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Protein

Aminopeptidase N

Gene

APN2

Organism
Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm)
Status
Reviewed-Annotation score: 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

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi340Zinc; catalyticPROSITE-ProRule annotation1
Active sitei341Proton acceptorPROSITE-ProRule annotation1
Metal bindingi344Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi363Zinc; catalyticPROSITE-ProRule annotation1
Sitei425Transition 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. 3173.

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

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_0000026742? – 942Removed in mature formSequence analysis
Signal peptidei1 – 15Sequence analysisAdd BLAST15
ChainiPRO_000002674116 – ?Aminopeptidase N

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi62N-linked (GlcNAc...)Sequence analysis1
Glycosylationi121N-linked (GlcNAc...)Sequence analysis1
Glycosylationi544N-linked (GlcNAc...)Sequence analysis1
Glycosylationi601N-linked (GlcNAc...)Sequence analysis1
Glycosylationi678N-linked (GlcNAc...)Sequence analysis1
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)DescriptionActionsGraphical viewLength
Regioni304 – 308Substrate 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.

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:
EMBLi
GenBanki
DDBJi
Links Updated
X97877 mRNA. Translation: CAA66466.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97877 mRNA. Translation: CAA66466.2.

3D structure databases

ProteinModelPortaliP91885.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM01.030.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.11.2. 3173.

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_MANSE
AccessioniPrimary (citable) accession number: P91885
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 30, 2000
Last modified: April 1, 2015
This is version 91 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

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.