R27AC_ARATH
ID R27AC_ARATH Reviewed; 157 AA.
AC P59233; O80715; P19233; P59263; Q0WV69; Q38875; Q9LDJ2; Q9LYW1; Q9M0W3;
AC Q9M1P9; Q9S7X3;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Ubiquitin-40S ribosomal protein S27a-3;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Contains:
DE RecName: Full=40S ribosomal protein S27a-3;
DE Flags: Precursor;
GN Name=RPS27AC; Synonyms=UBQ5; OrderedLocusNames=At3g62250;
GN ORFNames=T17J13.210;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=2165066; DOI=10.1016/s0021-9258(19)38372-3;
RA Callis J., Raasch J.A., Vierstra R.D.;
RT "Ubiquitin extension proteins of Arabidopsis thaliana. Structure,
RT localization, and expression of their promoters in transgenic tobacco.";
RL J. Biol. Chem. 265:12486-12493(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX PubMed=11598216; DOI=10.1104/pp.010265;
RA Barakat A., Szick-Miranda K., Chang I.-F., Guyot R., Blanc G., Cooke R.,
RA Delseny M., Bailey-Serres J.;
RT "The organization of cytoplasmic ribosomal protein genes in the Arabidopsis
RT genome.";
RL Plant Physiol. 127:398-415(2001).
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-11-linked is involved in ERAD (endoplasmic reticulum-associated
CC degradation) and in cell-cycle regulation; Lys-29-linked is involved in
CC lysosomal degradation; Lys-33-linked is involved in kinase
CC modification; Lys-48-linked is involved in protein degradation via the
CC proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage
CC responses. Linear polymer chains formed via attachment by the initiator
CC Met lead to cell signaling. Ubiquitin is usually conjugated to Lys
CC residues of target proteins, however, in rare cases, conjugation to Cys
CC or Ser residues has been observed. When polyubiquitin is free
CC (unanchored-polyubiquitin), it also has distinct roles, such as in
CC activation of protein kinases, and in signaling (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Ribosomal protein RSP27a-3 is a component of the 40S subunit
CC of the ribosome.
CC -!- SUBUNIT: Ribosomal protein RSP27a-3 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 encoded by 16 different genes. Ubiquitin is
CC generally synthesized as a polyubiquitin precursor with tandem head to
CC tail repeats. Often, there is one to three additional amino acids after
CC the last repeat, removed in the mature protein. Alternatively,
CC ubiquitin extension protein is synthesized as a single copy of
CC ubiquitin fused to a ribosomal protein (either L40 or S27A) or to a
CC ubiquitin-related protein (either RUB1 or RUB2). Following translation,
CC extension protein is cleaved from 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; J05539; AAA32906.1; -; Genomic_DNA.
DR EMBL; AL138651; CAB71885.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80327.1; -; Genomic_DNA.
DR EMBL; AY052219; AAK97689.1; -; mRNA.
DR EMBL; AY139810; AAM98116.1; -; mRNA.
DR EMBL; AK226902; BAE98979.1; -; mRNA.
DR EMBL; AY084978; AAM61537.1; -; mRNA.
DR PIR; C36571; C36571.
DR RefSeq; NP_191784.1; NM_116090.3.
DR AlphaFoldDB; P59233; -.
DR SMR; P59233; -.
DR BioGRID; 10712; 5.
DR IntAct; P59233; 2.
DR STRING; 3702.AT3G62250.1; -.
DR PaxDb; P59233; -.
DR PRIDE; P59233; -.
DR ProteomicsDB; 236621; -.
DR EnsemblPlants; AT3G62250.1; AT3G62250.1; AT3G62250.
DR GeneID; 825398; -.
DR Gramene; AT3G62250.1; AT3G62250.1; AT3G62250.
DR KEGG; ath:AT3G62250; -.
DR Araport; AT3G62250; -.
DR TAIR; locus:2098003; AT3G62250.
DR eggNOG; KOG0004; Eukaryota.
DR HOGENOM; CLU_010412_2_0_1; -.
DR InParanoid; P59233; -.
DR OMA; CINKPED; -.
DR OrthoDB; 1536766at2759; -.
DR PRO; PR:P59233; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P59233; baseline and differential.
DR Genevisible; P59233; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
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; Zinc; Zinc-finger.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000396873"
FT CHAIN 77..157
FT /note="40S ribosomal protein S27a-3"
FT /id="PRO_0000137676"
FT ZN_FING 121..144
FT /note="C4-type"
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 157 AA; 17797 MW; A8F1A3EAD7EFD558 CRC64;
MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN
IQKESTLHLV LRLRGGAKKR KKKTYTKPKK IKHKHKKVKL AVLQFYKIDG SGKVQRLRKE
CPNATCGAGT FMASHFDRHY CGKCGLTYVY QKEGVEA
