RS27A_MAIZE
ID RS27A_MAIZE Reviewed; 155 AA.
AC P27923; O82079; P03993; P69319;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 120.
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=UBF9; Synonyms=RPS27A;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Christensen A.H., Quail P.H.;
RT "Sequence analysis and transcriptional regulation by heat shock of
RT polyubiquitin transcripts from maize.";
RL Plant Mol. Biol. 12:619-632(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1660830; DOI=10.1016/0378-1119(91)90320-b;
RA Chen K., Rubenstein I.;
RT "Characterization of the structure and transcription of a ubiquitin fusion
RT gene from maize.";
RL Gene 107:205-212(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. DEA; TISSUE=Root tip;
RA Chevalier C., le Querrec F., Raymond P.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; M68937; AAA33519.1; -; Genomic_DNA.
DR EMBL; X92422; CAA63150.1; -; mRNA.
DR RefSeq; NP_001105472.1; NM_001112002.1.
DR RefSeq; NP_001131602.1; NM_001138130.1.
DR AlphaFoldDB; P27923; -.
DR SMR; P27923; -.
DR STRING; 4577.GRMZM2G431821_P01; -.
DR PaxDb; P27923; -.
DR PRIDE; P27923; -.
DR EnsemblPlants; Zm00001eb369510_T001; Zm00001eb369510_P001; Zm00001eb369510.
DR GeneID; 100192952; -.
DR GeneID; 101027200; -.
DR Gramene; Zm00001eb369510_T001; Zm00001eb369510_P001; Zm00001eb369510.
DR KEGG; zma:100192952; -.
DR KEGG; zma:101027200; -.
DR MaizeGDB; 26015; -.
DR MaizeGDB; 65187; -.
DR eggNOG; KOG0004; Eukaryota.
DR HOGENOM; CLU_010412_2_0_1; -.
DR OrthoDB; 1536766at2759; -.
DR Proteomes; UP000007305; Chromosome 8.
DR ExpressionAtlas; P27923; baseline and differential.
DR Genevisible; P27923; ZM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
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; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000114846"
FT CHAIN 77..155
FT /note="40S ribosomal protein S27a"
FT /id="PRO_0000137682"
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"
FT CONFLICT 80
FT /note="R -> P (in Ref. 3; CAA63150)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="E -> D (in Ref. 3; CAA63150)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="T -> A (in Ref. 3; CAA63150)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="G -> H (in Ref. 3; CAA63150)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="K -> Q (in Ref. 3; CAA63150)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 155 AA; 17682 MW; DE4839F327000B42 CRC64;
MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN
IQKESTLHLV LRLRGGAKKR KKKTYTKPKK IKHKHKKVKL AVLQFYKVDD ATGKVTRLRK
ECPNTECGAG VFMANHFDRH YCGKCGLTYV YNQKA
