ID   UBIQP_GEOCY             Reviewed;         457 AA.
AC   P59669;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Polyubiquitin;
DE   Contains:
DE     RecName: Full=Ubiquitin;
DE   Contains:
DE     RecName: Full=Ubiquitin-related;
DE   Flags: Precursor;
OS   Geodia cydonium (Sponge).
OC   Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC   Tetractinellida; Astrophorina; Geodiidae; Geodia.
OX   NCBI_TaxID=6047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8282761; DOI=10.1242/jcs.106.2.545;
RA   Pfeifer K., Frank K., Schroeder H.C., Gamulin V., Rinkevich B., Batel R.,
RA   Mueller I.M., Mueller W.E.G.;
RT   "Cloning of the polyubiquitin cDNA from the marine sponge Geodia cydonium
RT   and its preferential expression during reaggregation of cells.";
RL   J. Cell Sci. 106:545-554(1993).
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   -!- 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; X70917; CAA50268.1; -; mRNA.
DR   PIR; S32020; S32020.
DR   AlphaFoldDB; P59669; -.
DR   SMR; P59669; -.
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; 6.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 6.
DR   SUPFAM; SSF54236; SSF54236; 6.
DR   PROSITE; PS00299; UBIQUITIN_1; 6.
DR   PROSITE; PS50053; UBIQUITIN_2; 6.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Isopeptide bond; Nucleus; Repeat; Ubl conjugation.
FT   CHAIN           1..76
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000114818"
FT   CHAIN           77..152
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396351"
FT   CHAIN           153..228
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396352"
FT   CHAIN           229..304
FT                   /note="Ubiquitin-related"
FT                   /id="PRO_0000396353"
FT   CHAIN           305..380
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396354"
FT   CHAIN           381..456
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396355"
FT   PROPEP          457
FT                   /id="PRO_0000396356"
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   DOMAIN          153..228
FT                   /note="Ubiquitin-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          229..304
FT                   /note="Ubiquitin-like 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          305..380
FT                   /note="Ubiquitin-like 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          381..456
FT                   /note="Ubiquitin-like 6"
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"
SQ   SEQUENCE   457 AA;  51276 MW;  9344E1326727F57B CRC64;
     MQIFVKTLTG KTITLEVEAS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
     IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEASDTIE NVKAKIQDKE GIPPDQQRLI
     FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE ASDTIENVKA
     KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT
     ITLEVEASDT IENVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVVR
     LRGGMQIFVK TLTGKTITLE VEASDTIENV KAKIQDKEGI PPDQQRLIFA GKQLEDGRTL
     SDYNIQKEST LHLVLRLRGG MQIFVKTLTG KTITLEVEAS DTIENVKAKI QDKEGIPPDQ
     QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGGF