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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)DescriptionActionsGraphical viewLength
Metal bindingi344Zinc; catalyticPROSITE-ProRule annotation1
Active sitei345Proton acceptorPROSITE-ProRule annotation1
Metal bindingi348Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi367Zinc; catalyticPROSITE-ProRule annotation1
Sitei429Transition state stabilizerBy similarity1

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)DescriptionActionsGraphical viewLength
PropeptideiPRO_0000026744? – 946Removed in mature formSequence analysis
Signal peptidei1 – 15Sequence analysisAdd BLAST15
ChainiPRO_000002674316 – ?Aminopeptidase N

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi60N-linked (GlcNAc...)Sequence analysis1
Glycosylationi550N-linked (GlcNAc...)Sequence analysis1
Glycosylationi605N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi715 ↔ 722By similarity
Disulfide bondi751 ↔ 787By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PRIDEiP91887.

Structurei

3D structure databases

ProteinModelPortaliP91887.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni308 – 312Substrate bindingBy similarity5

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.

Proteomic databases

PRIDEiP91887.

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...

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: October 5, 2016
This is version 93 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

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 one 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.