Detail Information for IndEnz0002015774
IED ID IndEnz0002015774
Enzyme Type ID protease015774
Protein Name Aminopeptidase NAALADL1
EC 3.4.11.-
100 kDa ileum brush border membrane protein
I100
Ileal dipeptidylpeptidase
N-acetylated-alpha-linked acidic dipeptidase-like protein
NAALADase L
Gene Name Naaladl1 Naaladl
Organism Rattus norvegicus (Rat)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat)
Enzyme Sequence MHWAKILGVGIGAAALLGLGIILGHFAIPKATEPLASSVSDSQDLDLAILDSVMGQLDASRIRENLRELSKEPHVATSARDEALVQLLLGRWKDSASGLDTAKTYEYTVLLSFPSTEQPNSVEVVGPNGTVFHSFQPFEKNLTGEQAEPNVLQPYAAYAPPGTPKGPLVYANRGSEDDFKKLEAEGINLKGTIALTRYGSVGRGAKAINAARHGVVGVLVYTDPGDINDGKSLPNETFPNSWGLPPSGVERGSYYEYFGDPLTPYLPAHPVSFRLDPHNISGFPPIPTQPIGFEDAKNLLCNLNGTSAPDSWQGALGCEYKLGPGFEPNGNFPAGSEVKVSVYNRLELRNSSNVLGIIQGAVEPDRYVIYGNHRDSWVHGAVDPSSGTAVLLEISRVLGTLLKKGTWRPRRSIIFASWGAEEFGLIGSTEFTEEFLSKLQERTVTYINVDISVFSNATLRAQGTPPVQSVIFSATKEISAPGSSGLSIYDNWIRYTNRSSPVYGLVPSMGTLGAGSDYASFIHFLGITSMDLAYTYDRSKTSARIYPTYHTAFDTFDYVEKFLDPGFSSHQAVARTAGSVLLRLSDSLFLPLNVSDYSETLQSFLQAAQENLGALLESHNISLGPLVTAVEKFKAAAAALNQHILTLQKSSPDPLQVRMVNDQLMLLERAFLNPRAFPEERYYSHVLWAPNTASVATFPGLANAYARAQEINSGAEAWAEVERQLSIAVMALEGAAATLQPVTDL
Enzyme Length 745
Uniprot Accession Number O54697
Absorption
Active Site ACT_SITE 421; /note=Proton donor/acceptor; /evidence=ECO:0000250|UniProtKB:Q9UQQ1
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.11.-
Enzyme Function FUNCTION: Aminopeptidase with broad substrate specificity. Has lower activity with substrates that have Asp or Glu in the P2' position, or Pro in the P3' position. Lacks activity with substrates that have both Pro in the P3' position and Asp or Glu in the P2' position. Lacks carboxypeptidase activity. Lacks dipeptidyl-peptidase IV type activity. {ECO:0000250|UniProtKB:Q9UQQ1}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Disulfide bond (1); Glycosylation (10); Metal binding (10); Topological domain (2); Transmembrane (1)
Keywords Aminopeptidase;Calcium;Cell membrane;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:9388249}; Single-pass type II membrane protein {ECO:0000305|PubMed:9388249}. Note=Ileal brush border membrane. {ECO:0000269|PubMed:9388249}.
Modified Residue
Post Translational Modification PTM: N-glycosylated. {ECO:0000269|PubMed:9388249}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 80,641
Kinetics
Metal Binding METAL 263; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q9UQQ1; METAL 266; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q9UQQ1; METAL 373; /note=Zinc 1; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q9UQQ1; METAL 383; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q9UQQ1; METAL 383; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q9UQQ1; METAL 422; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:Q9UQQ1; METAL 430; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q9UQQ1; METAL 433; /note=Calcium; /evidence=ECO:0000250|UniProtKB:Q9UQQ1; METAL 450; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:Q9UQQ1; METAL 550; /note=Zinc 2; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:Q9UQQ1
Rhea ID
Cross Reference Brenda