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UniProtKB/Swiss-Prot entry Q9NQW7


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

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Entry information
Entry name XPP1_HUMAN
Primary accession number Q9NQW7
Secondary accession numbers O15250 Q53EX6 Q8N3Q0 Q96D23
Integrated into Swiss-Prot on July 5, 2005
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 67)
Name and origin of the protein
Protein name Xaa-Pro aminopeptidase 1
Synonyms EC 3.4.11.9
X-Pro aminopeptidase 1
X-prolyl aminopeptidase 1, soluble
Cytosolic aminopeptidase P
Soluble aminopeptidase P
sAmp
Aminoacylproline aminopeptidase
Gene name
Name: XPNPEP1
Synonyms: XPNPEPL, XPNPEPL1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Lymphocyte;
PubMed=9465902 [NCBI, ExPASy, EBI, Israel, Japan]
Vanhoof G., Goossens F., Juliano M.A., Juliano L., Hendriks D., Schatteman K., Lin A.H., Scharpe S.;
"Isolation and sequence analysis of a human cDNA clone (XPNPEPL) homologous to X-prolyl aminopeptidase (aminopeptidase P).";
Cytogenet. Cell Genet. 78:275-280(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
DOI=10.1006/abbi.2000.1792; PubMed=10871044 [NCBI, ExPASy, EBI, Israel, Japan]
Sprinkle T.J., Caldwell C., Ryan J.W.;
"Cloning, chromosomal sublocalization of the human soluble aminopeptidase P gene (XPNPEP1) to 10q25.3 and conservation of the putative proton shuttle and metal ligand binding sites with XPNPEP2.";
Arch. Biochem. Biophys. 378:51-56(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
TISSUE=Pancreatic adenocarcinoma;
DOI=10.1021/bi001585c; PubMed=11106490 [NCBI, ExPASy, EBI, Israel, Japan]
Cottrell G.S., Hooper N.M., Turner A.J.;
"Cloning, expression, and characterization of human cytosolic aminopeptidase P: a single manganese(II)-dependent enzyme.";
Biochemistry 39:15121-15128(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Adipose tissue;
The German cDNA consortium;
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02462; PubMed=15164054 [NCBI, ExPASy, EBI, Israel, Japan]
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon, Ovary, and Placenta;
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).
[9]
PROTEIN SEQUENCE OF 2-11.
TISSUE=Platelet;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[10]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
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
X95762; CAA65068.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF195530; AAF97866.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF272981; AAF75795.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL833411; CAD38640.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456922; CAG33203.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK223513; BAD97233.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL354951; CAI14248.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005126; AAH05126.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007579; AAH07579.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013417; AAH13417.4; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00607814; -.
IPI00793375; -.
RefSeq NP_065116.2; -.
UniGene Hs.390623
3D structure databases
PDB
3CTZ; X-ray; 1.60 A; A=1-623.[ExPASy / RCSB / EBI]
PDBsum 3CTZ; -.
ModBase Q9NQW7.
Protein-protein interaction databases
IntAct Q9NQW7; 4.
Protein family/group databases
MEROPS M24.009; -.
Enzyme and pathway databases
BRENDA 3.4.11.9; 247.
Organism-specific databases
GeneCards GC10M111614; -.
H-InvDB HIX0009194; -.
HGNC HGNC:12822; XPNPEP1.
GenAtlas XPNPEP1.
MIM 602443; gene. [NCBI / EBI]
PharmGKB PA37415; -.
Gene expression databases
ArrayExpress Q9NQW7; -.
Bgee Q9NQW7; -.
CleanEx HS_XPNPEP1; -.
GermOnline ENSG00000108039; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from sequence or structural similarity from UniProtKB).
GO:0004177; Molecular function: aminopeptidase activity (inferred from direct assay from UniProtKB).
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 direct assay from UniProtKB).
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 Q9NQW7; -.
Genome annotation databases
Ensembl ENSG00000108039; Homo sapiens. [Contig view]
GeneID 7511; -.
KEGG hsa:7511; -.
Phylogenomic databases
HOGENOM Q9NQW7; -.
HOVERGEN Q9NQW7; -.
OMA Q9NQW7; PRADEYL.
Other
NextBio 29395; -.
SOURCE XPNPEP1; Homo sapiens.
ProtoNet Q9NQW7.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Aminopeptidase; Cytoplasm; Direct protein sequencing; Hydrolase; Manganese; Metal-binding; Metalloprotease; Protease.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   623  622     Xaa-Pro aminopeptidase 1. PRO_0000185083
METAL   415   415        Manganese 2 (By similarity). 
METAL   426   426        Manganese 1 (By similarity). 
METAL   426   426        Manganese 2 (By similarity). 
METAL   523   523        Manganese 1 (By similarity). 
METAL   537   537        Manganese 1 (By similarity). 
METAL   537   537        Manganese 2 (By similarity). 
VAR_SEQ   398   421        Missing (in isoform 2). VSP_051752
CONFLICT   90    90        W -> C (in Ref. 8; AAH13417). 
CONFLICT   332   332        R -> P (in Ref. 1 and 2). 
CONFLICT   496   496        N -> D (in Ref. 6). 
CONFLICT   498   498        H -> R (in Ref. 6). 
HELIX   7    16  10      
TURN   20    22  3      
STRAND   28    32  5      
HELIX   45    47  3      
HELIX   49    54  6      
STRAND   62    68  7      
STRAND   70    74  5      
HELIX   76    78  3      
HELIX   79    85  7      
STRAND   90    94  5      
HELIX   103   110  8      
STRAND   116   119  4      
HELIX   121   123  3      
HELIX   126   138  13      
STRAND   142   145  4      
HELIX   150   154  5      
HELIX   171   174  4      
HELIX   178   190  13      
TURN   191   193  3      
STRAND   194   199  6      
HELIX   202   209  8      
STRAND   215   219  5      
STRAND   225   231  7      
STRAND   233   236  4      
HELIX   240   243  4      
HELIX   245   250  6      
TURN   251   254  4      
HELIX   259   261  3      
STRAND   263   266  4      
HELIX   268   270  3      
HELIX   271   280  10      
STRAND   287   291  5      
HELIX   296   301  6      
HELIX   304   306  3      
STRAND   307   312  6      
HELIX   314   320  7      
HELIX   324   351  28      
HELIX   352   354  3      
HELIX   359   371  13      
STRAND   376   381  6      
STRAND   384   387  4      
HELIX   388   392  5      
HELIX   400   402  3      
STRAND   412   416  5      
STRAND   418   420  3      
STRAND   427   431  5      
HELIX   438   455  18      
HELIX   465   472  8      
HELIX   474   478  5      
STRAND   487   490  4      
STRAND   493   495  3      
STRAND   519   522  4      
STRAND   525   528  4      
TURN   529   531  3      
STRAND   532   535  4      
STRAND   537   545  9      
STRAND   552   554  3      
STRAND   556   561  6      
HELIX   569   571  3      
HELIX   574   576  3      
HELIX   579   602  24      
HELIX   606   614  9      
Sequence information
Length: 623 AA [This is the length of the unprocessed precursor] Molecular weight: 69918 Da [This is the MW of the unprocessed precursor] CRC64: DF4F5AF41E2F3876 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPPKVTSELL RQLRQAMRNS EYVTEPIQAY IIPSGDAHQS EYIAPCDCRR AFVSGFDGSA 

        70         80         90        100        110        120 
GTAIITEEHA AMWTDGRYFL QAAKQMDSNW TLMKMGLKDT PTQEDWLVSV LPEGSRVGVD 

       130        140        150        160        170        180 
PLIIPTDYWK KMAKVLRSAG HHLIPVKENL VDKIWTDRPE RPCKPLLTLG LDYTGISWKD 

       190        200        210        220        230        240 
KVADLRLKMA ERNVMWFVVT ALDEIAWLFN LRGSDVEHNP VFFSYAIIGL ETIMLFIDGD 

       250        260        270        280        290        300 
RIDAPSVKEH LLLDLGLEAE YRIQVHPYKS ILSELKALCA DLSPREKVWV SDKASYAVSE 

       310        320        330        340        350        360 
TIPKDHRCCM PYTPICIAKA VKNSAESEGM RRAHIKDAVA LCELFNWLEK EVPKGGVTEI 

       370        380        390        400        410        420 
SAADKAEEFR RQQADFVDLS FPTISSTGPN GAIIHYAPVP ETNRTLSLDE VYLIDSGAQY 

       430        440        450        460        470        480 
KDGTTDVTRT MHFGTPTAYE KECFTYVLKG HIAVSAAVFP TGTKGHLLDS FARSALWDSG 

       490        500        510        520        530        540 
LDYLHGTGHG VGSFLNVHEG PCGISYKTFS DEPLEAGMIV TDEPGYYEDG AFGIRIENVV 

       550        560        570        580        590        600 
LVVPVKTKYN FNNRGSLTFE PLTLVPIQTK MIDVDSLTDK ECDWLNNYHL TCRDVIGKEL 

       610        620 
QKQGRQEALE WLIRETQPIS KQH 

Q9NQW7 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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