ID   XPP2_HUMAN              Reviewed;         674 AA.
AC   O43895; A0AV16; O75994;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-NOV-2002, sequence version 3.
DT   13-FEB-2019, entry version 156.
DE   RecName: Full=Xaa-Pro aminopeptidase 2;
DE            EC=3.4.11.9 {ECO:0000269|PubMed:15361070};
DE   AltName: Full=Aminoacylproline aminopeptidase;
DE   AltName: Full=Membrane-bound aminopeptidase P;
DE            Short=Membrane-bound APP;
DE            Short=Membrane-bound AmP;
DE            Short=mAmP;
DE   AltName: Full=X-Pro aminopeptidase 2;
DE   Flags: Precursor;
GN   Name=XPNPEP2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Kidney, and Lung;
RX   PubMed=9375790; DOI=10.1016/S0167-4781(97)00126-7;
RA   Venema R.C., Ju H., Zou R., Venema V.J., Ryan J.W.;
RT   "Cloning and tissue distribution of human membrane-bound
RT   aminopeptidase P.";
RL   Biochim. Biophys. Acta 1354:45-48(1997).
RN   [2]
RP   SEQUENCE REVISION.
RA   Sprinkle T.J.C., Venema R.C., Ju H., Zou R., Venema V.J., Ryan J.W.;
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Ryan J.W., Jin L., Horvath I., Sprinkle T.J.C.;
RT   "Human membrane-bound aminopeptidase P genomic DNA.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA   Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA   Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA   Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA   Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA   Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA   Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA   Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA   Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA   Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA   Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA   Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA   Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA   Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA   Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA   Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA   Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA   Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA   Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA   Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA   Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA   Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA   Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA   Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA   de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA   Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA   Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA   Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA   Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA   Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA   Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA   Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA   Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA   Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA   Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA   Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA   Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA   Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA   Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA   Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA   Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA   Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA   Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA   Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   INVOLVEMENT IN AEACEI.
RX   PubMed=16175507; DOI=10.1086/496899;
RA   Duan Q.L., Nikpoor B., Dube M.P., Molinaro G., Meijer I.A., Dion P.,
RA   Rochefort D., Saint-Onge J., Flury L., Brown N.J., Gainer J.V.,
RA   Rouleau J.L., Agostoni A., Cugno M., Simon P., Clavel P., Potier J.,
RA   Wehbe B., Benarbia S., Marc-Aurele J., Chanard J., Foroud T., Adam A.,
RA   Rouleau G.A.;
RT   "A variant in XPNPEP2 is associated with angioedema induced by
RT   angiotensin I-converting enzyme inhibitors.";
RL   Am. J. Hum. Genet. 77:617-626(2005).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND GLYCOSYLATION.
RX   PubMed=15361070; DOI=10.1042/BJ20040849;
RA   Molinaro G., Carmona A.K., Juliano M.A., Juliano L., Malitskaya E.,
RA   Yessine M.A., Chagnon M., Lepage Y., Simmons W.H., Boileau G.,
RA   Adam A.;
RT   "Human recombinant membrane-bound aminopeptidase P: production of a
RT   soluble form and characterization using novel, internally quenched
RT   fluorescent substrates.";
RL   Biochem. J. 385:389-397(2005).
RN   [8]
RP   INVOLVEMENT IN AEACEI.
RX   PubMed=20625347; DOI=10.1097/FPC.0b013e32833d3acb;
RA   Woodard-Grice A.V., Lucisano A.C., Byrd J.B., Stone E.R.,
RA   Simmons W.H., Brown N.J.;
RT   "Sex-dependent and race-dependent association of XPNPEP2 C-2399A
RT   polymorphism with angiotensin-converting enzyme inhibitor-associated
RT   angioedema.";
RL   Pharmacogenet. Genomics 20:532-536(2010).
RN   [9]
RP   INVOLVEMENT IN AEACEI, AND VARIANTS ILE-215; ILE-223 AND ASN-232.
RX   PubMed=21898657; DOI=10.1002/humu.21579;
RA   Cilia La Corte A.L., Carter A.M., Rice G.I., Duan Q.L., Rouleau G.A.,
RA   Adam A., Grant P.J., Hooper N.M.;
RT   "A functional XPNPEP2 promoter haplotype leads to reduced plasma
RT   aminopeptidase P and increased risk of ACE inhibitor-induced
RT   angioedema.";
RL   Hum. Mutat. 32:1326-1331(2011).
CC   -!- FUNCTION: Membrane-bound metalloprotease which catalyzes the
CC       removal of a penultimate prolyl residue from the N-termini of
CC       peptides, such as Arg-Pro-Pro. May play a role in the metabolism
CC       of the vasodilator bradykinin. {ECO:0000269|PubMed:15361070}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of any N-terminal amino acid, including proline,
CC         that is linked to proline, even from a dipeptide or tripeptide.;
CC         EC=3.4.11.9; Evidence={ECO:0000269|PubMed:15361070};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q95333};
CC   -!- ACTIVITY REGULATION: Inhibited by apstatin and the chelating agent
CC       1,10-phenanthroline. Also inhibited by high concentrations of
CC       Zn(2+). Not significantly inhibited by bestatin or phosphoramidon.
CC       {ECO:0000269|PubMed:15361070}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.837 mM for Arg-Pro-Pro {ECO:0000269|PubMed:15361070};
CC         KM=75 uM for Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg (bradykinin)
CC         {ECO:0000269|PubMed:15361070};
CC         KM=56 uM for Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe (bradykinin[1-8])
CC         {ECO:0000269|PubMed:15361070};
CC         KM=18 uM for synthetic fluorescent substrate Lys(Dnp)-Pro-Pro-
CC         Gly-Phe-Ser-Pro-Lys(Abz)NH(2) {ECO:0000269|PubMed:15361070};
CC         KM=20 uM for synthetic fluorescent substrate Lys(Dnp)-Pro-Pro-
CC         Gly-Lys(Abz)NH(2) {ECO:0000269|PubMed:15361070};
CC         KM=19 uM for synthetic fluorescent substrate Lys(Dnp)-Pro-Pro-
CC         Lys(Abz)NH(2) {ECO:0000269|PubMed:15361070};
CC       pH dependence:
CC         Optimum pH is 7.4. {ECO:0000269|PubMed:15361070};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q95333}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:Q95333}; Lipid-anchor, GPI-anchor
CC       {ECO:0000250|UniProtKB:Q95333}.
CC   -!- TISSUE SPECIFICITY: Expressed in kidney, lung, heart, placenta,
CC       liver, small intestine and colon. No expression in brain, skeletal
CC       muscle, pancreas, spleen, thymus, prostate, testis and ovary.
CC       {ECO:0000269|PubMed:9375790}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15361070}.
CC   -!- DISEASE: Angioedema induced by ACE inhibitors (AEACEI)
CC       [MIM:300909]: A potentially life-threatening side effect of ACE
CC       inhibitors that appears in a subset of patients taking these drugs
CC       for hypertension and cardiovascular disease treatment. AEACEI is
CC       characterized by swelling of the face, lips, tongue, and airway
CC       that can lead to suffocation and death if severe.
CC       {ECO:0000269|PubMed:16175507, ECO:0000269|PubMed:20625347,
CC       ECO:0000269|PubMed:21898657}. Note=Disease susceptibility is
CC       associated with variations affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR   EMBL; U90724; AAB96394.2; -; mRNA.
DR   EMBL; AF195953; AAG28480.1; -; Genomic_DNA.
DR   EMBL; AL023653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC126174; AAI26175.1; -; mRNA.
DR   CCDS; CCDS14613.1; -.
DR   RefSeq; NP_003390.4; NM_003399.5.
DR   UniGene; Hs.170499; -.
DR   ProteinModelPortal; O43895; -.
DR   SMR; O43895; -.
DR   IntAct; O43895; 1.
DR   STRING; 9606.ENSP00000360147; -.
DR   BindingDB; O43895; -.
DR   ChEMBL; CHEMBL4610; -.
DR   GuidetoPHARMACOLOGY; 1579; -.
DR   MEROPS; M24.005; -.
DR   iPTMnet; O43895; -.
DR   PhosphoSitePlus; O43895; -.
DR   BioMuta; XPNPEP2; -.
DR   EPD; O43895; -.
DR   jPOST; O43895; -.
DR   PaxDb; O43895; -.
DR   PeptideAtlas; O43895; -.
DR   PRIDE; O43895; -.
DR   ProteomicsDB; 49219; -.
DR   Ensembl; ENST00000371106; ENSP00000360147; ENSG00000122121.
DR   GeneID; 7512; -.
DR   KEGG; hsa:7512; -.
DR   UCSC; uc004eut.2; human.
DR   CTD; 7512; -.
DR   DisGeNET; 7512; -.
DR   EuPathDB; HostDB:ENSG00000122121.10; -.
DR   GeneCards; XPNPEP2; -.
DR   HGNC; HGNC:12823; XPNPEP2.
DR   HPA; CAB025136; -.
DR   HPA; CAB025269; -.
DR   HPA; HPA000339; -.
DR   MalaCards; XPNPEP2; -.
DR   MIM; 300145; gene.
DR   MIM; 300909; phenotype.
DR   neXtProt; NX_O43895; -.
DR   OpenTargets; ENSG00000122121; -.
DR   Orphanet; 100057; Renin-angiotensin-aldosterone system-blocker-induced angioedema.
DR   PharmGKB; PA37416; -.
DR   eggNOG; KOG2413; Eukaryota.
DR   eggNOG; COG0006; LUCA.
DR   GeneTree; ENSGT00940000157196; -.
DR   HOGENOM; HOG000255713; -.
DR   HOVERGEN; HBG002934; -.
DR   InParanoid; O43895; -.
DR   KO; K14208; -.
DR   OMA; PVMVTKA; -.
DR   OrthoDB; 1247045at2759; -.
DR   PhylomeDB; O43895; -.
DR   TreeFam; TF314183; -.
DR   Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   GeneWiki; XPNPEP2; -.
DR   GenomeRNAi; 7512; -.
DR   PRO; PR:O43895; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   Bgee; ENSG00000122121; Expressed in 98 organ(s), highest expression level in jejunal mucosa.
DR   ExpressionAtlas; O43895; baseline and differential.
DR   Genevisible; O43895; HS.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0004177; F:aminopeptidase activity; TAS:ProtInc.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   CDD; cd01085; APP; 1.
DR   Gene3D; 3.40.350.10; -; 2.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000587; Creatinase_N.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR033740; Pept_M24B.
DR   InterPro; IPR032416; Peptidase_M24_C.
DR   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR   Pfam; PF01321; Creatinase_N; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   Pfam; PF16188; Peptidase_M24_C; 1.
DR   SUPFAM; SSF53092; SSF53092; 1.
DR   SUPFAM; SSF55920; SSF55920; 1.
DR   PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Cell membrane; Complete proteome; Glycoprotein;
KW   GPI-anchor; Hydrolase; Lipoprotein; Membrane; Metal-binding;
KW   Metalloprotease; Polymorphism; Protease; Reference proteome; Signal;
KW   Zinc.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22    649       Xaa-Pro aminopeptidase 2.
FT                                /FTId=PRO_0000026829.
FT   PROPEP      650    674       Removed in mature form. {ECO:0000305}.
FT                                /FTId=PRO_0000026830.
FT   METAL       450    450       Zinc 1. {ECO:0000250|UniProtKB:O44750}.
FT   METAL       461    461       Zinc 1. {ECO:0000250|UniProtKB:O44750}.
FT   METAL       461    461       Zinc 2. {ECO:0000250|UniProtKB:O44750}.
FT   METAL       524    524       Zinc 2; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:O44750}.
FT   METAL       555    555       Zinc 2. {ECO:0000250|UniProtKB:O44750}.
FT   METAL       569    569       Zinc 1. {ECO:0000250|UniProtKB:O44750}.
FT   METAL       569    569       Zinc 2. {ECO:0000250|UniProtKB:O44750}.
FT   BINDING     116    116       Substrate.
FT                                {ECO:0000250|UniProtKB:O44750}.
FT   BINDING     430    430       Substrate; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:O44750}.
FT   BINDING     524    524       Substrate; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:O44750}.
FT   BINDING     533    533       Substrate; via tele nitrogen.
FT                                {ECO:0000250|UniProtKB:O44750}.
FT   BINDING     555    555       Substrate.
FT                                {ECO:0000250|UniProtKB:O44750}.
FT   LIPID       649    649       GPI-anchor amidated alanine.
FT                                {ECO:0000250|UniProtKB:Q95333}.
FT   CARBOHYD     35     35       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     49     49       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     65     65       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    278    278       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    291    291       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VARIANT     215    215       T -> I (in dbSNP:rs138365897).
FT                                {ECO:0000269|PubMed:21898657}.
FT                                /FTId=VAR_071310.
FT   VARIANT     223    223       V -> I (in dbSNP:rs61733030).
FT                                {ECO:0000269|PubMed:21898657}.
FT                                /FTId=VAR_071311.
FT   VARIANT     232    232       K -> N (in dbSNP:rs41311662).
FT                                {ECO:0000269|PubMed:21898657}.
FT                                /FTId=VAR_071312.
FT   CONFLICT     26     26       V -> L (in Ref. 1; AAB96394).
FT                                {ECO:0000305}.
FT   CONFLICT    339    339       K -> R (in Ref. 1; AAB96394).
FT                                {ECO:0000305}.
SQ   SEQUENCE   674 AA;  75625 MW;  75949336EDD0F3B4 CRC64;
     MARAHWGCCP WLVLLCACAW GHTKPVDLGG QDVRNCSTNP PYLPVTVVNT TMSLTALRQQ
     MQTQNLSAYI IPGTDAHMNE YIGQHDERRA WITGFTGSAG TAVVTMKKAA VWTDSRYWTQ
     AERQMDCNWE LHKEVGTTPI VTWLLTEIPA GGRVGFDPFL LSIDTWESYD LALQGSNRQL
     VSITTNLVDL VWGSERPPVP NQPIYALQEA FTGSTWQEKV SGVRSQMQKH QKVPTAVLLS
     ALEETAWLFN LRASDIPYNP FFYSYTLLTD SSIRLFANKS RFSSETLSYL NSSCTGPMCV
     QIEDYSQVRD SIQAYSLGDV RIWIGTSYTM YGIYEMIPKE KLVTDTYSPV MMTKAVKNSK
     EQALLKASHV RDAVAVIRYL VWLEKNVPKG TVDEFSGAEI VDKFRGEEQF SSGPSFETIS
     ASGLNAALAH YSPTKELNRK LSSDEMYLLD SGGQYWDGTT DITRTVHWGT PSAFQKEAYT
     RVLIGNIDLS RLIFPAATSG RMVEAFARRA LWDAGLNYGH GTGHGIGNFL CVHEWPVGFQ
     SNNIAMAKGM FTSIEPGYYK DGEFGIRLED VALVVEAKTK YPGSYLTFEV VSFVPYDRNL
     IDVSLLSPEH LQYLNRYYQT IREKVGPELQ RRQLLEEFEW LQQHTEPLAA RAPDTASWAS
     VLVVSTLAIL GWSV
//