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O43895

- XPP2_HUMAN

UniProt

O43895 - XPP2_HUMAN

Protein

Xaa-Pro aminopeptidase 2

Gene

XPNPEP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 3 (15 Nov 2002)
      Previous versions | rss
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    Functioni

    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 activityi

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

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi450 – 4501Manganese 2By similarity
    Metal bindingi461 – 4611Manganese 1By similarity
    Metal bindingi461 – 4611Manganese 2By similarity
    Metal bindingi555 – 5551Manganese 1By similarity
    Metal bindingi569 – 5691Manganese 1By similarity
    Metal bindingi569 – 5691Manganese 2By similarity

    GO - Molecular functioni

    1. aminopeptidase activity Source: ProtInc
    2. metal ion binding Source: UniProtKB-KW
    3. metallopeptidase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Manganese, Metal-binding

    Protein family/group databases

    MEROPSiM24.005.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:XPNPEP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:12823. XPNPEP2.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. extracellular vesicular exosome Source: UniProtKB
    3. membrane Source: ProtInc
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti100057. Renin-angiotensin-aldosterone system-blocker-induced angioedema.
    PharmGKBiPA37416.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 649628Xaa-Pro aminopeptidase 2PRO_0000026829Add
    BLAST
    Propeptidei650 – 67425Removed in mature formBy similarityPRO_0000026830Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi35 – 351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi49 – 491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi65 – 651N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi278 – 2781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi291 – 2911N-linked (GlcNAc...)Sequence Analysis
    Lipidationi649 – 6491GPI-anchor amidated alanineBy similarity

    Post-translational modificationi

    Heavily glycosylated.

    Keywords - PTMi

    Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    PaxDbiO43895.
    PRIDEiO43895.

    PTM databases

    PhosphoSiteiO43895.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiO43895.
    BgeeiO43895.
    CleanExiHS_XPNPEP2.
    GenevestigatoriO43895.

    Organism-specific databases

    HPAiCAB025136.
    CAB025269.
    HPA000339.

    Interactioni

    Subunit structurei

    Homotrimer.

    Protein-protein interaction databases

    MINTiMINT-5002270.
    STRINGi9606.ENSP00000360147.

    Structurei

    3D structure databases

    ProteinModelPortaliO43895.
    SMRiO43895. Positions 403-582.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M24B family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0006.
    HOGENOMiHOG000255713.
    HOVERGENiHBG002934.
    InParanoidiO43895.
    KOiK14208.
    OMAiAFTGSTW.
    OrthoDBiEOG7BGHK4.
    PhylomeDBiO43895.
    TreeFamiTF314183.

    Family and domain databases

    Gene3Di3.40.350.10. 1 hit.
    3.90.230.10. 1 hit.
    InterProiIPR029149. 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]
    PfamiPF01321. Creatinase_N. 1 hit.
    PF00557. Peptidase_M24. 1 hit.
    [Graphical view]
    SUPFAMiSSF53092. SSF53092. 1 hit.
    SSF55920. SSF55920. 1 hit.
    PROSITEiPS00491. PROLINE_PEPTIDASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O43895-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARAHWGCCP WLVLLCACAW GHTKPVDLGG QDVRNCSTNP PYLPVTVVNT    50
    TMSLTALRQQ MQTQNLSAYI IPGTDAHMNE YIGQHDERRA WITGFTGSAG 100
    TAVVTMKKAA VWTDSRYWTQ AERQMDCNWE LHKEVGTTPI VTWLLTEIPA 150
    GGRVGFDPFL LSIDTWESYD LALQGSNRQL VSITTNLVDL VWGSERPPVP 200
    NQPIYALQEA FTGSTWQEKV SGVRSQMQKH QKVPTAVLLS ALEETAWLFN 250
    LRASDIPYNP FFYSYTLLTD SSIRLFANKS RFSSETLSYL NSSCTGPMCV 300
    QIEDYSQVRD SIQAYSLGDV RIWIGTSYTM YGIYEMIPKE KLVTDTYSPV 350
    MMTKAVKNSK EQALLKASHV RDAVAVIRYL VWLEKNVPKG TVDEFSGAEI 400
    VDKFRGEEQF SSGPSFETIS ASGLNAALAH YSPTKELNRK LSSDEMYLLD 450
    SGGQYWDGTT DITRTVHWGT PSAFQKEAYT RVLIGNIDLS RLIFPAATSG 500
    RMVEAFARRA LWDAGLNYGH GTGHGIGNFL CVHEWPVGFQ SNNIAMAKGM 550
    FTSIEPGYYK DGEFGIRLED VALVVEAKTK YPGSYLTFEV VSFVPYDRNL 600
    IDVSLLSPEH LQYLNRYYQT IREKVGPELQ RRQLLEEFEW LQQHTEPLAA 650
    RAPDTASWAS VLVVSTLAIL GWSV 674
    Length:674
    Mass (Da):75,625
    Last modified:November 15, 2002 - v3
    Checksum:i75949336EDD0F3B4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261V → L in AAB96394. (PubMed:9375790)Curated
    Sequence conflicti339 – 3391K → R in AAB96394. (PubMed:9375790)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U90724 mRNA. Translation: AAB96394.2.
    AF195953 Genomic DNA. Translation: AAG28480.1.
    AL023653 Genomic DNA. Translation: CAA19220.1.
    BC126174 mRNA. Translation: AAI26175.1.
    CCDSiCCDS14613.1.
    RefSeqiNP_003390.4. NM_003399.5.
    UniGeneiHs.170499.

    Genome annotation databases

    EnsembliENST00000371106; ENSP00000360147; ENSG00000122121.
    GeneIDi7512.
    KEGGihsa:7512.
    UCSCiuc004eut.1. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U90724 mRNA. Translation: AAB96394.2 .
    AF195953 Genomic DNA. Translation: AAG28480.1 .
    AL023653 Genomic DNA. Translation: CAA19220.1 .
    BC126174 mRNA. Translation: AAI26175.1 .
    CCDSi CCDS14613.1.
    RefSeqi NP_003390.4. NM_003399.5.
    UniGenei Hs.170499.

    3D structure databases

    ProteinModelPortali O43895.
    SMRi O43895. Positions 403-582.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-5002270.
    STRINGi 9606.ENSP00000360147.

    Chemistry

    BindingDBi O43895.
    ChEMBLi CHEMBL4610.

    Protein family/group databases

    MEROPSi M24.005.

    PTM databases

    PhosphoSitei O43895.

    Proteomic databases

    PaxDbi O43895.
    PRIDEi O43895.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371106 ; ENSP00000360147 ; ENSG00000122121 .
    GeneIDi 7512.
    KEGGi hsa:7512.
    UCSCi uc004eut.1. human.

    Organism-specific databases

    CTDi 7512.
    GeneCardsi GC0XP128872.
    HGNCi HGNC:12823. XPNPEP2.
    HPAi CAB025136.
    CAB025269.
    HPA000339.
    MIMi 300145. gene.
    neXtProti NX_O43895.
    Orphaneti 100057. Renin-angiotensin-aldosterone system-blocker-induced angioedema.
    PharmGKBi PA37416.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0006.
    HOGENOMi HOG000255713.
    HOVERGENi HBG002934.
    InParanoidi O43895.
    KOi K14208.
    OMAi AFTGSTW.
    OrthoDBi EOG7BGHK4.
    PhylomeDBi O43895.
    TreeFami TF314183.

    Miscellaneous databases

    GeneWikii XPNPEP2.
    GenomeRNAii 7512.
    NextBioi 29399.
    PROi O43895.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43895.
    Bgeei O43895.
    CleanExi HS_XPNPEP2.
    Genevestigatori O43895.

    Family and domain databases

    Gene3Di 3.40.350.10. 1 hit.
    3.90.230.10. 1 hit.
    InterProi IPR029149. 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 ]
    Pfami PF01321. Creatinase_N. 1 hit.
    PF00557. Peptidase_M24. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53092. SSF53092. 1 hit.
    SSF55920. SSF55920. 1 hit.
    PROSITEi PS00491. PROLINE_PEPTIDASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiXPP2_HUMAN
    AccessioniPrimary (citable) accession number: O43895
    Secondary accession number(s): A0AV16, O75994
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: November 15, 2002
    Last modified: October 1, 2014
    This is version 121 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3