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Reviewed, UniProtKB/Swiss-Prot Q10737 (AMPN_HAECO)

Last modified October 13, 2009. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Aminopeptidase N
      Short name=AP-N
    EC=3.4.11.2
Alternative name(s):
    Microsomal aminopeptidase
    Membrane glycoprotein H11
OrganismHaemonchus contortus (Barber pole worm)
Taxonomic identifier6289 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaRhabditidaStrongylidaTrichostrongyloideaHaemonchidaeHaemonchinaeHaemonchus

Protein attributes

Sequence length972 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Catalytic activity

Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Membrane; Single-pass type II membrane protein By similarity.

Sequence similarities

Belongs to the peptidase M1 family.

Ontologies

Keywords
   Cellular componentMembrane
   DomainSignal-anchor
Transmembrane
   LigandMetal-binding
Zinc
   Molecular functionAminopeptidase
Hydrolase
Metalloprotease
Protease
   PTMGlycoprotein
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metallopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 972971Aminopeptidase N
PRO_0000095087

Regions

Topological domain2 – 1716Cytoplasmic Potential
Transmembrane18 – 3922Signal-anchor for type II membrane protein Potential
Topological domain40 – 972933Extracellular Potential

Sites

Active site3801 By similarity
Active site4661Proton donor Potential
Metal binding3791Zinc; catalytic By similarity
Metal binding3831Zinc; catalytic By similarity
Metal binding4021Zinc; catalytic By similarity

Amino acid modifications

Glycosylation991N-linked (GlcNAc...) Potential
Glycosylation2271N-linked (GlcNAc...) Potential
Glycosylation5491N-linked (GlcNAc...) Potential
Glycosylation8581N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q10737-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 5964328CC3C80E43

FASTA972110,674
        10         20         30         40         50         60 
MTSQGRTRTL LNLTPIRLIV ALFLVAAAVG LSIGLTYYFT RKAFDTSEKP GKDDTGGKDK 

        70         80         90        100        110        120 
DNSPSAAELL LPSNIKPLSY DLTIKTYLPG YVDFPPEKNL TFDGRVEISM VVIEPTKSIV 

       130        140        150        160        170        180 
LNSKKISVIP QECELVSGDK KLEIESVKEH PRLEKVEFLI KSQLEKDQQI LLKVGYIGLI 

       190        200        210        220        230        240 
SNSFGGIYQT TYTTPDGTPK IAAVSQNEPI DARRMVPCMD EPKYKANWTV TVIHPKGTKA 

       250        260        270        280        290        300 
VSNGIEVNGD GEISGDWITS KFLTTPRMSS YLLAVMVSEF EYIEGETKTG VRFRIWSRPE 

       310        320        330        340        350        360 
AKKMTQYALQ SGIKCIEFYE DFFDIRFPLK KQDMIALPDF SAGAMENWGL ITYRENSLLY 

       370        380        390        400        410        420 
DDRFYAPMNK QRIARIVAHE LAHQWFGDLV TMKWWDNLWL NEGFARFTEF IGAGQITQDD 

       430        440        450        460        470        480 
ARMRNYFLID VLERALKADS VASSHPLSFR IDKAAEVEEA FDDITYAKGA SVLTMLRALI 

       490        500        510        520        530        540 
GEEKHKHAVS QYLKKFSYSN AEATDLWAVF DEVVTDVEGP DGKPMKTTEF ASQWTTQMGF 

       550        560        570        580        590        600 
PVISVAEFNS TTLKLTQSRY EANKDAVEKE KYRHPKYGFK WDIPLWYQEG DKKEIKRTWL 

       610        620        630        640        650        660 
RRDEPLYLHV SDAGAPFVVN ADRYGFYRQN HDANGWKKII KQLKDNHEVY SPRTRNAIIS 

       670        680        690        700        710        720 
DAFAAAATDA IEYETVFELL NYAEKETEYL PLEIAMSGIS SILKYFGTEP EAKPAQTYMM 

       730        740        750        760        770        780 
NILKPMYEKS SIDFIANNYR NDKLFFQINL QKDVIDMFCA LGSQDCRKKY KKLFDDEVMN 

       790        800        810        820        830        840 
KCRDGQAATE CVRIAAPLRS SVYCYGVKEG GDYASDKVME LYTAETLALE KDFLRLALGC 

       850        860        870        880        890        900 
HKDVTALKGL LLRALDRNSS FVRMQDIPSA FNDVAANPIG GEFIFNFLIE RWPDIIESIG 

       910        920        930        940        950        960 
TKHTYVEKVI PACTSGIRSQ QQIDQLKNLQ KNGMNARQFG AFDKAIERAQ NRVDWIKKHF 

       970 
QKLAAFFKKA TL 

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References

[1]"Cloning and characterization of a microsomal aminopeptidase from the intestine of the nematode Haemonchus contortus."
Smith T.S., Graham M., Munn E.A., Newton S.E., Knox D.P., Coadwell W.J., McMichael-Phillips D., Smith H., Smith W.D., Oliver J.J.
Biochim. Biophys. Acta 1338:295-306(1997) [PubMed: 9128148] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

X94187 mRNA. Translation: CAA63897.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPSM01.015.

Enzyme and pathway databases

BRENDA3.4.11.2. 2482.

Family and domain databases

InterProIPR006025. Pept_M_Zn_BS.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. Peptidase_M1. 1 hit.
PfamPF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMPN_HAECO
AccessionPrimary (citable) accession number: Q10737
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: October 13, 2009
This is version 60 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents