NTAN1_MOUSE
ID NTAN1_MOUSE Reviewed; 310 AA.
AC Q64311;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Protein N-terminal asparagine amidohydrolase {ECO:0000303|PubMed:8910481};
DE EC=3.5.1.121 {ECO:0000269|PubMed:8910481};
DE AltName: Full=Protein NH2-terminal asparagine amidohydrolase;
DE Short=PNAA;
DE AltName: Full=Protein NH2-terminal asparagine deamidase;
DE Short=PNAD;
DE Short=Protein N-terminal Asn amidase;
DE Short=Protein NTN-amidase;
GN Name=Ntan1 {ECO:0000303|PubMed:8910481, ECO:0000312|MGI:MGI:108471};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=C129;
RX PubMed=8910481; DOI=10.1074/jbc.271.45.28521;
RA Grigoryev S., Stewart A.E., Kwon Y.T., Arfin S.M., Bradshaw R.A.,
RA Jenkins N.A., Copeland N.G., Varshavsky A.;
RT "A mouse amidase specific for N-terminal asparagine. The gene, the enzyme,
RT and their function in the N-end rule pathway.";
RL J. Biol. Chem. 271:28521-28532(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: N-terminal asparagine deamidase that mediates deamidation of
CC N-terminal asparagine residues to aspartate. Required for the
CC ubiquitin-dependent turnover of intracellular proteins that initiate
CC with Met-Asn. These proteins are acetylated on the retained initiator
CC methionine and can subsequently be modified by the removal of N-acetyl
CC methionine by acylaminoacid hydrolase (AAH). Conversion of the
CC resulting N-terminal asparagine to aspartate by NTAN1/PNAD renders the
CC protein susceptible to arginylation, polyubiquitination and degradation
CC as specified by the N-end rule. This enzyme does not act on substrates
CC with internal or C-terminal asparagines and does not act on glutamine
CC residues in any position. {ECO:0000269|PubMed:8910481}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O + N-terminal L-asparaginyl-[protein] = N-terminal
CC L-aspartyl-[protein] + NH4(+); Xref=Rhea:RHEA:50676, Rhea:RHEA-
CC COMP:12669, Rhea:RHEA-COMP:12776, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:50348,
CC ChEBI:CHEBI:64720; EC=3.5.1.121;
CC Evidence={ECO:0000269|PubMed:8910481};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q28955}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q28955}.
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DR EMBL; U57692; AAB66490.1; -; mRNA.
DR EMBL; U57691; AAC52885.1; -; Genomic_DNA.
DR EMBL; BC030172; AAH30172.1; -; mRNA.
DR CCDS; CCDS27969.1; -.
DR RefSeq; NP_035076.1; NM_010946.4.
DR AlphaFoldDB; Q64311; -.
DR SMR; Q64311; -.
DR STRING; 10090.ENSMUSP00000023362; -.
DR PhosphoSitePlus; Q64311; -.
DR EPD; Q64311; -.
DR MaxQB; Q64311; -.
DR PaxDb; Q64311; -.
DR PeptideAtlas; Q64311; -.
DR PRIDE; Q64311; -.
DR ProteomicsDB; 252863; -.
DR Antibodypedia; 24973; 98 antibodies from 20 providers.
DR DNASU; 18203; -.
DR Ensembl; ENSMUST00000023362; ENSMUSP00000023362; ENSMUSG00000022681.
DR GeneID; 18203; -.
DR KEGG; mmu:18203; -.
DR UCSC; uc007ygk.2; mouse.
DR CTD; 123803; -.
DR MGI; MGI:108471; Ntan1.
DR VEuPathDB; HostDB:ENSMUSG00000022681; -.
DR eggNOG; ENOG502QSQW; Eukaryota.
DR GeneTree; ENSGT00390000016730; -.
DR HOGENOM; CLU_077981_1_0_1; -.
DR InParanoid; Q64311; -.
DR OMA; YVQQREM; -.
DR OrthoDB; 1433017at2759; -.
DR PhylomeDB; Q64311; -.
DR TreeFam; TF325597; -.
DR BRENDA; 3.5.1.121; 3474.
DR BioGRID-ORCS; 18203; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Ntan1; mouse.
DR PRO; PR:Q64311; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q64311; protein.
DR Bgee; ENSMUSG00000022681; Expressed in cortical plate and 266 other tissues.
DR ExpressionAtlas; Q64311; baseline and differential.
DR Genevisible; Q64311; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0008418; F:protein-N-terminal asparagine amidohydrolase activity; IDA:MGI.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR GO; GO:0007613; P:memory; IMP:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:MGI.
DR InterPro; IPR026750; NTAN1.
DR PANTHER; PTHR12498; PTHR12498; 1.
DR Pfam; PF14736; N_Asn_amidohyd; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..310
FT /note="Protein N-terminal asparagine amidohydrolase"
FT /id="PRO_0000057972"
SQ SEQUENCE 310 AA; 34595 MW; 09B1611DF3366959 CRC64;
MPLLVDGQRV RLPRSAVELV RAHPPLEERA RLLRGQSVQQ VGPQGLLYVQ QRELAVTSPK
DGSISILGSD DATTCHIVVL RHTGNGATCL THCDGSDTKA EVPLIMSSIK SFSEHAECGR
LEVHLVGGFS DDRQLSQKLT HQLLSEFDKQ DDDIHLVTLC VTELNDREEN ENHFPIIYGI
AVNIKTAEIY RASFQDRGPE EQLRAARALA GGPMISIYDA KTEQLRIGPC SWTPFPQVDF
WLQQDDKQIL ESLSTSPLAE PPHFVEHIRS TLMFLKKFPS PENILFPGNK ALLYKKNKDG
LWEKISSPGS
