Reviewed,
UniProtKB/Swiss-Prot Q86TI2 (DPP9_HUMAN)
Last modified
November 25, 2008.
Version 50.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Dipeptidyl peptidase 9 EC=3.4.14.5 Alternative name(s): Dipeptidyl peptidase IX DP9 Dipeptidyl peptidase-like protein 9 Short name=DPLP9 Dipeptidyl peptidase IV-related protein 2 Short name=DPRP-2 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 863 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. |
| Catalytic activity | Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. |
| Enzyme regulation | Inhibited by the serine proteinase inhibitor 4-(2-aminoethyl)benzenesulphonyl fluoride (AEBSF), and by di-isopropylfuorophosphate. |
| Subcellular location | |
| Tissue specificity | Ubiquitously expressed, with highest levels in liver, heart and muscle, and lowest levels in brain. |
| Sequence similarities | Belongs to the peptidase S9B family. DPPIV subfamily. |
| Biophysicochemical properties | Kinetic parameters: KM=161 µM for Ala-Pro-AMC KM=180 µM for Ala-Pro-AFC pH dependence: Optimum pH is 7.5-8.5. Little activity below pH 6.5. |
| Sequence caution | The sequence AAC33801.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAC62840.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAD39039.3 differs from that shown. Reason: Frameshift at positions 432 and 460. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Coding sequence diversity | Alternative splicing |
| Molecular function | Aminopeptidase Hydrolase Protease Serine protease |
Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW membraneInferred from electronic annotation. Source: InterPro |
| Molecular function | aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 5 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q86TI2-1) Also known as: Short; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: Q86TI2-2) Also known as: Long; The sequence of this isoform differs from the canonical sequence as follows: 1-1: M → LSRRVPCVRR...FSLNSEGAER | ||||||
| Notes: Incomplete sequence. | ||||||
| Isoform 3 (identifier: Q86TI2-3) The sequence of this isoform differs from the canonical sequence as follows: 650-674: QLVNNSFKGIKYLRLNTLASLGYAV → SAHLLPRPPPHHPPEDSPSPLKCQL 675-863: Missing. | ||||||
| Isoform 4 (identifier: Q86TI2-4) The sequence of this isoform differs from the canonical sequence as follows: 832-858: Missing. | ||||||
| Isoform 5 (identifier: Q86TI2-5) The sequence of this isoform differs from the canonical sequence as follows: 1-1: M → LSRRVPCVRR...FSLNSEGAER 3-139: Missing. | ||||||
| Notes: Incomplete sequence. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 863 | 863 | Dipeptidyl peptidase 9 | PRO_0000122415 | |||||
Sites | |||||||||
| Active site | 730 | 1 | Charge relay system By similarity | ||||||
| Active site | 808 | 1 | Charge relay system By similarity | ||||||
| Active site | 840 | 1 | Charge relay system By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 | 1 | M → LSRRVPCVRRGCRPPLPPLP GSQSRAWSRDREAPLDPGRP AQSGRRPTSRSVSHACSWNG GSLDPLEGTPALLRSAERLM RKVKKLRLDKENTGSWRSFS LNSEGAER in isoform 2 and isoform 5. | VSP_013865 | |||||
| Alternative sequence | 3 – 139 | 137 | Missing in isoform 5. | VSP_013866 | |||||
| Alternative sequence | 650 – 674 | 25 | QLVNN…LGYAV → SAHLLPRPPPHHPPEDSPSP LKCQL in isoform 3. | VSP_013867 | |||||
| Alternative sequence | 675 – 863 | 189 | Missing in isoform 3. | VSP_013868 | |||||
| Alternative sequence | 832 – 858 | 27 | Missing in isoform 4. | VSP_013869 | |||||
Experimental info | |||||||||
| Sequence conflict | 204 | 1 | I → N in AAO73880 and AAQ83119. Ref.3 | ||||||
| Sequence conflict | 571 | 1 | C → W in BAC85150. Ref.6 | ||||||
| Sequence conflict | 709 | 1 | L → P in BAD18643. Ref.6 | ||||||
| Sequence conflict | 753 | 1 | G → C in BAB70784. Ref.6 | ||||||
Sequences
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References
| [1] | "Identification and characterization of human DPP9, a novel homologue of dipeptidyl peptidase IV." Olsen C., Wagtmann N. Gene 299:185-193(2002) [PubMed: 12459266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. |
| [2] | "Cloning and characterization of dipeptidyl peptidase 10, a new member of an emerging subgroup of serine proteases." Qi S.Y., Riviere P.J., Trojnar J., Junien J.-L., Akinsanya K.O. Biochem. J. 373:179-189(2003) [PubMed: 12662155] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Tissue: Colon. |
| [3] | "Dipeptidyl peptidase 9 has two forms, a broad tissue distribution, cytoplasmic localization and DPIV-like peptidase activity." Ajami K., Abbott C.A., McCaughan G.W., Gorrell M.D. Biochim. Biophys. Acta 1679:18-28(2004) [PubMed: 15245913] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. |
| [4] | "The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. Lucas S.M.Nature 428:529-535(2004) [PubMed: 15057824] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Placenta and Skin. |
| [6] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-863 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 272-863 (ISOFORM 2), PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). Tissue: Glial tumor, Ovary, Spleen and Trachea. |
| [7] | The German cDNA consortium Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 209-863 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 298-863 (ISOFORM 2). Tissue: Melanoma. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| AF452102 mRNA. Translation: AAL47179.1. AY172660 mRNA. Translation: AAO17262.1. AF542510 mRNA. Translation: AAO73880.2. AY374518 mRNA. Translation: AAQ83119.1. AC005594 Genomic DNA. Translation: AAC33801.1. Sequence problems. AC005783 Genomic DNA. Translation: AAC62840.1. Sequence problems. BC000970 mRNA. Translation: AAH00970.1. BC037948 mRNA. Translation: AAH37948.1. AK054656 mRNA. Translation: BAB70784.1. Different initiation. AK075030 mRNA. Translation: BAC11362.1. AK131100 mRNA. Translation: BAC85150.1. AK131499 mRNA. Translation: BAD18643.1. Different initiation. AL834376 mRNA. Translation: CAD39039.3. Frameshift. CR627380 mRNA. Translation: CAH10477.1. | |
| UniGene | Hs.515081 |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S09.019. |
PTM databases | |
| PhosphoSite | Q86TI2. |
Genome annotation databases | |
| Ensembl | ENSG00000142002. Homo sapiens. [Contig view] |
| KEGG | hsa:91039. |
Organism-specific databases | |
| H-InvDB | HIX0022644. |
| HGNC | HGNC:18648. DPP9. |
| MIM | 608258. gene. |
| PharmGKB | PA38620. |
| GenAtlas | Search... |
| GeneCards | Search... |
Phylogenomic databases | |
| HOVERGEN | Q86TI2. |
Gene expression databases | |
| ArrayExpress | Q86TI2. |
| GermOnline | ENSG00000142002. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR001375. Peptidase_S9. IPR002469. Peptidase_S9B. [Graphical view] |
| Pfam | PF00930. DPPIV_N. 1 hit. PF00326. Peptidase_S9. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 77078. |
| SOURCE | Search... |
Entry information
| Entry name | DPP9_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q86TI2 Secondary accession number(s): O75273 Q9BVR3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 19 Human chromosome 19: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


