Q2KHK3 · AMPQ_MOUSE
- ProteinAminopeptidase Q
- GeneLvrn
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids559 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo-maternal interface. On synthetic substrates it shows a marked preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met-MCA, Arg-LCA and Lys-LCA. Cleaves the N-terminal amino acid of several peptides such as angiotensin-3, kisspeptin-10 and endokinin C.
Cofactor
Note: Binds 1 zinc ion per subunit.
Activity regulation
Inhibited by bestatin.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 237 | substrate | ||||
Sequence: E | ||||||
Binding site | 376-380 | substrate | ||||
Sequence: GAMEN | ||||||
Binding site | 412 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 413 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 416 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 435 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Site | 501 | Transition state stabilizer | ||||
Sequence: Y |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | metallopeptidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAminopeptidase Q
- EC number
- Short namesAP-Q ; APQ
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ2KHK3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-13 | Cytoplasmic | ||||
Sequence: MSRPFSSGVYVSR | ||||||
Transmembrane | 14-34 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: GVALLLAALTAVLLLVLVALA | ||||||
Topological domain | 35-559 | Lumenal | ||||
Sequence: SLYGSCAHVQPSEQGNSRVKNTSLWPPGGQEWALPTPAQEPTVGTSQDLGPPSGPWDHLRLPPWLVPLHYDLELWPWLQPDKLSPPNLTFTGRVNITVRCTVASSRLLLHSFLLNYKQVEVWGPLAQDTRNATVGRVQVEKVWFAPDMQFVVLDLGQSLEPGSRYELSFHFSGQVLQVGLEGLFLNLYHDEDELRALVATQMEPTFARHVFPCFDEPALKATFNITVIHHPGYAALSNMPQLGQSERIDVNGSRWTVTTFHTTPRMPTYLVALVVCDLDHISRTERGKEIRVWARKDDIANGYLDFAANITGPIFSFLEDLFNISYRLPKTDIVALPIFASGAMENWGLLIFDESSLLLEPEDELTEKRAMILSIIAHEVGHQWFGNLVTMSWWNNIWLNEGFASYFELELTNYFYPKVPMNMIFFFTVLHGILGEDHALESRAVSTAVENFTETSEINRLFDLYTYKKGACMAWMLASFLSPHLFINALKSYLETFSYSNAEQDDLWRHIQMVIVPFRHFLAEH |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000247069 | 1-559 | Aminopeptidase Q | |||
Sequence: MSRPFSSGVYVSRGVALLLAALTAVLLLVLVALASLYGSCAHVQPSEQGNSRVKNTSLWPPGGQEWALPTPAQEPTVGTSQDLGPPSGPWDHLRLPPWLVPLHYDLELWPWLQPDKLSPPNLTFTGRVNITVRCTVASSRLLLHSFLLNYKQVEVWGPLAQDTRNATVGRVQVEKVWFAPDMQFVVLDLGQSLEPGSRYELSFHFSGQVLQVGLEGLFLNLYHDEDELRALVATQMEPTFARHVFPCFDEPALKATFNITVIHHPGYAALSNMPQLGQSERIDVNGSRWTVTTFHTTPRMPTYLVALVVCDLDHISRTERGKEIRVWARKDDIANGYLDFAANITGPIFSFLEDLFNISYRLPKTDIVALPIFASGAMENWGLLIFDESSLLLEPEDELTEKRAMILSIIAHEVGHQWFGNLVTMSWWNNIWLNEGFASYFELELTNYFYPKVPMNMIFFFTVLHGILGEDHALESRAVSTAVENFTETSEINRLFDLYTYKKGACMAWMLASFLSPHLFINALKSYLETFSYSNAEQDDLWRHIQMVIVPFRHFLAEH | ||||||
Glycosylation | 121 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 129 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 258 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 285 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 343 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
N-glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Sequence
- Sequence statusComplete
- Length559
- Mass (Da)63,338
- Last updated2007-01-23 v3
- Checksum8C1FF55A36AE05F3
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A3Q4L2Z6 | A0A3Q4L2Z6_MOUSE | Lvrn | 559 | ||
E9QJR0 | E9QJR0_MOUSE | Lvrn | 991 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 335 | in Ref. 1; BAB29490 | ||||
Sequence: N → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK014652 EMBL· GenBank· DDBJ | BAB29490.1 EMBL· GenBank· DDBJ | mRNA | ||
BC113158 EMBL· GenBank· DDBJ | AAI13159.1 EMBL· GenBank· DDBJ | mRNA |