RL402_TRYCR
ID RL402_TRYCR Reviewed; 356 AA.
AC P0CH27; P08565;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Ubiquitin-60S ribosomal protein L40;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Contains:
DE RecName: Full=60S ribosomal protein L40;
DE Flags: Precursor;
OS Trypanosoma cruzi.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=5693;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2457589; DOI=10.1016/s0021-9258(18)37809-8;
RA Kirchhoff L.V., Kim K.S., Engman D.M., Donelson J.E.;
RT "Ubiquitin genes in trypanosomatidae.";
RL J. Biol. Chem. 263:12698-12704(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-78.
RC STRAIN=CL;
RX PubMed=2841110; DOI=10.1002/j.1460-2075.1988.tb02921.x;
RA Swindle J., Ajioka J., Eisen H., Sanwal B., Jacquemot C., Browder Z.,
RA Buck G.;
RT "The genomic organization and transcription of the ubiquitin genes of
RT Trypanosoma cruzi.";
RL EMBO J. 7:1121-1127(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 -!- FUNCTION: [60S ribosomal protein L40]: Component of the 60S subunit of
CC the ribosome. {ECO:0000250}.
CC -!- SUBUNIT: Ribosomal protein L40 is part of the 60S ribosomal subunit.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [60S ribosomal protein L40]: Cytoplasm
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Ubiquitin is synthesized as a polyubiquitin precursor
CC with 5 or 6 exact head to tail repeats. Some ubiquitin genes contain a
CC single copy of ubiquitin fused to a ribosomal protein. This gene is an
CC exception, since it contains for 4 copies of the ubiquitin fused to the
CC ribosomal protein L40.
CC -!- MISCELLANEOUS: For a better understanding, features related to
CC ubiquitin are only indicated for the first chain.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic
CC ribosomal protein eL40 family. {ECO:0000305}.
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DR EMBL; J03945; AAA30271.1; -; mRNA.
DR EMBL; X07451; CAA30334.1; -; Genomic_DNA.
DR PIR; A31115; UQUTRC.
DR PIR; S00510; UQUTC.
DR AlphaFoldDB; P0CH27; -.
DR SMR; P0CH27; -.
DR VEuPathDB; TriTrypDB:BCY84_17803; -.
DR VEuPathDB; TriTrypDB:C3747_46g18; -.
DR VEuPathDB; TriTrypDB:C4B63_138g30; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0024880; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0110030; -.
DR VEuPathDB; TriTrypDB:TcCL_Unassigned07130; -.
DR VEuPathDB; TriTrypDB:TcG_06155; -.
DR VEuPathDB; TriTrypDB:TcYC6_0037170; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 4.10.1060.50; -; 1.
DR InterPro; IPR038587; L40e_sf.
DR InterPro; IPR001975; Ribosomal_L40e.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
DR Pfam; PF01020; Ribosomal_L40e; 1.
DR Pfam; PF00240; ubiquitin; 4.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM01377; Ribosomal_L40e; 1.
DR SMART; SM00213; UBQ; 4.
DR SUPFAM; SSF54236; SSF54236; 4.
DR SUPFAM; SSF57829; SSF57829; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 4.
DR PROSITE; PS50053; UBIQUITIN_2; 4.
PE 2: Evidence at transcript level;
KW Cytoplasm; Isopeptide bond; Nucleus; Repeat; Ribonucleoprotein;
KW Ribosomal protein; Ubl conjugation.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000396447"
FT CHAIN 77..152
FT /note="Ubiquitin"
FT /id="PRO_0000396448"
FT CHAIN 153..228
FT /note="Ubiquitin"
FT /id="PRO_0000396449"
FT CHAIN 229..304
FT /note="Ubiquitin"
FT /id="PRO_0000396450"
FT CHAIN 305..356
FT /note="60S ribosomal protein L40"
FT /id="PRO_0000396451"
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 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 356 AA; 40131 MW; 813CCC9FE137E68D CRC64;
MQIFVKTLTG KTIALEVESS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN
IQKESTLHLV LRLRGGMQIF VKTLTGKTIA LEVESSDTIE NVKAKIQDKE GIPPDQQRLI
FAGKQLEDGR TLADYNIQKE STLHLVLRLR GGMQIFVKTL TGKTIALEVE SSDTIENVKA
KIQDKEGIPP DQQRLIFAGK QLEDGRTLAD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT
IALEVESSDT IENVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLADYNIQ KESTLHLVLR
LRGGVMEPTL EALAKKYNWE KKVCRRCYAR LPVRASNCRK KACGHCSNLR MKKKLR
