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Protein

Aminopeptidase N

Gene

APN1

Organism
Plutella xylostella (Diamondback moth) (Plutella maculipennis)
Status
Reviewed-Annotation score: 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

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi344 – 3441Zinc; catalyticPROSITE-ProRule annotation
Active sitei345 – 3451Proton acceptorPROSITE-ProRule annotation
Metal bindingi348 – 3481Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi367 – 3671Zinc; catalyticPROSITE-ProRule annotation
Sitei429 – 4291Transition state stabilizerBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.11.2. 4920.

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

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei? – 946Removed in mature formSequence AnalysisPRO_0000026744
Signal peptidei1 – 1515Sequence AnalysisAdd
BLAST
Chaini16 – ?Aminopeptidase NPRO_0000026743

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Structurei

3D structure databases

ProteinModelPortaliP91887.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

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

« Hide

        10         20         30         40         50
MRLLICLTLL GLVCGNPVQL TDNSIALQNT YDNYVLPGES FPTFYDVQLF
60 70 80 90 100
FDPEYEASFN GTVAIRVVPR IATQEIVLHA MEMEILSIRA YSDLPSDDNL
110 120 130 140 150
NENLFSSYTL ATDDTHLLKI QFTRVLDALQ PITVEISYSA QYAPNMFGVY
160 170 180 190 200
VSRYVENGAT VSLVTSQLQP TFARRAFPCY DEPALKAVFR TTIYAPPAYN
210 220 230 240 250
VVETNMPLRT DSLKSDRPGF TKHEFQDTLV MSSYLLAYLV SKFDYISNEN
260 270 280 290 300
NPTYDKSMKV FSRPGTQNTA EFALDFGQKN MVELEKYTEF PYAFPKIDKV
310 320 330 340 350
AVPDFAAGAM ENWGLVIYRE IALLVQEGVT TTSTLQGIGR IISHENTHQW
360 370 380 390 400
FGNEVGPDSW TYTWLNEGFA NFFESFATDL VLPEWRMMDQ FVINMQNVFQ
410 420 430 440 450
SDAVLSVNPI TFEVRTPSQI LGTFNSVAYQ KSGSVIRMMQ HFLTPEIFRK
460 470 480 490 500
SLALYISRMS RKAAKPTDLF EAIQEVVDAS DHSIRWRLSI IMNRWTQQGG
510 520 530 540 550
FPVVTVRRSA PSAQSFVITQ RRFLTDSTQE SNTVWNVPLN WVLSTDVNFN
560 570 580 590 600
DTRPMAWLPP QLAAEAVQVP GLQNAEWFIV NKQQTGYYRV NYDPENWRAL
610 620 630 640 650
AKVLNDTHEI IHLLNRAQLI DDSFNLARNG RLDYSLAFDL SRYLVQERDY
660 670 680 690 700
IPWAAANAAF NYLNSVLSGS SVHPLFQEYL LFLTAPLYQR LGFNAATGEE
710 720 730 740 750
HVTPFHRNII LNINCLHGNE DCVSTAETLL QNFRDNPTQT LNPDIQTTVF
760 770 780 790 800
CSGLRGGDVD NFNFLWARYT ATQDSSEQSI LLNALGCTSN ADRRDFLFSQ
810 820 830 840 850
VIASDSQVRE QDRHSVLVSA INSGPDNMNA ALDFVLENFA NIQPNVQGLT
860 870 880 890 900
GTTNILNAFA RTLTTQEHAN KIDEFSNKYA NVFTAGEMAS VAAIKENIAA
910 920 930 940
SITWNSQNAA TVEAWLRKNF GTDGASTVSA SITIIISAMV AIYNIL
Length:946
Mass (Da):106,578
Last modified:May 1, 1997 - v1
Checksum:i1DFD81A364067BFB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97878 mRNA. Translation: CAA66467.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97878 mRNA. Translation: CAA66467.1.

3D structure databases

ProteinModelPortaliP91887.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM01.030.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.11.2. 4920.

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]
ProtoNetiSearch...

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: April 1, 2015
This is version 92 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.