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Q10737

- AMPN_HAECO

UniProt

Q10737 - AMPN_HAECO

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Protein

Aminopeptidase N

Gene
N/A
Organism
Haemonchus contortus (Barber pole worm)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei208 – 2081SubstrateBy similarity
Metal bindingi379 – 3791Zinc; catalyticPROSITE-ProRule annotation
Active sitei380 – 3801Proton acceptorPROSITE-ProRule annotation
Metal bindingi383 – 3831Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi402 – 4021Zinc; catalyticPROSITE-ProRule annotation
Sitei466 – 4661Transition state stabilizerBy similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-KW
  2. metallopeptidase activity Source: UniProtKB-KW
  3. zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM01.015.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminopeptidase N (EC:3.4.11.2)
Short name:
AP-N
Alternative name(s):
Membrane glycoprotein H11
Microsomal aminopeptidase
OrganismiHaemonchus contortus (Barber pole worm)
Taxonomic identifieri6289 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaStrongylidaTrichostrongyloideaHaemonchidaeHaemonchinaeHaemonchus

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 1716CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei18 – 3922Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini40 – 972933ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 972971Aminopeptidase NPRO_0000095087Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis
Glycosylationi227 – 2271N-linked (GlcNAc...)Sequence Analysis
Glycosylationi549 – 5491N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi759 ↔ 766By similarity
Disulfide bondi804 ↔ 840By similarity
Glycosylationi858 – 8581N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ10737.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni343 – 3475Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 1 hit.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q10737-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTSQGRTRTL LNLTPIRLIV ALFLVAAAVG LSIGLTYYFT RKAFDTSEKP
60 70 80 90 100
GKDDTGGKDK DNSPSAAELL LPSNIKPLSY DLTIKTYLPG YVDFPPEKNL
110 120 130 140 150
TFDGRVEISM VVIEPTKSIV LNSKKISVIP QECELVSGDK KLEIESVKEH
160 170 180 190 200
PRLEKVEFLI KSQLEKDQQI LLKVGYIGLI SNSFGGIYQT TYTTPDGTPK
210 220 230 240 250
IAAVSQNEPI DARRMVPCMD EPKYKANWTV TVIHPKGTKA VSNGIEVNGD
260 270 280 290 300
GEISGDWITS KFLTTPRMSS YLLAVMVSEF EYIEGETKTG VRFRIWSRPE
310 320 330 340 350
AKKMTQYALQ SGIKCIEFYE DFFDIRFPLK KQDMIALPDF SAGAMENWGL
360 370 380 390 400
ITYRENSLLY DDRFYAPMNK QRIARIVAHE LAHQWFGDLV TMKWWDNLWL
410 420 430 440 450
NEGFARFTEF IGAGQITQDD ARMRNYFLID VLERALKADS VASSHPLSFR
460 470 480 490 500
IDKAAEVEEA FDDITYAKGA SVLTMLRALI GEEKHKHAVS QYLKKFSYSN
510 520 530 540 550
AEATDLWAVF DEVVTDVEGP DGKPMKTTEF ASQWTTQMGF PVISVAEFNS
560 570 580 590 600
TTLKLTQSRY EANKDAVEKE KYRHPKYGFK WDIPLWYQEG DKKEIKRTWL
610 620 630 640 650
RRDEPLYLHV SDAGAPFVVN ADRYGFYRQN HDANGWKKII KQLKDNHEVY
660 670 680 690 700
SPRTRNAIIS DAFAAAATDA IEYETVFELL NYAEKETEYL PLEIAMSGIS
710 720 730 740 750
SILKYFGTEP EAKPAQTYMM NILKPMYEKS SIDFIANNYR NDKLFFQINL
760 770 780 790 800
QKDVIDMFCA LGSQDCRKKY KKLFDDEVMN KCRDGQAATE CVRIAAPLRS
810 820 830 840 850
SVYCYGVKEG GDYASDKVME LYTAETLALE KDFLRLALGC HKDVTALKGL
860 870 880 890 900
LLRALDRNSS FVRMQDIPSA FNDVAANPIG GEFIFNFLIE RWPDIIESIG
910 920 930 940 950
TKHTYVEKVI PACTSGIRSQ QQIDQLKNLQ KNGMNARQFG AFDKAIERAQ
960 970
NRVDWIKKHF QKLAAFFKKA TL
Length:972
Mass (Da):110,674
Last modified:January 23, 2007 - v2
Checksum:i5964328CC3C80E43
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94187 mRNA. Translation: CAA63897.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94187 mRNA. Translation: CAA63897.1 .

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M01.015.

Proteomic databases

PRIDEi Q10737.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view ]
PANTHERi PTHR11533. PTHR11533. 1 hit.
Pfami PF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view ]
PRINTSi PR00756. ALADIPTASE.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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].

Entry informationi

Entry nameiAMPN_HAECO
AccessioniPrimary (citable) accession number: Q10737
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3