ID   UBIQP_STRPU             Reviewed;         133 AA.
AC   P23398;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Polyubiquitin;
DE   Contains:
DE     RecName: Full=Ubiquitin;
DE   Flags: Precursor; Fragment;
OS   Strongylocentrotus purpuratus (Purple sea urchin).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC   Strongylocentrotus.
OX   NCBI_TaxID=7668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Blastula;
RX   PubMed=1645680; DOI=10.1016/0012-1606(91)90124-l;
RA   Nemer M., Rondinelli E., Infante D., Infante A.A.;
RT   "Polyubiquitin RNA characteristics and conditional induction in sea urchin
RT   embryos.";
RL   Dev. Biol. 145:255-265(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; M61772; AAA30082.1; -; mRNA.
DR   PIR; A49768; A49768.
DR   AlphaFoldDB; P23398; -.
DR   SMR; P23398; -.
DR   STRING; 7668.SPU_021496-tr; -.
DR   eggNOG; KOG0001; Eukaryota.
DR   HOGENOM; CLU_010412_7_0_1; -.
DR   Proteomes; UP000007110; Unassembled WGS sequence.
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; 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; Reference proteome; Repeat;
KW   Ubl conjugation.
FT   CHAIN           <1..56
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000114820"
FT   CHAIN           57..132
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396357"
FT   PROPEP          133
FT                   /id="PRO_0000396358"
FT   DOMAIN          1..56
FT                   /note="Ubiquitin-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          57..132
FT                   /note="Ubiquitin-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CROSSLNK        104
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        132
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   133 AA;  14994 MW;  F57405A5540708F0 CRC64;
     DSIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGGMQIF
     VKTLTGKTIT LEVEPSDSIE NVKAKIQDKE GIPPDQQRLI FAGKQLEDGR TLSDYNIQKE
     STLHLVLRLR GGQ