NTAN1_PIG
ID NTAN1_PIG Reviewed; 311 AA.
AC Q28955; A0A286ZPV6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 4.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Protein N-terminal asparagine amidohydrolase;
DE EC=3.5.1.121 {ECO:0000269|PubMed:8089117};
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;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-18; 107-119; 215-228
RP AND 234-249.
RC TISSUE=Liver;
RX PubMed=7814382; DOI=10.1074/jbc.270.1.25;
RA Stewart A.E., Arfin S.M., Bradshaw R.A.;
RT "The sequence of porcine protein NH2-terminal asparagine amidohydrolase. A
RT new component of the N-end Rule pathway.";
RL J. Biol. Chem. 270:25-28(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc;
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Liver;
RX PubMed=8089117; DOI=10.1016/s0021-9258(17)31545-4;
RA Stewart A.E., Arfin S.M., Bradshaw R.A.;
RT "Protein NH2-terminal asparagine deamidase. Isolation and characterization
RT of a new enzyme.";
RL J. Biol. Chem. 269:23509-23517(1994).
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:8089117}.
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:8089117};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.265 mM for NHGSGAWL peptide {ECO:0000269|PubMed:8089117};
CC KM=0.325 mM for NAGVELEG peptide {ECO:0000269|PubMed:8089117};
CC KM=0.291 mM for NHGVELEG peptide {ECO:0000269|PubMed:8089117};
CC KM=0.210 mM for NRVYVHPFL peptide {ECO:0000269|PubMed:8089117};
CC KM=0.604 mM for NV peptide {ECO:0000269|PubMed:8089117};
CC KM=0.601 mM for NA peptide {ECO:0000269|PubMed:8089117};
CC Note=kcat is 554 sec(-1) with NHGSGAWL as substrate. kcat is 457
CC sec(-1) with NAGVELEG as substrate. kcat is 470 sec(-1) with NHGVELEG
CC as substrate. kcat is 598 sec(-1) with NRVYVHPFL as substrate. kcat
CC is 398 sec(-1) with NV as substrate. kcat is 354 sec(-1) with NA as
CC substrate. {ECO:0000269|PubMed:8089117};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8089117}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:7814382}.
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DR EMBL; U17062; AAA65019.1; -; mRNA.
DR EMBL; AEMK02000014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A55768; A55768.
DR RefSeq; NP_999207.1; NM_214042.1.
DR AlphaFoldDB; Q28955; -.
DR SMR; Q28955; -.
DR PeptideAtlas; Q28955; -.
DR PRIDE; Q28955; -.
DR Ensembl; ENSSSCT00035086018; ENSSSCP00035035808; ENSSSCG00035063955.
DR Ensembl; ENSSSCT00040080708; ENSSSCP00040034961; ENSSSCG00040059367.
DR GeneID; 397107; -.
DR KEGG; ssc:397107; -.
DR CTD; 123803; -.
DR InParanoid; Q28955; -.
DR OrthoDB; 1433017at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008418; F:protein-N-terminal asparagine amidohydrolase activity; IBA:GO_Central.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR026750; NTAN1.
DR PANTHER; PTHR12498; PTHR12498; 1.
DR Pfam; PF14736; N_Asn_amidohyd; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7814382"
FT CHAIN 2..311
FT /note="Protein N-terminal asparagine amidohydrolase"
FT /id="PRO_0000057973"
FT CONFLICT 122
FT /note="E -> G (in Ref. 1; AAA65019)"
FT CONFLICT 293
FT /note="L -> V (in Ref. 1; AAA65019)"
FT CONFLICT 300
FT /note="G -> A (in Ref. 1; AAA65019)"
FT CONFLICT 309
FT /note="Missing (in Ref. 1; AAA65019)"
SQ SEQUENCE 311 AA; 34890 MW; 28966DE99FC89ADF CRC64;
MPLLVEGRRV RLPQSAGDLV RAHPPLEERA RLLRGQSVQQ VGPQGLLYVQ QRELAVTSPK
DGSVCILGSD DATTCHIVVL RHTGNGATCL THCDGTDTKA EVSLIMSSIK SFSDHTQRGR
LEVHLVGGFS DDRQLSQKLT HQLLSEFDRQ EDDIHLVTLC VTELNDREEN ENHFPIIYGI
AVNVKTAEIY RASFPDRGPE EELRAARVLT GGPMISIYDA KTEQLRIGPY SWMPFPHVDF
WLQQDDKQIL ENLSTSPLAE PPHFVEHIRS TLMFLKKYPS PTNTLFPGNK ALLYKKNEDG
LWKEISSGGE T
