Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q95333 (XPP2_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Xaa-Pro aminopeptidase 2
EC=3.4.11.9
Alternative name(s):
Aminoacylproline aminopeptidase
Membrane-bound aminopeptidase P
Short name=Membrane-bound APP
Short name=Membrane-bound AmP
Short name=mAmP
X-Pro aminopeptidase 2
Gene names
Name:XPNPEP2
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length673 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Is a key enzyme in the metabolism of the vasodilator bradykinin. In addition to bradykinin, AP-P also cleaves substance P and peptides of the pancreatic polypeptide family.

Catalytic activity

Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.

Cofactor

Binds 2 manganese ions per subunit By similarity.

Subunit structure

Homotrimer.

Subcellular location

Cell membrane; Lipid-anchor › GPI-anchor.

Tissue specificity

In the kidney microvillar membrane fractions.

Sequence similarities

Belongs to the peptidase M24B family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 649628Xaa-Pro aminopeptidase 2
PRO_0000026831
Propeptide650 – 67324Removed in mature form
PRO_0000026832

Sites

Metal binding4491Manganese 2 By similarity
Metal binding4601Manganese 1 By similarity
Metal binding4601Manganese 2 By similarity
Metal binding5541Manganese 1 By similarity
Metal binding5681Manganese 1 By similarity
Metal binding5681Manganese 2 By similarity

Amino acid modifications

Lipidation6491GPI-anchor amidated alanine
Glycosylation341N-linked (GlcNAc...) Ref.2
Glycosylation481N-linked (GlcNAc...) Ref.2
Glycosylation641N-linked (GlcNAc...) Ref.2
Glycosylation2771N-linked (GlcNAc...) Ref.2
Glycosylation2901N-linked (GlcNAc...) Ref.2
Glycosylation2941N-linked (GlcNAc...) Ref.2

Experimental info

Sequence conflict5301C → G AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q95333 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: F480F50537CFD1B2

FASTA67375,756
        10         20         30         40         50         60 
MAQACWGCYP WLVLICACAW GHPKSLNQRE DVRNCSTSPP YLPVTAVNTT AQLTALREQM 

        70         80         90        100        110        120 
LTQNLSAYII PDTDAHMSEY IGECDQRRAW ITGFIGSAGI AVVTERKAAL WTDSRYWTQA 

       130        140        150        160        170        180 
ERQMDCNWEL HKEVSTGHIV TWLLTEIPVG GRVGFDPFLF SIDSWESYDV ALQDADRELV 

       190        200        210        220        230        240 
SITVNLVDLV WGSERPPLPN APIYALQEAF AGSTWQEKVS NIRSQMQKHH ERPTAVLLSA 

       250        260        270        280        290        300 
LDETAWLFNL RSSDIPYNPF FYSYTLLTDS SIRLFANKSR FSSETLQYLN SSCNSSMCVQ 

       310        320        330        340        350        360 
LEDYSQIRDS IQAYTSGDVK IWIGTRYTSY GLYEVIPKEK LVEDDYSPVM ITKAVKNSRE 

       370        380        390        400        410        420 
QALLKASHVR DAVAVIRYLA WLEKNVPTGT VDEFSGAKRV EEFRGEEEFF SGPSFETISA 

       430        440        450        460        470        480 
SGLNAALAHY SPTKELHRKL SSDEMYLLDS GGQYWDGTTD ITRTVHWGTP SAFQKEAYTR 

       490        500        510        520        530        540 
VLIGNIDLSR LVFPAATSGR VVEAFARKAL WDVGLNYGHG TGHGIGNFLC VHEWPVGFQY 

       550        560        570        580        590        600 
GNIPMAEGMF TSIEPGYYQD GEFGIRLEDV ALVVEAKTKY PGTYLTFEVV SLVPYDRKLI 

       610        620        630        640        650        660 
DVSLLSPEQL QYLNRYYQAI REKVGPELQR RGLLEELSWL QRHTEPLSAR AAPTTSLGSL 

       670 
MTVSALAILG WSV

« Hide

References

[1]"Molecular cloning and expression in COS-1 cells of pig kidney aminopeptidase P."
Hyde R.J., Hooper N.M., Turner A.J.
Biochem. J. 319:197-201(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney cortex.
[2]"Purification and amino acid sequence of aminopeptidase P from pig kidney."
Vergas Romero C., Neudorfer I., Mann K., Schaefer W.
Eur. J. Biochem. 229:262-269(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-649, GLYCOSYLATION AT ASN-34; ASN-48; ASN-64; ASN-277; ASN-290 AND ASN-294, CHARACTERIZATION.
Tissue: Kidney cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U55039 mRNA. Translation: AAC48664.1.
PIRS72440.
RefSeqNP_001004048.1. NM_001004048.1.
UniGeneSsc.16106.

3D structure databases

ProteinModelPortalQ95333.
ModBaseSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000013450.

Protein family/group databases

MEROPSM24.005.

Proteomic databases

PaxDbQ95333.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000013832; ENSSSCP00000013450; ENSSSCG00000012651.
GeneID445538.
KEGGssc:445538.

Organism-specific databases

CTD7512.

Phylogenomic databases

eggNOGCOG0006.
GeneTreeENSGT00390000013970.
HOGENOMHOG000255713.
HOVERGENHBG002934.
KOK14208.
OMALPKAQKN.
OrthoDBEOG4CZBFH.

Family and domain databases

Gene3D3.90.230.10. 1 hit.
InterProIPR000587. Creatinase.
IPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
[Graphical view]
PfamPF01321. Creatinase_N. 1 hit.
PF00557. Peptidase_M24. 1 hit.
[Graphical view]
SUPFAMSSF55920. Peptidase_M24_cat_core. 1 hit.
PROSITEPS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXPP2_PIG
AccessionPrimary (citable) accession number: Q95333
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: February 1, 1997
Last modified: April 3, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents