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Reviewed, UniProtKB/Swiss-Prot P15541 (AMPN_RABIT)

Last modified October 13, 2009. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Aminopeptidase N
      Short name=AP-N
      Short name=rbAPN
    EC=3.4.11.2
Alternative name(s):
    Alanyl aminopeptidase
    Microsomal aminopeptidase
    Aminopeptidase M
      Short name=AP-M
    CD_antigen=CD13
Gene names
Name: ANPEP
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

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Protein attributes

Sequence length966 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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 and in the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis By similarity.

Catalytic activity

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.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Membrane; Single-pass type II membrane protein.

Post-translational modification

Sulfated By similarity.

Sequence similarities

Belongs to the peptidase M1 family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 966965Aminopeptidase N
PRO_0000095084

Regions

Topological domain2 – 87Cytoplasmic Potential
Transmembrane9 – 3224Signal-anchor for type II membrane protein Potential
Region33 – 6533Cytosolic Ser/Thr-rich junction
Region66 – 966901Metalloprotease

Sites

Active site3851 By similarity
Active site4731Proton donor Potential
Metal binding3841Zinc; catalytic By similarity
Metal binding3881Zinc; catalytic By similarity
Metal binding4071Zinc; catalytic By similarity

Amino acid modifications

Modified residue1731Sulfotyrosine Potential
Modified residue4151Sulfotyrosine Potential
Modified residue4201Sulfotyrosine Potential
Modified residue8521Phosphotyrosine By similarity
Modified residue9121Sulfotyrosine Potential
Modified residue9271Phosphothreonine By similarity
Glycosylation401N-linked (GlcNAc...) Potential
Glycosylation1251N-linked (GlcNAc...) Potential
Glycosylation2591N-linked (GlcNAc...) Potential
Glycosylation3151N-linked (GlcNAc...) Potential
Glycosylation5521N-linked (GlcNAc...) Potential
Glycosylation5701N-linked (GlcNAc...) Potential
Glycosylation6241N-linked (GlcNAc...) Potential
Glycosylation7341N-linked (GlcNAc...) Potential
Glycosylation8171N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict101S → A AA sequence Ref.2
Sequence conflict161I → F AA sequence Ref.2
Sequence conflict2101Q → QMQ Ref.3
Sequence conflict2261M → S in CAA35873. Ref.3
Sequence conflict2341P → L in CAA35873. Ref.3
Sequence conflict593 – 5942LE → QQ in CAA35873. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
P15541-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: ED12832072B0DB52

FASTA966109,318
        10         20         30         40         50         60 
MAKGFYISKS LGILGILLGV AALCTIVALS VVYRQEKNKN TSQSPSMAPL NPTATSSPAT 

        70         80         90        100        110        120 
TLDQNLPWNR YRLPKTLIPD SYNVVLRPYL SPNSQGLYIF TGSSTVRFTC QEATNVIIIH 

       130        140        150        160        170        180 
SKKLNYTITQ GHRVVLRGVR GSQPPAIAST ELVELTEYLV VHLQGQLVAG SQYEMDTQFQ 

       190        200        210        220        230        240 
GELADDLAGF YRSEYMEGNV RKVVATTQMQ AADARKSFPC FDEPAMKATF NITPIHPRDY 

       250        260        270        280        290        300 
TALSNMLPRS STALPEDPNW TVTEFHTTPK MSTYLLAYIV SEFTNIEAQS PNNVQIRIWA 

       310        320        330        340        350        360 
RPSAISEGHG QYALNVTGPI LNFFANHYNT PYPLEKSDQI GLPDFNAGAM ENWGLVTYRE 

       370        380        390        400        410        420 
SALLFDPLVS SISNKERVVT VVAHELAHQW FGNLVTVDWW NDLWLNEGFA SYVEYLGADY 

       430        440        450        460        470        480 
AEPTWNLKDL IVLNELHSVM AVDALASSHP LSSPADEVNT PAQISELFDS ITYSKGASVL 

       490        500        510        520        530        540 
RMLSSFLTED LFKEGLASYL HTFAYQNTIY LDLWEHLQQA VNSQSAIQLP ASVRDIMDRW 

       550        560        570        580        590        600 
ILQMGFPVVT VNTTNGIISQ HHFLLDPTSN VTRPSDFNYL WIVPVSSMRN GVLEQEFWLE 

       610        620        630        640        650        660 
GVEQTQNSLF RVEGDNNWIL ANLNVTGYYQ VNYDEGNWKK LQTQLQTNPS VIPVINRAQI 

       670        680        690        700        710        720 
IHDAFNLASA QKVPVTLALD NTLFLIRETE YMPWQAALSS LNYFKLMFDR SEVYGPMKNY 

       730        740        750        760        770        780 
LSKQVRPLFE HFKNITNDWT RRPDTLMDQY NEINAISTAC SNGIQECETL VSDLFKQWMD 

       790        800        810        820        830        840 
DPSNNPIHPN LRTTVYCNAI ALGGEREWDF AWEQFRNATL VNEADKLRSA LACSNEVWIL 

       850        860        870        880        890        900 
NRYLSYTLNP DYIRRQDATS TINSIASNVI GQTLVWDFVQ SNWKKLFEDF GGGSFSFANL 

       910        920        930        940        950        960 
IRAVTRRFST EYELQQLEQF RLNNLDTGFG SGTRALEQAL EQTRANIKWV QENKEAVLAW 


FTANSA

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References

[1]"Complete sequence of rabbit kidney aminopeptidase N and mRNA localization in rabbit kidney by in situ hybridization."
Yang X.F., Milhiet P.E., Gaudoux F., Crine P., Boileau G.
Biochem. Cell Biol. 71:278-287(1993) [PubMed: 7903857] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney.
[2]"The amino acid sequence of the hydrophobic anchor of rabbit intestinal brush border aminopeptidase N."
Feracci H., Maroux S., Bonicel J., Desnuelle P.
Biochim. Biophys. Acta 684:133-136(1982) [PubMed: 6120002] [Abstract]
Cited for: PROTEIN SEQUENCE OF 6-19.
[3]"Onset of transcription of the aminopeptidase N (leukemia antigen CD 13) gene at the crypt/villus transition zone during rabbit enterocyte differentiation."
Noren O., Dabelsteen E., Hoeyer P.E., Olsen J., Sjoestroem H., Hansen G.H.
FEBS Lett. 259:107-112(1989) [PubMed: 2574692] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 178-966.

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Cross-references

Sequence databases

S68687 mRNA. Translation: AAB29534.1.
X51508 mRNA. Translation: CAA35873.1.
PIRS07099.
RefSeqNP_001075795.1.
UniGeneOcu.2069

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP15541.

Protein family/group databases

MEROPSM01.001.

Genome annotation databases

GeneID100009167.

Organism-specific databases

CTD100009167.

Phylogenomic databases

HOVERGENP15541.

Enzyme and pathway databases

BRENDA3.4.11.2. 255.

Family and domain databases

InterProIPR006025. Pept_M_Zn_BS.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERPTHR11533. Peptidase_M1. 1 hit.
PfamPF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSPR00756. ALADIPTASE.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAMPN_RABIT
AccessionPrimary (citable) accession number: P15541
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: October 13, 2009
This is version 87 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents