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O43895 (XPP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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

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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length674 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

A metalloprotease that may play a role in the inflammatory process and other reactions produced in response to injury or infection. May also play a role in the metabolism of the vasodilator bradykinin.

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-anchorGPI-anchor.

Tissue specificity

Expressed in kidney, lung, heart, placenta, liver, small intestine and colon. No expression in brain, skeletal muscle, pancreas, spleen, thymus, prostate, testis and ovary.

Post-translational modification

Heavily glycosylated.

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_0000026829
Propeptide650 – 67425Removed in mature form By similarity
PRO_0000026830

Sites

Metal binding4501Manganese 2 By similarity
Metal binding4611Manganese 1 By similarity
Metal binding4611Manganese 2 By similarity
Metal binding5551Manganese 1 By similarity
Metal binding5691Manganese 1 By similarity
Metal binding5691Manganese 2 By similarity

Amino acid modifications

Lipidation6491GPI-anchor amidated alanine By similarity
Glycosylation351N-linked (GlcNAc...) Potential
Glycosylation491N-linked (GlcNAc...) Potential
Glycosylation651N-linked (GlcNAc...) Potential
Glycosylation2781N-linked (GlcNAc...) Potential
Glycosylation2911N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict261V → L in AAB96394. Ref.1
Sequence conflict3391K → R in AAB96394. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O43895 [UniParc].

Last modified November 15, 2002. Version 3.
Checksum: 75949336EDD0F3B4

FASTA67475,625
        10         20         30         40         50         60 
MARAHWGCCP WLVLLCACAW GHTKPVDLGG QDVRNCSTNP PYLPVTVVNT TMSLTALRQQ 

        70         80         90        100        110        120 
MQTQNLSAYI IPGTDAHMNE YIGQHDERRA WITGFTGSAG TAVVTMKKAA VWTDSRYWTQ 

       130        140        150        160        170        180 
AERQMDCNWE LHKEVGTTPI VTWLLTEIPA GGRVGFDPFL LSIDTWESYD LALQGSNRQL 

       190        200        210        220        230        240 
VSITTNLVDL VWGSERPPVP NQPIYALQEA FTGSTWQEKV SGVRSQMQKH QKVPTAVLLS 

       250        260        270        280        290        300 
ALEETAWLFN LRASDIPYNP FFYSYTLLTD SSIRLFANKS RFSSETLSYL NSSCTGPMCV 

       310        320        330        340        350        360 
QIEDYSQVRD SIQAYSLGDV RIWIGTSYTM YGIYEMIPKE KLVTDTYSPV MMTKAVKNSK 

       370        380        390        400        410        420 
EQALLKASHV RDAVAVIRYL VWLEKNVPKG TVDEFSGAEI VDKFRGEEQF SSGPSFETIS 

       430        440        450        460        470        480 
ASGLNAALAH YSPTKELNRK LSSDEMYLLD SGGQYWDGTT DITRTVHWGT PSAFQKEAYT 

       490        500        510        520        530        540 
RVLIGNIDLS RLIFPAATSG RMVEAFARRA LWDAGLNYGH GTGHGIGNFL CVHEWPVGFQ 

       550        560        570        580        590        600 
SNNIAMAKGM FTSIEPGYYK DGEFGIRLED VALVVEAKTK YPGSYLTFEV VSFVPYDRNL 

       610        620        630        640        650        660 
IDVSLLSPEH LQYLNRYYQT IREKVGPELQ RRQLLEEFEW LQQHTEPLAA RAPDTASWAS 

       670 
VLVVSTLAIL GWSV 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and tissue distribution of human membrane-bound aminopeptidase P."
Venema R.C., Ju H., Zou R., Venema V.J., Ryan J.W.
Biochim. Biophys. Acta 1354:45-48(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Kidney and Lung.
[2]Sprinkle T.J.C., Venema R.C., Ju H., Zou R., Venema V.J., Ryan J.W.
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Human membrane-bound aminopeptidase P genomic DNA."
Ryan J.W., Jin L., Horvath I., Sprinkle T.J.C.
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U90724 mRNA. Translation: AAB96394.2.
AF195953 Genomic DNA. Translation: AAG28480.1.
AL023653 Genomic DNA. Translation: CAA19220.1.
BC126174 mRNA. Translation: AAI26175.1.
CCDSCCDS14613.1.
RefSeqNP_003390.4. NM_003399.5.
UniGeneHs.170499.

3D structure databases

ProteinModelPortalO43895.
SMRO43895. Positions 403-582.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-5002270.
STRING9606.ENSP00000360147.

Chemistry

BindingDBO43895.
ChEMBLCHEMBL4610.

Protein family/group databases

MEROPSM24.005.

PTM databases

PhosphoSiteO43895.

Proteomic databases

PaxDbO43895.
PRIDEO43895.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371106; ENSP00000360147; ENSG00000122121.
GeneID7512.
KEGGhsa:7512.
UCSCuc004eut.1. human.

Organism-specific databases

CTD7512.
GeneCardsGC0XP128872.
HGNCHGNC:12823. XPNPEP2.
HPACAB025136.
CAB025269.
HPA000339.
MIM300145. gene.
neXtProtNX_O43895.
Orphanet100057. Renin-angiotensin-aldosterone system-blocker-induced angioedema.
PharmGKBPA37416.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0006.
HOGENOMHOG000255713.
HOVERGENHBG002934.
InParanoidO43895.
KOK14208.
OMAAFTGSTW.
OrthoDBEOG7BGHK4.
PhylomeDBO43895.
TreeFamTF314183.

Gene expression databases

ArrayExpressO43895.
BgeeO43895.
CleanExHS_XPNPEP2.
GenevestigatorO43895.

Family and domain databases

Gene3D3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProIPR029149. Creatin/AminoP/Spt16_NTD.
IPR028980. Creatinase/Aminopeptidase_P_N.
IPR000587. Creatinase_N.
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]
SUPFAMSSF53092. SSF53092. 1 hit.
SSF55920. SSF55920. 1 hit.
PROSITEPS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiXPNPEP2.
GenomeRNAi7512.
NextBio29399.
PROO43895.
SOURCESearch...

Entry information

Entry nameXPP2_HUMAN
AccessionPrimary (citable) accession number: O43895
Secondary accession number(s): A0AV16, O75994
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: July 9, 2014
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM