A0A6J2ATK2 · AMPQ_ACIJB
- ProteinAminopeptidase Q
- GeneLVRN
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids992 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo-maternal interface (By similarity).
Involved in coat pigmentation patterns. During skin development, may be required to establish the periodicity of tabby markings, initiating a pre-pattern at or before hair follicle development (PubMed:22997338).
Involved in coat pigmentation patterns. During skin development, may be required to establish the periodicity of tabby markings, initiating a pre-pattern at or before hair follicle development (PubMed:22997338).
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 241 | substrate | ||||
Sequence: E | ||||||
Binding site | 380-384 | substrate | ||||
Sequence: SAMEN | ||||||
Binding site | 416 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 417 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 420 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 439 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Active site | 505 | Proton donor | ||||
Sequence: Y | ||||||
Site | 505 | 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 | cytoplasm | |
Cellular Component | membrane | |
Molecular Function | metalloaminopeptidase activity | |
Molecular Function | peptide binding | |
Molecular Function | zinc ion binding | |
Biological Process | peptide catabolic process | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAminopeptidase Q
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Feliformia > Felidae > Acinonychinae > Acinonyx
Accessions
- Primary accessionA0A6J2ATK2
Proteomes
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 | 2-13 | Cytoplasmic | ||||
Sequence: GPPSSSGFYVSR | ||||||
Transmembrane | 14-34 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: AVALLLAALAAALLLALAVLA | ||||||
Topological domain | 35-992 | Extracellular | ||||
Sequence: ALYGRCARVQPSDLHHGGVPDAASSPRGTQEEQLPTWPPRPTREPAGTATPGHWRPPGPWDQLRLPPWLVPLHYELELWPRLRPNEFQSPTLSFTGRVNITVRCTAATARLLLHSLFLDCESAEVRGPLSSGPRDGAVGRVPVDDVWFAFDMQYMVLELGATLQPGSRYELQLSFSGLVYRDLREGLFFSIYTDQGERRALLASQMEPTFARSVFPCFDEPALKATFNITIIHHPSYGALSNMPKLGQSEKRDVNGSVWTITTFSTTPHMPTYLVALAICDYDHVSRTERGQEIRIWARKDAIANGNAAFALNITGPIFSFLEDLFNISYPLPKTDIIALPTFDNSAMENWGLLIFDESLLLMQPNDQVTDKKAVISFILSHEIGHQWFGNLVTMNWWNDIWLKEGFASYFEFGVINYFNPKFRRNEVFFSNILHHVLSEDHALVSRAVSLKVENFTETSEINELFDLFTYNKGASLARMLSSFLNENVFISALKSYLKTFSYSTAEQDDLWRHFQMVVDDQSKILLPAPVKSIMDRWTHQSGFPVITLNVSTGAMKQEPFYLGKVKNQTLLTHNDTWIVPILWIKNGITQSLVWLDKSSKIFPEMQVSDSDHDWVILNLNMTGYYRVNYDKVGWKKLKQQLEKDPKAIPVIHRLQMIDDAFSLSKNNYVEIETALDLTKYLAEEDEIIVWYAVLVNLVTKDLVFDVNNYDMYPLLKKYLLKRLISIWNMYSTVIRENVAALQDDYLALVALEKLFETACWLGLEDCLQLSRELFKNWTNHPENEIPYPIKSVVLCYGVAFGSDEEWDFLLNMYSNKTKEEERIQLTYAMSCSKDPWILHRYLEYAVTAAPFTFNETNIMEVVAESEVGRYIVKDFLINNWQAVSERYGTQSLVNLMYIIGRTISTDLQITELQQFFSNMLEEHQKLTVRAKLQTIKNKNLGNKKLNARMTAWLRKNT |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000452324 | 2-992 | Aminopeptidase Q | |||
Sequence: GPPSSSGFYVSRAVALLLAALAAALLLALAVLAALYGRCARVQPSDLHHGGVPDAASSPRGTQEEQLPTWPPRPTREPAGTATPGHWRPPGPWDQLRLPPWLVPLHYELELWPRLRPNEFQSPTLSFTGRVNITVRCTAATARLLLHSLFLDCESAEVRGPLSSGPRDGAVGRVPVDDVWFAFDMQYMVLELGATLQPGSRYELQLSFSGLVYRDLREGLFFSIYTDQGERRALLASQMEPTFARSVFPCFDEPALKATFNITIIHHPSYGALSNMPKLGQSEKRDVNGSVWTITTFSTTPHMPTYLVALAICDYDHVSRTERGQEIRIWARKDAIANGNAAFALNITGPIFSFLEDLFNISYPLPKTDIIALPTFDNSAMENWGLLIFDESLLLMQPNDQVTDKKAVISFILSHEIGHQWFGNLVTMNWWNDIWLKEGFASYFEFGVINYFNPKFRRNEVFFSNILHHVLSEDHALVSRAVSLKVENFTETSEINELFDLFTYNKGASLARMLSSFLNENVFISALKSYLKTFSYSTAEQDDLWRHFQMVVDDQSKILLPAPVKSIMDRWTHQSGFPVITLNVSTGAMKQEPFYLGKVKNQTLLTHNDTWIVPILWIKNGITQSLVWLDKSSKIFPEMQVSDSDHDWVILNLNMTGYYRVNYDKVGWKKLKQQLEKDPKAIPVIHRLQMIDDAFSLSKNNYVEIETALDLTKYLAEEDEIIVWYAVLVNLVTKDLVFDVNNYDMYPLLKKYLLKRLISIWNMYSTVIRENVAALQDDYLALVALEKLFETACWLGLEDCLQLSRELFKNWTNHPENEIPYPIKSVVLCYGVAFGSDEEWDFLLNMYSNKTKEEERIQLTYAMSCSKDPWILHRYLEYAVTAAPFTFNETNIMEVVAESEVGRYIVKDFLINNWQAVSERYGTQSLVNLMYIIGRTISTDLQITELQQFFSNMLEEHQKLTVRAKLQTIKNKNLGNKKLNARMTAWLRKNT | ||||||
Glycosylation | 133 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 262 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 289 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 347 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 361 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 489 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 584 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 602 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 609 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 655 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 811 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 850 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 889 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Expression
Tissue specificity
Expressed in skin. Expression levels do not differ between dark and light skin areas.
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 48-92 | Disordered | ||||
Sequence: LHHGGVPDAASSPRGTQEEQLPTWPPRPTREPAGTATPGHWRPPG |
Sequence similarities
Belongs to the peptidase M1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length992
- Mass (Da)113,497
- Last updated2020-10-07 v1
- Checksum49274CDC4859717B
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8N3GNP1 | A0A8N3GNP1_ACIJB | LVRN | 992 |
Polymorphism
A frameshift variant at position 997 (p.Asn977LysfsTer110) has been shown to cosegregate with the king coat pattern, a rare phenotype in which spots coalesce into blotches and stripes. This polymorphism was not detected in almost 220 spotted cheetahs.
Keywords
- Technical term