AAP_NEUCR
ID AAP_NEUCR Reviewed; 24 AA.
AC P22702;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Arginine attenuator peptide;
DE Short=AAP;
DE AltName: Full=Arg-2 leader peptide;
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 [GENOMIC DNA].
RX PubMed=2141606; DOI=10.1016/s0021-9258(19)38545-x;
RA Orbach M.J., Sachs M.S., Yanofsky C.;
RT "The Neurospora crassa arg-2 locus. Structure and expression of the gene
RT encoding the small subunit of arginine-specific carbamoyl phosphate
RT synthetase.";
RL J. Biol. Chem. 265:10981-10987(1990).
RN [2]
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).
RN [3]
RP MUTAGENESIS OF ASP-12.
RX PubMed=8770589; DOI=10.1093/genetics/142.1.117;
RA Freitag M., Dighde N., Sachs M.S.;
RT "A UV-induced mutation in Neurospora that affects translational regulation
RT in response to arginine.";
RL Genetics 142:117-127(1996).
RN [4]
RP FUNCTION.
RX PubMed=8636015; DOI=10.1128/jb.178.8.2172-2177.1996;
RA Luo Z., Sachs M.S.;
RT "Role of an upstream open reading frame in mediating arginine-specific
RT translational control in Neurospora crassa.";
RL J. Bacteriol. 178:2172-2177(1996).
RN [5]
RP FUNCTION.
RX PubMed=9271370; DOI=10.1128/mcb.17.9.4904;
RA Wang Z., Sachs M.S.;
RT "Ribosome stalling is responsible for arginine-specific translational
RT attenuation in Neurospora crassa.";
RL Mol. Cell. Biol. 17:4904-4913(1997).
RN [6]
RP FUNCTION.
RX PubMed=9819438; DOI=10.1128/mcb.18.12.7528;
RA Wang Z., Fang P., Sachs M.S.;
RT "The evolutionarily conserved eukaryotic arginine attenuator peptide
RT regulates the movement of ribosomes that have translated it.";
RL Mol. Cell. Biol. 18:7528-7536(1998).
RN [7]
RP FUNCTION.
RX PubMed=10608810; DOI=10.1074/jbc.274.53.37565;
RA Wang Z., Gaba A., Sachs M.S.;
RT "A highly conserved mechanism of regulated ribosome stalling mediated by
RT fungal arginine attenuator peptides that appears independent of the
RT charging status of arginyl-tRNAs.";
RL J. Biol. Chem. 274:37565-37574(1999).
CC -!- FUNCTION: Arginine attenuator peptide (AAP) that has a regulatory role
CC in the production of arginine-specific carbamoyl phosphate synthetase.
CC Encoded by an upstream open reading frame (uORF) within the 5'-leader
CC region of arginine-specific carbamoyl phosphate synthetase small chain
CC (arg-2) mRNA, it attenuates the translation of the downstream arg-2
CC ORF. In the presence of high concentrations of arginine, ribosomes
CC translating the uORF encoding AAP stall at the termination codon,
CC resulting in reduced translation from the downstream arg-2 initiation
CC codon. {ECO:0000269|PubMed:10608810, ECO:0000269|PubMed:8636015,
CC ECO:0000269|PubMed:9271370, ECO:0000269|PubMed:9819438}.
CC -!- SIMILARITY: Belongs to the arginine attenuator peptide family.
CC {ECO:0000305}.
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DR EMBL; J05512; AAA33610.1; -; Genomic_DNA.
DR EMBL; CM002239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B42224; B42224.
DR PDB; 2XL1; NMR; -; A=1-24.
DR PDBsum; 2XL1; -.
DR AlphaFoldDB; P22702; -.
DR SMR; P22702; -.
DR EvolutionaryTrace; P22702; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0009386; P:translational attenuation; IDA:CACAO.
DR InterPro; IPR013203; Leader_Arg2_CPA1.
DR Pfam; PF08252; Leader_CPA1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Leader peptide; Reference proteome.
FT PEPTIDE 1..24
FT /note="Arginine attenuator peptide"
FT /id="PRO_0000043975"
FT MUTAGEN 12
FT /note="D->N: Eliminates arginine-specific stalling of
FT ribosomes at the termination codon."
FT /evidence="ECO:0000269|PubMed:8770589"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:2XL1"
SQ SEQUENCE 24 AA; 2779 MW; 8FF33F527EAD244C CRC64;
MNGRPSVFTS QDYLSDHLWR ALNA