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UniProtKB/Swiss-Prot entry O43895


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name XPP2_HUMAN
Primary accession number O43895
Secondary accession numbers A0AV16 O75994
Integrated into Swiss-Prot on November 15, 2002
Sequence was last modified on November 15, 2002 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 73)
Name and origin of the protein
Protein name Xaa-Pro aminopeptidase 2 [Precursor]
Synonyms EC 3.4.11.9
X-Pro aminopeptidase 2
Membrane-bound aminopeptidase P
Membrane-bound APP
Membrane-bound AmP
mAmP
Aminoacylproline aminopeptidase
Gene name
Name: XPNPEP2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney, and Lung;
DOI=10.1016/S0167-4781(97)00126-7; PubMed=9375790 [NCBI, ExPASy, EBI, Israel, Japan]
Venema R.C., Ju H., Zou R., Venema V.J., Ryan J.W.;
"Cloning and tissue distribution of human membrane-bound aminopeptidase P.";
Biochim. Biophys. Acta 1354:45-48(1997).
[2]
SEQUENCE REVISION.
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.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Ryan J.W., Jin L., Horvath I., Sprinkle T.J.C.;
"Human membrane-bound aminopeptidase P genomic DNA.";
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03440; PubMed=15772651 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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: Homotrimer.
  • SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-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.
  • PTM: Heavily glycosylated.
  • SIMILARITY: Belongs to the peptidase M24B family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U90724; AAB96394.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF195953; AAG28480.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL023653; CAA19220.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC126174; AAI26175.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00439344; -.
RefSeq NP_003390.4; -.
UniGene Hs.170499
3D structure databases
ModBase O43895.
Protein family/group databases
MEROPS M24.005; -.
PTM databases
PhosphoSite O43895; -.
Enzyme and pathway databases
BRENDA 3.4.11.9; 247.
Organism-specific databases
GeneCards GC0XP128700; -.
HGNC HGNC:12823; XPNPEP2.
GenAtlas XPNPEP2.
MIM 300145; gene. [NCBI / EBI]
PharmGKB PA37416; -.
Gene expression databases
ArrayExpress O43895; -.
Bgee O43895; -.
CleanEx HS_XPNPEP2; -.
GermOnline ENSG00000122121; Homo sapiens.
Ontologies
GO
GO:0031225; Cellular component: anchored to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004177; Molecular function: aminopeptidase activity (traceable author statement from ProtInc).
GO:0030145; Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008235; Molecular function: metalloexopeptidase activity (inferred from electronic annotation from InterPro).
GO:0009987; Biological process: cellular process (inferred from electronic annotation from InterPro).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR000587; Creatinase.
IPR000994; Pept_M24_structural-domain.
IPR001131; Peptidase_M24B_aminopep-P_CS.
Graphical view of domain structure.
Gene3D G3DSA:3.90.230.10; Peptidase_M24_cat_core; 1.
PANTHER PTHR10804; Peptidase_M24_cat_core; 1.
Pfam PF01321; Creatinase_N; 1.
PF00557; Peptidase_M24; 1.
Pfam graphical view of domain structure.
PROSITE PS00491; PROLINE_PEPTIDASE; 1.
Proteomic databases
PRIDE O43895; -.
Genome annotation databases
Ensembl ENSG00000122121; Homo sapiens. [Contig view]
GeneID 7512; -.
KEGG hsa:7512; -.
Phylogenomic databases
HOGENOM O43895; -.
HOVERGEN O43895; -.
OMA O43895; GSTWQEK.
Other
NextBio 29399; -.
SOURCE XPNPEP2; Homo sapiens.
ProtoNet O43895.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Aminopeptidase; Cell membrane; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Manganese; Membrane; Metal-binding; Metalloprotease; Protease; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    21  21     Potential. 
CHAIN   22   649  628     Xaa-Pro aminopeptidase 2. PRO_0000026829
PROPEP   650   674  25     Removed in mature form (By similarity). PRO_0000026830
METAL   450   450        Manganese 2 (By similarity). 
METAL   461   461        Manganese 1 (By similarity). 
METAL   461   461        Manganese 2 (By similarity). 
METAL   555   555        Manganese 1 (By similarity). 
METAL   569   569        Manganese 1 (By similarity). 
METAL   569   569        Manganese 2 (By similarity). 
LIPID   649   649        GPI-anchor amidated alanine (By similarity). 
CARBOHYD   35    35        N-linked (GlcNAc...) (Potential). 
CARBOHYD   49    49        N-linked (GlcNAc...) (Potential). 
CARBOHYD   65    65        N-linked (GlcNAc...) (Potential). 
CARBOHYD   278   278        N-linked (GlcNAc...) (Potential). 
CARBOHYD   291   291        N-linked (GlcNAc...) (Potential). 
CONFLICT   26    26        V -> L (in Ref. 1; AAB96394). 
CONFLICT   339   339        K -> R (in Ref. 1; AAB96394). 
Sequence information
Length: 674 AA [This is the length of the unprocessed precursor] Molecular weight: 75625 Da [This is the MW of the unprocessed precursor] CRC64: 75949336EDD0F3B4 [This is a checksum on the sequence]
        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 

O43895 in FASTA format

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