Protein detail

AMPE

Glutamyl aminopeptidase (EAP) (EC 3.4.11.7) (Aminopeptidase A) (AP-A) (Differentiation antigen gp160) (CD antigen CD249)

Protein symbol
AMPE
UniProt ID
EVMP score
0.25
Frequency
1
Transmembrane count
1
Protein classification
CD markersEnzymesPlasma proteinsPredicted membrane proteins
Basic Information
Protein Names
Glutamyl aminopeptidase (EAP) (EC 3.4.11.7) (Aminopeptidase A) (AP-A) (Differentiation antigen gp160) (CD antigen CD249)
Protein Class
CD markersEnzymesPlasma proteinsPredicted membrane proteins
Protein Function
  • Peptidases:Metallopeptidases
  • Enzymes
  • CD markers
  • ENZYME proteins:Hydrolases
Transmembrane
19..39; Helical; Signal-anchor for type II membrane protein
Transmembrane Count
1
Entrez Gene Symbol
Gene Synonym
CD249gp160
Gene Description
Glutamyl aminopeptidase
Chromosome
4
Position
110365733-110565285
Frequency
1
EVMP Score
0.25
Fluorescence & Localization
Function & Pathway
Relations & Evidence

Enzyme-Mediated Modification

0 records.

Ligand-Receptor Signaling

25 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
cell_surfacecell_surfaceOmniPathNoNoNoNoNo
transmembranetransmembrane_predictedPhobiusNoNoNoNoNo
transmembrane_phobiustransmembrane_predictedAlmen2009NoNoNoNoNo
transmembrane_sosuitransmembrane_predictedAlmen2009NoNoNoNoNo
transmembrane_tmhmmtransmembrane_predictedAlmen2009NoNoNoNoNo
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Regulatory Interaction Network

0 records.

Protein Complex Composition

0 records.

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationSize Exclusion ChromatographyELISA126775013
Sequence, Structure & Domains

Sequences

Length
957
Mass
109,244
Sequence
MNFAEREGSKRYCIQTKHVAILCAVVVGVGLIVGLAVGLTRSCDSSGDGGPGTAPAPSHLPSSTASPSGPPAQDQDICPASEDESGQWKNFRLPDFVNPVHYDLHVKPLLEEDTYTGTVSISINLSAPTRYLWLHLRETRITRLPELKRPSGDQVQVRRCFEYKKQEYVVVEAEEELTPSSGDGLYLLTMEFAGWLNGSLVGFYRTTYTENGQVKSIVATDHEPTDARKSFPCFDEPNKKATYTISITHPKEYGALSNMPVAKEESVDDKWTRTTFEKSVPMSTYLVCFAVHQFDSVKRISNSGKPLTIYVQPEQKHTAEYAANITKSVFDYFEEYFAMNYSLPKLDKIAIPDFGTGAMENWGLITYRETNLLYDPKESASSNQQRVATVVAHELVHQWFGNIVTMDWWEDLWLNEGFASFFEFLGVNHAETDWQMRDQMLLEDVLPVQEDDSLMSSHPIIVTVTTPDEITSVFDGISYSKGSSILRMLEDWIKPENFQKGCQMYLEKYQFKNAKTSDFWAALEEASRLPVKEVMDTWTRQMGYPVLNVNGVKNITQKRFLLDPRANPSQPPSDLGYTWNIPVKWTEDNITSSVLFNRSEKEGITLNSSNPSGNAFLKINPDHIGFYRVNYEVATWDSIATALSLNHKTFSSADRASLIDDAFALARAQLLDYKVALNLTKYLKREENFLPWQRVISAVTYIISMFEDDKELYPMIEEYFQGQVKPIADSLGWNDAGDHVTKLLRSSVLGFACKMGDREALNNASSLFEQWLNGTVSLPVNLRLLVYRYGMQNSGNEISWNYTLEQYQKTSLAQEKEKLLYGLASVKNVTLLSRYLDLLKDTNLIKTQDVFTVIRYISYNSYGKNMAWNWIQLNWDYLVNRYTLNNRNLGRIVTIAEPFNTELQLWQMESFFAKYPQAGAGEKPREQVLETVKNNIEWLKQHRNTIREWFFNLLESG

3D Structural Models

Turn
223..226; 376..378; 401..403; 551..553; 574..577; 679..682; 706..708; 780..782; 842..844
Helix
87..89; 110..112; 164..166; 227..230; 284..286; 313..319; 320..336; 369..371; 381..397; 409..412; 413..430; 432..434; 436..443; 445..451; 467..472; 476..493; 495..508; 516..527; 531..535; 536..538; 621..623; 633..646; 647..649; 652..667; 673..678; 683..685; 689..705; 712..731; 739..754; 758..771; 783..794; 797..809; 813..823; 829..838; 847..849; 850..858; 863..873; 875..882; 887..891; 892..896; 902..914; 919..921; 922..953
Beta Strand
90..92; 97..109; 114..125; 129..135; 138..148; 157..163; 168..177; 181..183; 186..195; 200..210; 213..221; 241..250; 253..259; 261..276; 289..292; 295..300; 306..311; 342..344; 346..353; 355..359; 364..368; 404..408; 512..514; 545..550; 554..559; 581..587; 590..596; 618..620; 625..630
3D Structure
X-ray crystallography (7)

Domain & Motif Annotations

Region
44..83; Disordered
Protein Families
Peptidase M1 family
Sequence Similarities
Belongs to the peptidase M1 family.
Clinical Relevance
Related Diseases
Biomarker
Phase 2
Antibody