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Protein

Aminopeptidase N

Gene

ANPEP

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines and involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis (By similarity).By similarity

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 bindingi384Zinc; catalyticPROSITE-ProRule annotation1
Active sitei385Proton acceptorPROSITE-ProRule annotation1
Metal bindingi388Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi407Zinc; catalyticPROSITE-ProRule annotation1
Sitei473Transition state stabilizerBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Developmental protein, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Angiogenesis, Differentiation

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM01.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Aminopeptidase N (EC:3.4.11.2)
Short name:
AP-N
Short name:
rbAPN
Alternative name(s):
Alanyl aminopeptidase
Aminopeptidase M
Short name:
AP-M
Microsomal aminopeptidase
CD_antigen: CD13
Gene namesi
Name:ANPEP
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 8CytoplasmicBy similarity7
Transmembranei9 – 32Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST24
Topological domaini33 – 966ExtracellularBy similarityAdd BLAST934

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000950842 – 966Aminopeptidase NAdd BLAST965

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi40N-linked (GlcNAc...)Sequence analysis1
Glycosylationi125N-linked (GlcNAc...)Sequence analysis1
Modified residuei173SulfotyrosineSequence analysis1
Glycosylationi259N-linked (GlcNAc...)Sequence analysis1
Glycosylationi315N-linked (GlcNAc...)Sequence analysis1
Modified residuei415SulfotyrosineSequence analysis1
Modified residuei420SulfotyrosineSequence analysis1
Glycosylationi552N-linked (GlcNAc...)Sequence analysis1
Glycosylationi570N-linked (GlcNAc...)Sequence analysis1
Glycosylationi624N-linked (GlcNAc...)Sequence analysis1
Glycosylationi734N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi760 ↔ 767By similarity
Disulfide bondi797 ↔ 833By similarity
Glycosylationi817N-linked (GlcNAc...)Sequence analysis1
Modified residuei852PhosphotyrosineBy similarity1
Modified residuei912SulfotyrosineSequence analysis1

Post-translational modificationi

Sulfated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

Proteomic databases

PRIDEiP15541.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000015166.

Structurei

3D structure databases

ProteinModelPortaliP15541.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 65Cytosolic Ser/Thr-rich junctionAdd BLAST33
Regioni66 – 966MetalloproteaseAdd BLAST901
Regioni348 – 352Substrate bindingBy similarity5

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
HOGENOMiHOG000106482.
HOVERGENiHBG006616.
InParanoidiP15541.
KOiK11140.

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.

P15541-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKGFYISKS LGILGILLGV AALCTIVALS VVYRQEKNKN TSQSPSMAPL
60 70 80 90 100
NPTATSSPAT TLDQNLPWNR YRLPKTLIPD SYNVVLRPYL SPNSQGLYIF
110 120 130 140 150
TGSSTVRFTC QEATNVIIIH SKKLNYTITQ GHRVVLRGVR GSQPPAIAST
160 170 180 190 200
ELVELTEYLV VHLQGQLVAG SQYEMDTQFQ GELADDLAGF YRSEYMEGNV
210 220 230 240 250
RKVVATTQMQ AADARKSFPC FDEPAMKATF NITPIHPRDY TALSNMLPRS
260 270 280 290 300
STALPEDPNW TVTEFHTTPK MSTYLLAYIV SEFTNIEAQS PNNVQIRIWA
310 320 330 340 350
RPSAISEGHG QYALNVTGPI LNFFANHYNT PYPLEKSDQI GLPDFNAGAM
360 370 380 390 400
ENWGLVTYRE SALLFDPLVS SISNKERVVT VVAHELAHQW FGNLVTVDWW
410 420 430 440 450
NDLWLNEGFA SYVEYLGADY AEPTWNLKDL IVLNELHSVM AVDALASSHP
460 470 480 490 500
LSSPADEVNT PAQISELFDS ITYSKGASVL RMLSSFLTED LFKEGLASYL
510 520 530 540 550
HTFAYQNTIY LDLWEHLQQA VNSQSAIQLP ASVRDIMDRW ILQMGFPVVT
560 570 580 590 600
VNTTNGIISQ HHFLLDPTSN VTRPSDFNYL WIVPVSSMRN GVLEQEFWLE
610 620 630 640 650
GVEQTQNSLF RVEGDNNWIL ANLNVTGYYQ VNYDEGNWKK LQTQLQTNPS
660 670 680 690 700
VIPVINRAQI IHDAFNLASA QKVPVTLALD NTLFLIRETE YMPWQAALSS
710 720 730 740 750
LNYFKLMFDR SEVYGPMKNY LSKQVRPLFE HFKNITNDWT RRPDTLMDQY
760 770 780 790 800
NEINAISTAC SNGIQECETL VSDLFKQWMD DPSNNPIHPN LRTTVYCNAI
810 820 830 840 850
ALGGEREWDF AWEQFRNATL VNEADKLRSA LACSNEVWIL NRYLSYTLNP
860 870 880 890 900
DYIRRQDATS TINSIASNVI GQTLVWDFVQ SNWKKLFEDF GGGSFSFANL
910 920 930 940 950
IRAVTRRFST EYELQQLEQF RLNNLDTGFG SGTRALEQAL EQTRANIKWV
960
QENKEAVLAW FTANSA
Length:966
Mass (Da):109,318
Last modified:January 23, 2007 - v4
Checksum:iED12832072B0DB52
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti10S → A AA sequence (PubMed:6120002).Curated1
Sequence conflicti16I → F AA sequence (PubMed:6120002).Curated1
Sequence conflicti210Q → QMQ (PubMed:2574692).Curated1
Sequence conflicti226M → S in CAA35873 (PubMed:2574692).Curated1
Sequence conflicti234P → L in CAA35873 (PubMed:2574692).Curated1
Sequence conflicti593 – 594LE → QQ in CAA35873 (PubMed:2574692).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S68687 mRNA. Translation: AAB29534.1.
X51508 mRNA. Translation: CAA35873.1.
PIRiS07099.
RefSeqiNP_001075795.1. NM_001082326.1.
UniGeneiOcu.2069.

Genome annotation databases

GeneIDi100009167.
KEGGiocu:100009167.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S68687 mRNA. Translation: AAB29534.1.
X51508 mRNA. Translation: CAA35873.1.
PIRiS07099.
RefSeqiNP_001075795.1. NM_001082326.1.
UniGeneiOcu.2069.

3D structure databases

ProteinModelPortaliP15541.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000015166.

Protein family/group databases

MEROPSiM01.001.

Proteomic databases

PRIDEiP15541.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009167.
KEGGiocu:100009167.

Organism-specific databases

CTDi290.

Phylogenomic databases

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
HOGENOMiHOG000106482.
HOVERGENiHBG006616.
InParanoidiP15541.
KOiK11140.

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_RABIT
AccessioniPrimary (citable) accession number: P15541
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: October 5, 2016
This is version 130 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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.