Q8C129 · LCAP_MOUSE
- ProteinLeucyl-cystinyl aminopeptidase
- GeneLnpep
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1025 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Release of an N-terminal amino acid, cleave before cysteine, leucine as well as other amino acids. Degrades peptide hormones such as oxytocin, vasopressin and angiotensin III, and plays a role in maintaining homeostasis during pregnancy. May be involved in the inactivation of neuronal peptides in the brain. Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may be the angiotensin IV receptor in the brain (By similarity).
Catalytic activity
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 295 | substrate | ||||
Sequence: E | ||||||
Binding site | 428-432 | substrate | ||||
Sequence: GAMEN | ||||||
Binding site | 464 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 465 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 468 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 487 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Site | 549 | Transition state stabilizer | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell surface | |
Cellular Component | cytoplasm | |
Cellular Component | cytoplasmic vesicle membrane | |
Cellular Component | extracellular space | |
Cellular Component | insulin-responsive compartment | |
Cellular Component | membrane | |
Cellular Component | neuronal cell body | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | plasma membrane | |
Cellular Component | vesicle | |
Molecular Function | aminopeptidase activity | |
Molecular Function | metalloaminopeptidase activity | |
Molecular Function | peptide binding | |
Molecular Function | zinc ion binding | |
Biological Process | negative regulation of cold-induced thermogenesis | |
Biological Process | neuropeptide catabolic process | |
Biological Process | peptide catabolic process | |
Biological Process | positive regulation of blood pressure | |
Biological Process | protein catabolic process | |
Biological Process | proteolysis | |
Biological Process | regulation of blood pressure | |
Biological Process | regulation of long-term neuronal synaptic plasticity | |
Biological Process | response to hormone |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameLeucyl-cystinyl aminopeptidase
- EC number
- Short namesCystinyl aminopeptidase
- 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 accessionQ8C129
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type II membrane protein
Endomembrane system ; Single-pass type II membrane protein
Note: Localized mainly in intracellular vesicles together with GLUT4. Relocalizes to the plasma membrane in response to insulin. The dileucine internalization motif and/or the interaction with tankyrases may be involved in intracellular sequestration (By similarity).
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-109 | Cytoplasmic | ||||
Sequence: MESFTNDRLQLPRNMIENSMFEEEPDVVDLAKEPCLHPLEPDEVEYEPRGSRLLVRGLGEHEMDEDEEDYESSAKLLGMSFMNRSSGLRNSAAGYRQSPDGTCSLPSAR | ||||||
Transmembrane | 110-131 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: TLVICVFVIVVAVSVIMVIYLL | ||||||
Topological domain | 132-1025 | Extracellular | ||||
Sequence: PRCTFTKEGCHKTNQSAELIQPVATNGKVFPWAQIRLPTAIIPLCYELSLHPNLTSMTFRGSVTISLQALQDTRDIILHSTGHNISRVTFMSAVSSQEKQVEILEYPYHEQIAVVAPEPLLTGHNYTLKIEYSANISNSYYGFYGITYTDKSNEKKYFAATQFEPLAARSAFPCFDEPAFKATFIIKITRNEHHTALSNMPKKSSVPAEEGLIQDEFSESVKMSTYLVAFIVGEMRNLSQDVNGTLVSVYAVPEKIGQVHHALDTTIKLLEFYQTYFEIQYPLKKLDLVAIPDFEAGAMENWGLLTFREETLLYDNATSSVADRKLVTKIIAHELAHQWFGNLVTMQWWNDLWLNEGFATFMEYFSVEKIFKELNSYEDFLDARFKTMRKDSLNSSHPISSSVQSSEQIEEMFDSLSYFKGASLLLMLKSYLSEDVFRHAVILYLHNHSYAAIQSDDLWDSFNEVTDKTLDVKKMMKTWTLQKGFPLVTVQRKGTELLLQQERFFLRMQPESQPSDTSHLWHIPISYVTDGRNYSEYRSVSLLDKKSDVINLTEQVQWVKVNSNMTGYYIVHYAHDDWTALINQLKRNPYVLSDKDRANLINNIFELAGLGKVPLRMAFDLIDYLKNETHTAPITEALFQTNLIYNLLEKLGHMDLSSRLVARVHKLLQNQIQQQTWTDEGTPSMRELRSALLEFACAHSLENCTTMATNLFDSWMASNGTQSLPTDVMVTVFKVGARTEKGWLFLFSMYSSMGSEAEKNKILEALASSEDVHKLYWLMKSSLDGDIIRTQKLSLIIRTVGRHFPGHLLAWDFVKENWNKLVHKFHLGSYTIQSIVAGSTHLFSTKTHLSEVQAFFENQSEATLKLRCVQEALEVIQLNIQWMVRNLKTLSQWL |
Keywords
- Cellular component
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 42 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for modified residue, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000278198 | 1-1025 | Leucyl-cystinyl aminopeptidase | |||
Sequence: MESFTNDRLQLPRNMIENSMFEEEPDVVDLAKEPCLHPLEPDEVEYEPRGSRLLVRGLGEHEMDEDEEDYESSAKLLGMSFMNRSSGLRNSAAGYRQSPDGTCSLPSARTLVICVFVIVVAVSVIMVIYLLPRCTFTKEGCHKTNQSAELIQPVATNGKVFPWAQIRLPTAIIPLCYELSLHPNLTSMTFRGSVTISLQALQDTRDIILHSTGHNISRVTFMSAVSSQEKQVEILEYPYHEQIAVVAPEPLLTGHNYTLKIEYSANISNSYYGFYGITYTDKSNEKKYFAATQFEPLAARSAFPCFDEPAFKATFIIKITRNEHHTALSNMPKKSSVPAEEGLIQDEFSESVKMSTYLVAFIVGEMRNLSQDVNGTLVSVYAVPEKIGQVHHALDTTIKLLEFYQTYFEIQYPLKKLDLVAIPDFEAGAMENWGLLTFREETLLYDNATSSVADRKLVTKIIAHELAHQWFGNLVTMQWWNDLWLNEGFATFMEYFSVEKIFKELNSYEDFLDARFKTMRKDSLNSSHPISSSVQSSEQIEEMFDSLSYFKGASLLLMLKSYLSEDVFRHAVILYLHNHSYAAIQSDDLWDSFNEVTDKTLDVKKMMKTWTLQKGFPLVTVQRKGTELLLQQERFFLRMQPESQPSDTSHLWHIPISYVTDGRNYSEYRSVSLLDKKSDVINLTEQVQWVKVNSNMTGYYIVHYAHDDWTALINQLKRNPYVLSDKDRANLINNIFELAGLGKVPLRMAFDLIDYLKNETHTAPITEALFQTNLIYNLLEKLGHMDLSSRLVARVHKLLQNQIQQQTWTDEGTPSMRELRSALLEFACAHSLENCTTMATNLFDSWMASNGTQSLPTDVMVTVFKVGARTEKGWLFLFSMYSSMGSEAEKNKILEALASSEDVHKLYWLMKSSLDGDIIRTQKLSLIIRTVGRHFPGHLLAWDFVKENWNKLVHKFHLGSYTIQSIVAGSTHLFSTKTHLSEVQAFFENQSEATLKLRCVQEALEVIQLNIQWMVRNLKTLSQWL | ||||||
Modified residue | 70 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 80 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 91 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 145 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 184 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 215 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 256 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 266 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 368 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 374 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 447 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 525 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 578 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 664 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 682 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 695 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 758 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 834 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 850 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 989 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for motif, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 53-54 | Dileucine internalization motif | ||||
Sequence: LL | ||||||
Motif | 76-77 | Dileucine internalization motif | ||||
Sequence: LL | ||||||
Region | 96-101 | Tankyrase binding | ||||
Sequence: RQSPDG |
Sequence similarities
Belongs to the peptidase M1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,025
- Mass (Da)117,304
- Last updated2003-03-01 v1
- ChecksumAD6F98196EBA683B
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK029094 EMBL· GenBank· DDBJ | BAC26293.1 EMBL· GenBank· DDBJ | mRNA | ||
BC120925 EMBL· GenBank· DDBJ | AAI20926.1 EMBL· GenBank· DDBJ | mRNA | ||
BC120926 EMBL· GenBank· DDBJ | AAI20927.1 EMBL· GenBank· DDBJ | mRNA |