RS27A_NEUCR
ID RS27A_NEUCR Reviewed; 154 AA.
AC P14799; P13117; Q7RVR9; Q7RVX5; Q7RWD8; V5IMD6;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 4.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Ubiquitin-40S ribosomal protein S27a;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Contains:
DE RecName: Full=40S ribosomal protein S27a;
DE AltName: Full=Cytoplasmic ribosomal protein 6;
DE Short=CRP6;
DE AltName: Full=S37;
DE Flags: Precursor;
GN Name=ubi::crp-6; Synonyms=ubi-3; ORFNames=NCU04553;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=74-ORS-6a / FGSC 4200;
RX PubMed=1650731; DOI=10.1016/0378-1119(91)90552-m;
RA Taccioli G.E., Grotewold E., Aisemberg G.O., Judewicz D.N.;
RT "The cDNA sequence and expression of an ubiquitin-tail gene fusion in
RT Neurospora crassa.";
RL Gene 102:133-137(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=8088539; DOI=10.1016/0378-1119(94)90053-1;
RA Tarawneh K.A., Anumula K.R., Free S.J.;
RT "The isolation and characterization of a Neurospora crassa gene (ubi::crp-
RT 6) encoding a ubiquitin-40S ribosomal protein fusion protein.";
RL Gene 147:137-140(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(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-6-linked may be involved in DNA repair; Lys-11-linked is involved
CC in ERAD (endoplasmic reticulum-associated degradation) and in cell-
CC cycle regulation; Lys-29-linked is involved in lysosomal degradation;
CC Lys-33-linked is involved in kinase modification; Lys-48-linked is
CC involved in protein degradation via the proteasome; Lys-63-linked is
CC involved in endocytosis, and DNA-damage responses. Linear polymer
CC chains formed via attachment by the initiator Met lead to cell
CC signaling. Ubiquitin is usually conjugated to Lys residues of target
CC proteins, however, in rare cases, conjugation to Cys or Ser residues
CC 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 encoded by 3 different genes. Crp-79 is
CC synthesized as a polyprotein with one copy of ubiquitin fused to
CC ribosomal protein L40. Crp-6/ubi-3 is a polyprotein with one copy of
CC ubiquitin fused to ribosomal protein S27a. Ubi is a polyprotein
CC containing 4 exact head to tail repeats of 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; X15338; CAA33390.1; -; mRNA.
DR EMBL; U01221; AAA03351.1; -; mRNA.
DR EMBL; U01220; AAA56880.1; -; Genomic_DNA.
DR EMBL; CM002242; ESA41890.1; -; Genomic_DNA.
DR EMBL; CM002242; ESA41891.1; -; Genomic_DNA.
DR PIR; PQ0201; UQNCR.
DR PIR; T46664; T46664.
DR RefSeq; XP_011395193.1; XM_011396891.1.
DR RefSeq; XP_011395194.1; XM_011396892.1.
DR PDB; 7R81; EM; 2.70 A; g2=1-154.
DR PDBsum; 7R81; -.
DR AlphaFoldDB; P14799; -.
DR SMR; P14799; -.
DR STRING; 5141.EFNCRP00000005481; -.
DR PRIDE; P14799; -.
DR EnsemblFungi; ESA41890; ESA41890; NCU04553.
DR EnsemblFungi; ESA41891; ESA41891; NCU04553.
DR GeneID; 3872092; -.
DR KEGG; ncr:NCU04553; -.
DR VEuPathDB; FungiDB:NCU04553; -.
DR HOGENOM; CLU_010412_2_0_1; -.
DR InParanoid; P14799; -.
DR OMA; FMAQHAN; -.
DR Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
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: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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation;
KW Zinc; Zinc-finger.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000396485"
FT CHAIN 77..154
FT /note="40S ribosomal protein S27a"
FT /id="PRO_0000137686"
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 CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT CROSSLNK 29
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
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 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 115
FT /note="E -> D (in Ref. 1; AAA03351 and 2; AAA56880)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 154 AA; 17739 MW; 83086792A3AF9432 CRC64;
MQIFVKTLTG KTITLEVESS DTIDNVKQKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGGKKR KKKVYTTPKK IKHKRKKTKL AVLKYYKVDS DGKIERLRRE
CPNETCGAGV FMAAMQDRQY CGRCHLTYVF EKSS
