O43895 (XPP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

XPNPEP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	674 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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-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.
Post-translational modification	Heavily glycosylated.
Sequence similarities	Belongs to the peptidase M24B family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Signal
Ligand	Manganese Metal-binding
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
PTM	GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular process Inferred from electronic annotation. Source: InterPro proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane Traceable author statement Ref.1. Source: ProtInc plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	aminopeptidase activity Traceable author statement Ref.1. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 649	628	Xaa-Pro aminopeptidase 2		PRO_0000026829
	Propeptide	650 – 674	25	Removed in mature form By similarity		PRO_0000026830
Sites
	Metal binding	450	1	Manganese 2 By similarity
	Metal binding	461	1	Manganese 1 By similarity
	Metal binding	461	1	Manganese 2 By similarity
	Metal binding	555	1	Manganese 1 By similarity
	Metal binding	569	1	Manganese 1 By similarity
	Metal binding	569	1	Manganese 2 By similarity
Amino acid modifications
	Lipidation	649	1	GPI-anchor amidated alanine By similarity
	Glycosylation	35	1	N-linked (GlcNAc...) Potential
	Glycosylation	49	1	N-linked (GlcNAc...) Potential
	Glycosylation	65	1	N-linked (GlcNAc...) Potential
	Glycosylation	278	1	N-linked (GlcNAc...) Potential
	Glycosylation	291	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	26	1	V → L in AAB96394. Ref.1
	Sequence conflict	339	1	K → R in AAB96394. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O43895 [UniParc]. Last modified November 15, 2002. Version 3. Checksum: 75949336EDD0F3B4	FASTA	674	75,625
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00439344.
RefSeq	NP_003390.4. NM_003399.5.
UniGene	Hs.170499.
3D structure databases
ProteinModelPortal	O43895.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000360147.
Protein family/group databases
MEROPS	M24.005.
PTM databases
PhosphoSite	O43895.
Proteomic databases
PaxDb	O43895.
PRIDE	O43895.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000371106; ENSP00000360147; ENSG00000122121.
GeneID	7512.
KEGG	hsa:7512.
UCSC	uc004eut.1. human.
Organism-specific databases
CTD	7512.
GeneCards	GC0XP128872.
HGNC	HGNC:12823. XPNPEP2.
HPA	CAB025136. CAB025269. HPA000339.
MIM	300145. gene.
neXtProt	NX_O43895.
Orphanet	100057. Renin-angiotensin-aldosterone system-blocker-induced angioedema.
PharmGKB	PA37416.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0006.
HOGENOM	HOG000255713.
HOVERGEN	HBG002934.
InParanoid	O43895.
KO	K14208.
OMA	LPKAQKN.
OrthoDB	EOG4CZBFH.
PhylomeDB	O43895.
Gene expression databases
ArrayExpress	O43895.
Bgee	O43895.
CleanEx	HS_XPNPEP2.
Genevestigator	O43895.
GermOnline	ENSG00000122121. Homo sapiens.
Family and domain databases
Gene3D	3.90.230.10. 1 hit.
InterPro	IPR000587. Creatinase. IPR000994. Pept_M24_structural-domain. IPR001131. Peptidase_M24B_aminopep-P_CS. [Graphical view]
Pfam	PF01321. Creatinase_N. 1 hit. PF00557. Peptidase_M24. 1 hit. [Graphical view]
SUPFAM	SSF55920. Peptidase_M24_cat_core. 1 hit.
PROSITE	PS00491. PROLINE_PEPTIDASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	O43895.
ChEMBL	CHEMBL4610.
GenomeRNAi	7512.
NextBio	29399.
SOURCE	Search...

Entry information

Entry name

XPP2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 109 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.