RS27A_SPOFR
ID RS27A_SPOFR Reviewed; 156 AA.
AC P68203; P68195; Q8WQI4; Q9VKW6; Q9VQX7; Q9VZL4;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Ubiquitin-40S ribosomal protein S27a;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Contains:
DE RecName: Full=40S ribosomal protein S27a;
DE Flags: Precursor;
OS Spodoptera frugiperda (Fall armyworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Amphipyrinae; Spodoptera.
OX NCBI_TaxID=7108;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-76.
RX PubMed=2153300; DOI=10.1073/pnas.87.1.409;
RA Guarino L.A.;
RT "Identification of a viral gene encoding a ubiquitin-like protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:409-413(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14668217; DOI=10.1093/bioinformatics/btg324;
RA Landais I., Ogliastro M., Mita K., Nohata J., Lopez-Ferber M.,
RA Duonor-Cerutti M., Shimada T., Fournier P., Devauchelle G.;
RT "Annotation pattern of ESTs from Spodoptera frugiperda Sf9 cells and
RT analysis of the ribosomal protein genes reveal insect-specific features and
RT unexpectedly low codon usage bias.";
RL Bioinformatics 19:2343-2350(2003).
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: Ribosomal protein S27a is a component of the 40S subunit of
CC the ribosome.
CC -!- SUBUNIT: Ribosomal protein S27a is part of the 40S ribosomal subunit.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Ubiquitin is synthesized as a polyubiquitin precursor
CC with exact head to tail repeats, the number of repeats differs between
CC species. In some species there is a final amino-acid after the last
CC repeat. Some ubiquitin genes contain a single copy of ubiquitin fused
CC to a ribosomal protein (either L40 or S27A).
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 eS31 family. {ECO:0000305}.
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DR EMBL; M30306; AAA29989.1; -; Genomic_DNA.
DR EMBL; AY072292; AAL62473.1; -; mRNA.
DR PIR; B34813; UQUYSF.
DR AlphaFoldDB; P68203; -.
DR SMR; P68203; -.
DR PRIDE; P68203; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 6.20.50.150; -; 1.
DR InterPro; IPR002906; Ribosomal_S27a.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR InterPro; IPR038582; S27a-like_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
DR Pfam; PF01599; Ribosomal_S27; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM01402; Ribosomal_S27; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF57829; SSF57829; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Isopeptide bond; Metal-binding; Nucleus; Ribonucleoprotein;
KW Ribosomal protein; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000114816"
FT CHAIN 77..156
FT /note="40S ribosomal protein S27a"
FT /id="PRO_0000137673"
FT DOMAIN 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT ZN_FING 121..144
FT /note="C4-type"
FT SITE 54
FT /note="Interacts with activating enzyme"
FT SITE 68
FT /note="Essential for function"
FT SITE 72
FT /note="Interacts with activating enzyme"
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 51
FT /note="E -> G (in Ref. 1; AAA29989)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="L -> F (in Ref. 1; AAA29989)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 156 AA; 17973 MW; 330D03979D414EF4 CRC64;
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGAKKR KKKNYSTPKK IKHKKKKVKL AVLRFYKVDE NGKIHRLRRE
CTGEQCGAGV FMAVMEDRHY CGKCHSTMVF KDDDRP
