related;
DE   Flags: Precursor; Fragment;
OS   Linum usitatissimum (Flax) (Linum humile).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Linaceae; Linum.
OX   NCBI_TaxID=4006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Stormont cirrus; TISSUE=Leaf;
RX   PubMed=1850710; DOI=10.1016/0378-1119(91)90035-a;
RA   Agarwal M.L., Cullis C.A.;
RT   "The ubiquitin-encoding multigene family of flax, Linum usitatissimum.";
RL   Gene 99:69-75(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-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: 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; M57895; AAA33401.1; -; Genomic_DNA.
DR   PIR; PS0428; PS0428.
DR   AlphaFoldDB; P69315; -.
DR   SMR; P69315; -.
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; 5.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 5.
DR   SUPFAM; SSF54236; SSF54236; 5.
DR   PROSITE; PS00299; UBIQUITIN_1; 3.
DR   PROSITE; PS50053; UBIQUITIN_2; 5.
PE   3: Inferred from homology;
KW   Cytoplasm; Isopeptide bond; Nucleus; Repeat; Ubl conjugation.
FT   CHAIN           <1..41
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000114842"
FT   CHAIN           42..117
FT                   /note="Ubiquitin-related"
FT                   /id="PRO_0000396391"
FT   CHAIN           118..193
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396392"
FT   CHAIN           194..269
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396393"
FT   CHAIN           270..>305
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396394"
FT   DOMAIN          <1..41
FT                   /note="Ubiquitin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          42..117
FT                   /note="Ubiquitin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          118..193
FT                   /note="Ubiquitin-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          194..269
FT                   /note="Ubiquitin-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          270..>305
FT                   /note="Ubiquitin-like 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CROSSLNK        89
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        117
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
FT   NON_TER         305
SQ   SEQUENCE   305 AA;  34172 MW;  ADDA591EAF65F03F CRC64;
     IPPDQQRLIF AGKQLEDGRT LADYNIQKES TLHLVLRLRG GMQIFLKTLT GKTITLEVES
     SDTIDNVKAK IQDKEGIPPD QQRLIFAGKQ LEDGRTLADY NIQKESTLHL VLRLRGGMQI
     FVKTLTGKTI TLEVESSDTI DNVKAKIQDK EGIPPDQQRL IFAGKQLEDG RTLADYNIQK
     ESTLHLVLRL RGGMQIFVKT LTGKTITLEV ESSDTIDNVK AKIQDKEGIP PDQQRLIFAG
     KQLEDGRTLA DYNIQKESTL HLVLRLRGGM QIFVKTLTGK TITLEVESSD TIDNVKAKIQ
     DKEGI