ID   RS272_HORVU             Reviewed;         155 AA.
AC   P0CG87; O82079; P03993; P22277; P69314;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   03-AUG-2022, entry version 39.
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;
GN   Name=MUB2; Synonyms=RPS27A2;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Bomi;
RX   PubMed=1701748; DOI=10.1016/0378-1119(90)90383-3;
RA   Gausing K., Jensen C.B.;
RT   "Two ubiquitin-long-tail fusion genes arranged as closely spaced direct
RT   repeats in barley.";
RL   Gene 94:165-171(1990).
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 generally synthesized as a polyubiquitin
CC       precursor with tandem head to tail repeats. Often, there is one to
CC       three additional amino acids after the last repeat, removed in the
CC       mature protein. Alternatively, ubiquitin extension protein is
CC       synthesized as a single copy of ubiquitin fused to a ribosomal protein
CC       (either L40 or S27A) or to an ubiquitin-related protein (either RUB1 or
CC       RUB2). Following translation, extension protein is cleaved from
CC       ubiquitin.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M60176; AAA62699.1; -; Genomic_DNA.
DR   PIR; JH0227; JH0227.
DR   AlphaFoldDB; P0CG87; -.
DR   SMR; P0CG87; -.
DR   ExpressionAtlas; P0CG87; baseline and differential.
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:0003729; F:mRNA binding; IEA:UniProt.
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   3: Inferred from homology;
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_0000396522"
FT   CHAIN           77..155
FT                   /note="40S ribosomal protein S27a"
FT                   /id="PRO_0000396523"
FT   DOMAIN          1..76
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   ZN_FING         122..145
FT                   /note="C4-type"
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   155 AA;  17671 MW;  A18E9BE5A637D478 CRC64;
     MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN
     IQKESTLHLV LRLRGGAKKR KKKTYTKPKK QKHKHKKVKL AVLQFYKVDD STGKVTRLRK
     ECPNADCGAG TFMANHFDRH YCGKCGLTYV YNQKA