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P91885

- AMPN_MANSE

UniProt

P91885 - AMPN_MANSE

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Protein

Aminopeptidase N

Gene

APN2

Organism
Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Status
Reviewed - Annotation score: 4 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 bindingi340 – 3401Zinc; catalyticPROSITE-ProRule annotation
Active sitei341 – 3411Proton acceptorPROSITE-ProRule annotation
Metal bindingi344 – 3441Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi363 – 3631Zinc; catalyticPROSITE-ProRule annotation
Sitei425 – 4251Transition 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

MEROPSiM01.030.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminopeptidase N (EC:3.4.11.2)
Short name:
AP-N
Alternative name(s):
Apn2
Microsomal aminopeptidase
Gene namesi
Name:APN2
OrganismiManduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Taxonomic identifieri7130 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaSphingidaeSphinginaeSphinginiManduca

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei? – 942Removed in mature formSequence AnalysisPRO_0000026742
Signal peptidei1 – 1515Sequence AnalysisAdd
BLAST
Chaini16 – ?Aminopeptidase NPRO_0000026741

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi62 – 621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi544 – 5441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi601 – 6011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi678 – 6781N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi711 ↔ 718By similarity
Disulfide bondi747 ↔ 783By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Interactioni

Subunit structurei

Binds to CRY1AB5.

Structurei

3D structure databases

ProteinModelPortaliP91885.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni304 – 3085Substrate 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.

P91885-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MYSLIFLALI GAAFGVPLST NEDSTRNQNL AALYVLPQTS YPTFYDVRLF
60 70 80 90 100
IDPGYTEAFH GNVSIRIIPN INIDQITIHA MAMRIDSIRV VSDVNPNEDL
110 120 130 140 150
FSDFTLATDD THLLTIRLTR NITALQPHVI HIDYVAQYAD DMFGVYVSTY
160 170 180 190 200
EENGRTVNLV TSQLQPTFAR RAFPCYDEPA LKAVFRTTIY APAAYATVRS
210 220 230 240 250
NTPERRDSLK PNEPGYVKHE FEDTLVMSTY LIAYLVSNFN YIENSQNPIY
260 270 280 290 300
PIPFRVYSRP GTQNTAEFAL EFGQQNMIAL EEYTEFPYAF PKIDKAAVPD
310 320 330 340 350
FAAGAMENWG LVIYREVALL VREGVTTTSV KQNIGRIICH ENTHMWFGNE
360 370 380 390 400
VGPMSWTYTW LNEGFANFFE NYATDFVRPQ WRMMDQFVIA MQNVFQSDAV
410 420 430 440 450
LSVNPMTHPV YTPSQIIGTF NAVAYQKSGS VIRMLQHFMT PEIFRRGLVI
460 470 480 490 500
YIKANSRAAA APSDLYVALQ QALDESSHRI PKPISTIMTE WSTQGGFPVL
510 520 530 540 550
TVRRTAPNAD SVFVAQERYL TDRSLTSTDR WHVPVNWVIS SNVNFSDTSP
560 570 580 590 600
QAWILPTFPA TAVDVPGLSN ADWYIFNKQQ TGYYRVNYDV ENWVALARVL
610 620 630 640 650
NNSHEIIHVL NRAQIVDDAF NLARNGRLHY KNAFEISRYL EMEKDYIPWA
660 670 680 690 700
AANPAFNYLD IVLSGANSYN LYRYYLLNLT APMFEDLGFD VKSGEEFVTP
710 720 730 740 750
YHRNIILDIN CRFGNQRCIS RAQEILQAFK NNPNQRPNPD IQTLVYCSSL
760 770 780 790 800
RAGNVENFNF LWNMYLGTSD SSEQSILLSA LGCTSNAERR NFYLNQIIDD
810 820 830 840 850
NSAVREQDRH SIAVSVINSS PEGMNVALDF VVENFHRIQP RVQALTGTTN
860 870 880 890 900
ILNTFARRLT TSAHNEKIDE LVRRHESIFS AGERASIAAI RENIAASIAW
910 920 930 940
SNSNAGIVEN WLKENYGPPS GAKSLTAGLL VLISLFVAIF NH
Length:942
Mass (Da):106,780
Last modified:May 30, 2000 - v2
Checksum:iEFD4D906600E17B9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X97877 mRNA. Translation: CAA66466.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X97877 mRNA. Translation: CAA66466.2 .

3D structure databases

ProteinModelPortali P91885.
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], PROTEIN SEQUENCE OF 68-72; 187-199; 460-475; 602-612; 693-703; 875-884 AND 893-908, CHARACTERIZATION.
    Tissue: Midgut.
  2. Denolf P.H.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.

Entry informationi

Entry nameiAMPN_MANSE
AccessioniPrimary (citable) accession number: P91885
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 30, 2000
Last modified: October 29, 2014
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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