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Q10737 (AMPN_HAECO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aminopeptidase N

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

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.

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 – 3922Helical; Signal-anchor for type II membrane protein; Potential
Topological domain40 – 972933Extracellular Potential
Region343 – 3475Substrate binding By similarity

Sites

Active site3801Proton acceptor By similarity
Metal binding3791Zinc; catalytic By similarity
Metal binding3831Zinc; catalytic By similarity
Metal binding4021Zinc; catalytic By similarity
Binding site2081Substrate By similarity
Site4661Transition state stabilizer By similarity

Amino acid modifications

Glycosylation991N-linked (GlcNAc...) Potential
Glycosylation2271N-linked (GlcNAc...) Potential
Glycosylation5491N-linked (GlcNAc...) Potential
Glycosylation8581N-linked (GlcNAc...) Potential
Disulfide bond759 ↔ 766 By similarity
Disulfide bond804 ↔ 840 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q10737 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X94187 mRNA. Translation: CAA63897.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM01.015.

Proteomic databases

PRIDEQ10737.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. PTHR11533. 1 hit.
PfamPF11838. ERAP1_C. 1 hit.
PF01433. 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: May 14, 2014
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries