UBIQP_TETPY
ID UBIQP_TETPY Reviewed; 381 AA.
AC P0CG82; P20685;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 25-MAY-2022, entry version 24.
DE RecName: Full=Polyubiquitin;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Flags: Precursor;
GN Name=TU20;
OS Tetrahymena pyriformis.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=5908;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1667985; DOI=10.3109/10425179109039687;
RA Neves A.M., Guerreiro P., Rodrigues-Pousada C.;
RT "The macronuclear polyubiquitin gene of the ciliate Tetrahymena
RT pyriformis.";
RL DNA Seq. 2:173-180(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-78.
RX PubMed=2854094; DOI=10.1016/0378-1119(88)90315-0;
RA Neves A.M., Barahona I., Galego L., Rodrigues-Pousada C.;
RT "Ubiquitin genes in Tetrahymena pyriformis and their expression during heat
RT shock.";
RL Gene 73:87-96(1988).
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: Ubiquitin is generally synthesized as a polyubiquitin
CC precursor. Some ubiquitin genes contain a single copy of ubiquitin
CC fused to a ribosomal protein.
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; X61053; CAA43387.1; -; Genomic_DNA.
DR EMBL; M24081; AAA56861.1; -; Genomic_DNA.
DR PIR; JT0491; JT0491.
DR PIR; S25848; S25848.
DR AlphaFoldDB; P0CG82; -.
DR SMR; P0CG82; -.
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; 5.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 5.
DR SUPFAM; SSF54236; SSF54236; 5.
DR PROSITE; PS00299; UBIQUITIN_1; 5.
DR PROSITE; PS50053; UBIQUITIN_2; 5.
PE 3: Inferred from homology;
KW Cytoplasm; Isopeptide bond; Nucleus; Repeat; Ubl conjugation.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000396362"
FT CHAIN 77..152
FT /note="Ubiquitin"
FT /id="PRO_0000396363"
FT CHAIN 153..228
FT /note="Ubiquitin"
FT /id="PRO_0000396364"
FT CHAIN 229..304
FT /note="Ubiquitin"
FT /id="PRO_0000396365"
FT CHAIN 305..380
FT /note="Ubiquitin"
FT /id="PRO_0000396366"
FT PROPEP 381
FT /id="PRO_0000396367"
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 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 CONFLICT 77
FT /note="M -> S (in Ref. 2; AAA56861)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 42680 MW; 0A70CC76DBBBC3F7 CRC64;
MQIFVKTLTG KTITLDVEAS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LDVEASDTIE NVKAKIQDKE GIPPDQQRLI
FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLDVE ASDTIENVKA
KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT
ITLDVEASDT IENVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR
LRGGMQIFVK TLTGKTITLD VEASDTIENV KAKIQDKEGI PPDQQRLIFA GKQLEDGRTL
SDYNIQKEST LHLVLRLRGG Q
