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P91887

- AMPN_PLUXY

UniProt

P91887 - AMPN_PLUXY

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Protein
Aminopeptidase N
Gene
APN1
Organism
Plutella xylostella (Diamondback moth) (Plutella maculipennis)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein 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

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi344 – 3441Zinc; catalytic By similarity
Active sitei345 – 3451Proton acceptor By similarity
Metal bindingi348 – 3481Zinc; catalytic By similarity
Metal bindingi367 – 3671Zinc; catalytic By similarity
Sitei429 – 4291Transition state stabilizer By 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

MEROPSiM01.030.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminopeptidase N (EC:3.4.11.2)
Short name:
AP-N
Alternative name(s):
Apn1
Microsomal aminopeptidase
Gene namesi
Name:APN1
OrganismiPlutella xylostella (Diamondback moth) (Plutella maculipennis)
Taxonomic identifieri51655 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaYponomeutoideaPlutellidaePlutella

Subcellular locationi

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei? – 946Removed in mature form Reviewed predictionPRO_0000026744
Signal peptidei1 – 1515 Reviewed prediction
Add
BLAST
Chaini16 – ?Aminopeptidase NPRO_0000026743

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi60 – 601N-linked (GlcNAc...) Reviewed prediction
Glycosylationi550 – 5501N-linked (GlcNAc...) Reviewed prediction
Glycosylationi605 – 6051N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi715 ↔ 722 By similarity
Disulfide bondi751 ↔ 787 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Structurei

3D structure databases

ProteinModelPortaliP91887.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni308 – 3125Substrate binding By similarity

Sequence similaritiesi

Belongs to the peptidase M1 family.

Keywords - Domaini

Signal

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.

P91887-1 [UniParc]FASTAAdd to Basket

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MRLLICLTLL GLVCGNPVQL TDNSIALQNT YDNYVLPGES FPTFYDVQLF    50
FDPEYEASFN GTVAIRVVPR IATQEIVLHA MEMEILSIRA YSDLPSDDNL 100
NENLFSSYTL ATDDTHLLKI QFTRVLDALQ PITVEISYSA QYAPNMFGVY 150
VSRYVENGAT VSLVTSQLQP TFARRAFPCY DEPALKAVFR TTIYAPPAYN 200
VVETNMPLRT DSLKSDRPGF TKHEFQDTLV MSSYLLAYLV SKFDYISNEN 250
NPTYDKSMKV FSRPGTQNTA EFALDFGQKN MVELEKYTEF PYAFPKIDKV 300
AVPDFAAGAM ENWGLVIYRE IALLVQEGVT TTSTLQGIGR IISHENTHQW 350
FGNEVGPDSW TYTWLNEGFA NFFESFATDL VLPEWRMMDQ FVINMQNVFQ 400
SDAVLSVNPI TFEVRTPSQI LGTFNSVAYQ KSGSVIRMMQ HFLTPEIFRK 450
SLALYISRMS RKAAKPTDLF EAIQEVVDAS DHSIRWRLSI IMNRWTQQGG 500
FPVVTVRRSA PSAQSFVITQ RRFLTDSTQE SNTVWNVPLN WVLSTDVNFN 550
DTRPMAWLPP QLAAEAVQVP GLQNAEWFIV NKQQTGYYRV NYDPENWRAL 600
AKVLNDTHEI IHLLNRAQLI DDSFNLARNG RLDYSLAFDL SRYLVQERDY 650
IPWAAANAAF NYLNSVLSGS SVHPLFQEYL LFLTAPLYQR LGFNAATGEE 700
HVTPFHRNII LNINCLHGNE DCVSTAETLL QNFRDNPTQT LNPDIQTTVF 750
CSGLRGGDVD NFNFLWARYT ATQDSSEQSI LLNALGCTSN ADRRDFLFSQ 800
VIASDSQVRE QDRHSVLVSA INSGPDNMNA ALDFVLENFA NIQPNVQGLT 850
GTTNILNAFA RTLTTQEHAN KIDEFSNKYA NVFTAGEMAS VAAIKENIAA 900
SITWNSQNAA TVEAWLRKNF GTDGASTVSA SITIIISAMV AIYNIL 946
Length:946
Mass (Da):106,578
Last modified:May 1, 1997 - v1
Checksum:i1DFD81A364067BFB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X97878 mRNA. Translation: CAA66467.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X97878 mRNA. Translation: CAA66467.1 .

3D structure databases

ProteinModelPortali P91887.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M01.030.

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 Manduca sexta and Plutella xylostella midgut aminopeptidase N related to Bacillus thuringiensis toxin-binding proteins."
    Denolf P.H., Hendrickx K., van Damme J., Jansens S., Peferoen M., Degheele D., van Rie J.
    Eur. J. Biochem. 248:748-761(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
    Tissue: Midgut.

Entry informationi

Entry nameiAMPN_PLUXY
AccessioniPrimary (citable) accession number: P91887
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: May 14, 2014
This is version 87 of the entry and version 1 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

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