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O43895

- XPP2_HUMAN

UniProt

O43895 - XPP2_HUMAN

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Protein

Xaa-Pro aminopeptidase 2

Gene

XPNPEP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

Mn2+By similarityNote: 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
Complete GO annotation...

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-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Angioedema induced by ACE inhibitors (AEACEI) [MIM:300909]: A potentially life-threatening side effect of ACE inhibitors that appears in a subset of patients taking these drugs for hypertension and cardiovascular disease treatment. AEACEI is characterized by swelling of the face, lips, tongue, and airway that can lead to suffocation and death if severe.3 Publications
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Organism-specific databases

MIMi300909. phenotype.
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

BgeeiO43895.
CleanExiHS_XPNPEP2.
ExpressionAtlasiO43895. baseline and differential.
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.
GeneTreeiENSGT00390000013970.
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

        10         20         30         40         50
MARAHWGCCP WLVLLCACAW GHTKPVDLGG QDVRNCSTNP PYLPVTVVNT
60 70 80 90 100
TMSLTALRQQ MQTQNLSAYI IPGTDAHMNE YIGQHDERRA WITGFTGSAG
110 120 130 140 150
TAVVTMKKAA VWTDSRYWTQ AERQMDCNWE LHKEVGTTPI VTWLLTEIPA
160 170 180 190 200
GGRVGFDPFL LSIDTWESYD LALQGSNRQL VSITTNLVDL VWGSERPPVP
210 220 230 240 250
NQPIYALQEA FTGSTWQEKV SGVRSQMQKH QKVPTAVLLS ALEETAWLFN
260 270 280 290 300
LRASDIPYNP FFYSYTLLTD SSIRLFANKS RFSSETLSYL NSSCTGPMCV
310 320 330 340 350
QIEDYSQVRD SIQAYSLGDV RIWIGTSYTM YGIYEMIPKE KLVTDTYSPV
360 370 380 390 400
MMTKAVKNSK EQALLKASHV RDAVAVIRYL VWLEKNVPKG TVDEFSGAEI
410 420 430 440 450
VDKFRGEEQF SSGPSFETIS ASGLNAALAH YSPTKELNRK LSSDEMYLLD
460 470 480 490 500
SGGQYWDGTT DITRTVHWGT PSAFQKEAYT RVLIGNIDLS RLIFPAATSG
510 520 530 540 550
RMVEAFARRA LWDAGLNYGH GTGHGIGNFL CVHEWPVGFQ SNNIAMAKGM
560 570 580 590 600
FTSIEPGYYK DGEFGIRLED VALVVEAKTK YPGSYLTFEV VSFVPYDRNL
610 620 630 640 650
IDVSLLSPEH LQYLNRYYQT IREKVGPELQ RRQLLEEFEW LQQHTEPLAA
660 670
RAPDTASWAS VLVVSTLAIL GWSV
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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti215 – 2151T → I.1 Publication
VAR_071310
Natural varianti223 – 2231V → I.1 Publication
VAR_071311
Natural varianti232 – 2321K → N.1 Publication
VAR_071312

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
300909. phenotype.
neXtProti NX_O43895.
Orphaneti 100057. Renin-angiotensin-aldosterone system-blocker-induced angioedema.
PharmGKBi PA37416.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0006.
GeneTreei ENSGT00390000013970.
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

Bgeei O43895.
CleanExi HS_XPNPEP2.
ExpressionAtlasi O43895. baseline and differential.
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

« Hide 'large scale' publications
  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.
  6. Cited for: INVOLVEMENT IN AEACEI.
  7. "Sex-dependent and race-dependent association of XPNPEP2 C-2399A polymorphism with angiotensin-converting enzyme inhibitor-associated angioedema."
    Woodard-Grice A.V., Lucisano A.C., Byrd J.B., Stone E.R., Simmons W.H., Brown N.J.
    Pharmacogenet. Genomics 20:532-536(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN AEACEI.
  8. "A functional XPNPEP2 promoter haplotype leads to reduced plasma aminopeptidase P and increased risk of ACE inhibitor-induced angioedema."
    Cilia La Corte A.L., Carter A.M., Rice G.I., Duan Q.L., Rouleau G.A., Adam A., Grant P.J., Hooper N.M.
    Hum. Mutat. 32:1326-1331(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN AEACEI, VARIANTS ILE-215; ILE-223 AND ASN-232.

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: November 26, 2014
This is version 123 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. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3