R27AB_ORYSJ
ID R27AB_ORYSJ Reviewed; 155 AA.
AC P51431; B7F573; O82079; P03993; P69321; Q0DKI9; Q652Q2; Q67UR4; Q69P70;
AC Q6ATC2; Q7XN78; Q8S5Y3; Q9AR09;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 3.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Ubiquitin-40S ribosomal protein S27a-2;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Contains:
DE RecName: Full=40S ribosomal protein S27a-2;
DE Flags: Precursor;
GN Name=RPS27AB; Synonyms=UBQ6;
GN OrderedLocusNames=Os05g0160200, LOC_Os05g06770;
GN ORFNames=OsJ_17209 {ECO:0000312|EMBL:EEE62418.1}, OSJNBa0017J22.14,
GN OSJNBa0034O12.6;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7610191; DOI=10.1104/pp.108.2.865;
RA Kim H.U., Yun C.H., Cho W.S., Kang S.K., Chung T.Y.;
RT "Nucleotide sequence of rice cDNA that encodes a ubiquitin protein and a
RT 79-amino acid protein.";
RL Plant Physiol. 108:865-865(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(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 Lys-63-linked is involved in endocytosis, and DNA-damage responses.
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 RSP27a-2 is a component of the 40S subunit
CC of the ribosome.
CC -!- SUBUNIT: Ribosomal protein RSP27a-2 is part of the 40S ribosomal
CC subunit. {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; L31941; AAA74960.1; -; mRNA.
DR EMBL; AC119288; AAV43924.1; -; Genomic_DNA.
DR EMBL; AC137614; AAT93912.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF16634.2; -; Genomic_DNA.
DR EMBL; AP014961; BAS92399.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE62418.1; -; Genomic_DNA.
DR EMBL; AK119731; BAG99770.1; -; mRNA.
DR PIR; T04026; T04026.
DR RefSeq; XP_015639337.1; XM_015783851.1.
DR AlphaFoldDB; P51431; -.
DR SMR; P51431; -.
DR STRING; 4530.OS05T0160200-01; -.
DR PaxDb; P51431; -.
DR PRIDE; P51431; -.
DR EnsemblPlants; Os05t0160200-01; Os05t0160200-01; Os05g0160200.
DR GeneID; 4337883; -.
DR Gramene; Os05t0160200-01; Os05t0160200-01; Os05g0160200.
DR KEGG; osa:4337883; -.
DR eggNOG; KOG0004; Eukaryota.
DR HOGENOM; CLU_010412_2_0_1; -.
DR InParanoid; P51431; -.
DR OMA; CINKPED; -.
DR OrthoDB; 1536766at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR Genevisible; P51431; OS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; IEA:UniProt.
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_0000396876"
FT CHAIN 77..155
FT /note="40S ribosomal protein S27a-2"
FT /id="PRO_0000137683"
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 63
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 20..21
FT /note="SD -> RH (in Ref. 1; AAA74960)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="L -> F (in Ref. 1; AAA74960)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="L -> H (in Ref. 1; AAA74960)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="N -> H (in Ref. 1; AAA74960)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="G -> R (in Ref. 1; AAA74960)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="G -> R (in Ref. 1; AAA74960)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 155 AA; 17683 MW; 27881BF3270100F2 CRC64;
MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN
IQKESTLHLV LRLRGGAKKR KKKTYTKPKK IKHKHKKVKL AVLQFYKVDD ATGKVTRLRK
ECPNNDCGAG TFMANHFDRH YCGKCGLTYV YNQKA
