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Q6V1X1 (DPP8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dipeptidyl peptidase 8

Short name=DP8
EC=3.4.14.5
Alternative name(s):
Dipeptidyl peptidase IV-related protein 1
Short name=DPRP-1
Dipeptidyl peptidase VIII
Short name=DPP VIII
Prolyl dipeptidase DPP8
Gene names
Name:DPP8
Synonyms:DPRP1
ORF Names:MSTP097, MSTP135, MSTP141
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length898 AA.
Sequence statusComplete.
Protein existenceEvidence 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. May play a role in T-cell activation and immune function. Ref.1

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. Ref.1 Ref.2 Ref.7

Enzyme regulation

Inhibited by zinc. Inhibited by the serine proteinase inhibitor 4-(2-aminoethyl)benzenesulphonyl fluoride (AEBSF), and by di-isopropylfuorophosphate. Specifically inhibited by isoindoline derivatives. Ref.1 Ref.2 Ref.9

Subcellular location

Cytoplasm Ref.1 Ref.2 Ref.7.

Tissue specificity

Ubiquitously expressed, with highest levels in testis, placenta, prostate, muscle and brain. Ref.1 Ref.2

Induction

In activated T-cells. Ref.1 Ref.2 Ref.9

Sequence similarities

Belongs to the peptidase S9B family. DPPIV subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=208 µM for Ala-Pro-AMC Ref.2 Ref.7 Ref.8

KM=130 µM for Ala-Pro-AFC

KM=120 µM for H-Ala-Pro-pNa

KM=1420 µM for H-Ala-Ala-pNa

KM=310 µM for H-Arg-Pro-pNa

KM=2050 µM for H-Asp-Pro-pNa

KM=480 µM for H-Gly-Pro-pNa

pH dependence:

Optimum pH is 7.4-8.5. Little activity below pH 6.5.

Sequence caution

The sequence AAQ13623.1 differs from that shown. Reason: Frameshift at several positions.

The sequence AAQ13650.1 differs from that shown. Reason: Frameshift at several positions.

The sequence AAQ13657.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA91059.1 differs from that shown. Reason: Frameshift at position 486.

The sequence BAB55395.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6V1X1-1)

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: Q6V1X1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     723-773: Missing.
Isoform 3 (identifier: Q6V1X1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.
Isoform 4 (identifier: Q6V1X1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-16: Missing.
     674-773: Missing.
Isoform 5 (identifier: Q6V1X1-5)

The sequence of this isoform differs from the canonical sequence as follows:
     674-722: Missing.
Isoform 6 (identifier: Q6V1X1-6)

The sequence of this isoform differs from the canonical sequence as follows:
     358-530: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 898898Dipeptidyl peptidase 8
PRO_0000122413

Sites

Active site7551Charge relay system Probable
Active site8331Charge relay system Probable
Active site8651Charge relay system Probable

Natural variations

Alternative sequence1 – 1616Missing in isoform 3 and isoform 4.
VSP_013860
Alternative sequence358 – 530173Missing in isoform 6.
VSP_013861
Alternative sequence674 – 773100Missing in isoform 4.
VSP_013862
Alternative sequence674 – 72249Missing in isoform 5.
VSP_013863
Alternative sequence723 – 77351Missing in isoform 2.
VSP_013864

Experimental info

Mutagenesis2751E → K: 13-fold reduction in affinity for Ala-Pro-AFC; no effect on subcellular location. Ref.7
Mutagenesis7551S → A: Abolishes activity; no effect on subcellular location. Ref.7
Mutagenesis8331D → A: Abolishes activity; no effect on subcellular location. Ref.7
Mutagenesis8651H → A: Abolishes activity; no effect on subcellular location. Ref.7
Sequence conflict2331S → G in BC040203. Ref.5
Sequence conflict5701G → S in BAB55395. Ref.4
Sequence conflict6731Q → K in AAQ13650. Ref.6
Sequence conflict6861Y → F in AAQ13650. Ref.6
Sequence conflict693 – 6942AS → PF in AAQ13650. Ref.6
Sequence conflict7011V → G in AAQ13650. Ref.6
Sequence conflict7091H → P in AAQ13650. Ref.6
Sequence conflict7201Y → F in AAQ13650. Ref.6
Sequence conflict799 – 8035PDQNE → LTRMN in AAQ13623. Ref.6
Sequence conflict8201S → F in AAQ13623. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 60B0D036F026DE2A

FASTA898103,358
        10         20         30         40         50         60 
MWKRSEQMKI KSGKCNMAAA METEQLGVEI FETADCEENI ESQDRPKLEP FYVERYSWSQ 

        70         80         90        100        110        120 
LKKLLADTRK YHGYMMAKAP HDFMFVKRND PDGPHSDRIY YLAMSGENRE NTLFYSEIPK 

       130        140        150        160        170        180 
TINRAAVLML SWKPLLDLFQ ATLDYGMYSR EEELLRERKR IGTVGIASYD YHQGSGTFLF 

       190        200        210        220        230        240 
QAGSGIYHVK DGGPQGFTQQ PLRPNLVETS CPNIRMDPKL CPADPDWIAF IHSNDIWISN 

       250        260        270        280        290        300 
IVTREERRLT YVHNELANME EDARSAGVAT FVLQEEFDRY SGYWWCPKAE TTPSGGKILR 

       310        320        330        340        350        360 
ILYEENDESE VEIIHVTSPM LETRRADSFR YPKTGTANPK VTFKMSEIMI DAEGRIIDVI 

       370        380        390        400        410        420 
DKELIQPFEI LFEGVEYIAR AGWTPEGKYA WSILLDRSQT RLQIVLISPE LFIPVEDDVM 

       430        440        450        460        470        480 
ERQRLIESVP DSVTPLIIYE ETTDIWINIH DIFHVFPQSH EEEIEFIFAS ECKTGFRHLY 

       490        500        510        520        530        540 
KITSILKESK YKRSSGGLPA PSDFKCPIKE EIAITSGEWE VLGRHGSNIQ VDEVRRLVYF 

       550        560        570        580        590        600 
EGTKDSPLEH HLYVVSYVNP GEVTRLTDRG YSHSCCISQH CDFFISKYSN QKNPHCVSLY 

       610        620        630        640        650        660 
KLSSPEDDPT CKTKEFWATI LDSAGPLPDY TPPEIFSFES TTGFTLYGML YKPHDLQPGK 

       670        680        690        700        710        720 
KYPTVLFIYG GPQVQLVNNR FKGVKYFRLN TLASLGYVVV VIDNRGSCHR GLKFEGAFKY 

       730        740        750        760        770        780 
KMGQIEIDDQ VEGLQYLASR YDFIDLDRVG IHGWSYGGYL SLMALMQRSD IFRVAIAGAP 

       790        800        810        820        830        840 
VTLWIFYDTG YTERYMGHPD QNEQGYYLGS VAMQAEKFPS EPNRLLLLHG FLDENVHFAH 

       850        860        870        880        890 
TSILLSFLVR AGKPYDLQIY PQERHSIRVP ESGEHYELHL LHYLQENLGS RIAALKVI 

« Hide

Isoform 2 [UniParc].

Checksum: AB07EF0087231B56
Show »

FASTA84797,464
Isoform 3 [UniParc].

Checksum: AD801C302DB4652B
Show »

FASTA882101,422
Isoform 4 [UniParc].

Checksum: 784922477DB8F5B5
Show »

FASTA78289,908
Isoform 5 [UniParc].

Checksum: 4B6C88F29CA55475
Show »

FASTA84997,739
Isoform 6 [UniParc].

Checksum: 0476E0AEBD94131B
Show »

FASTA72583,398

References

« Hide 'large scale' references
[1]"Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8."
Abbott C.A., Yu D.M.T., Woollatt E., Sutherland G.R., McCaughan G.W., Gorrell M.D.
Eur. J. Biochem. 267:6140-6150(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 334-898 (ISOFORM 4), NUCLEOTIDE SEQUENCE [MRNA] OF 540-898 (ISOFORM 5), NUCLEOTIDE SEQUENCE [MRNA] OF 260-792 (ISOFORM 6), FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION.
Tissue: Placenta.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Testis.
[3]Sha J.H., Zhou Z.M., Li J.M.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Testis.
[4]"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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 211-898 (ISOFORM 2).
Tissue: Hepatoma and Placenta.
[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] (ISOFORMS 1 AND 2).
Tissue: Testis.
[6]Zhao B., Xu H.S., Tong Y.K., Sheng H., Qin B.M., Liu Y.Q., Liu B., Wang X.Y., Zhang Q., Song L., Gao Y., Zhang C.L., Ye J., Ji X.J., Liu B.H., Lu H., Chen J.Z., Cai M.Q. expand/collapse author list , Zheng W.Y., Teng C.Y., Liu Q., Yu L.T., Lin J., Gong Q., Zhang A.M., Gao R.L., Hui R.T.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 561-898.
Tissue: Aorta.
[7]"Structural requirements for catalysis, expression, and dimerization in the CD26/DPIV gene family."
Ajami K., Abbott C.A., Obradovic M., Gysbers V., Kaehne T., McCaughan G.W., Gorrell M.D.
Biochemistry 42:694-701(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLU-275; SER-755; ASP-833 AND HIS-865, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
[8]"Purification and characterization of human prolyl dipeptidase DPP8 in Sf9 insect cells."
Chen Y.-S., Chien C.-H., Goparaju C.M., Hsu J.T.-A., Liang P.-H., Chen X.
Protein Expr. Purif. 35:142-146(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[9]"Novel isoindoline compounds for potent and selective inhibition of prolyl dipeptidase DPP8."
Jiaang W.-T., Chen Y.-S., Hsu T., Wu S.-H., Chien C.-H., Chang C.-N., Chang S.-P., Lee S.-J., Chen X.
Bioorg. Med. Chem. Lett. 15:687-691(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF221634 mRNA. Translation: AAG29766.1.
AF221635 mRNA. Translation: AAG29767.1.
AF221636 mRNA. Translation: AAG29768.1.
AF221637 mRNA. Translation: AAG29769.1.
AY172659 mRNA. Translation: AAO17261.1.
AY354202 mRNA. Translation: AAQ63887.1.
AK000290 mRNA. Translation: BAA91059.1. Frameshift.
AK027826 mRNA. Translation: BAB55395.1. Different initiation.
BC030688 mRNA. Translation: AAH30688.3.
BC040203 mRNA. No translation available.
AF176779 mRNA. Translation: AAQ13657.1. Different initiation.
AF175225 mRNA. Translation: AAQ13650.1. Frameshift.
AF173382 mRNA. Translation: AAQ13623.1. Frameshift.
CCDSCCDS10207.1. [Q6V1X1-1]
CCDS10208.1. [Q6V1X1-2]
CCDS10209.1. [Q6V1X1-4]
CCDS10210.1. [Q6V1X1-3]
RefSeqNP_060213.2. NM_017743.4. [Q6V1X1-4]
NP_569118.1. NM_130434.3. [Q6V1X1-3]
NP_932064.1. NM_197960.2. [Q6V1X1-1]
NP_932065.1. NM_197961.2. [Q6V1X1-2]
XP_005254557.1. XM_005254500.1. [Q6V1X1-1]
UniGeneHs.591106.

3D structure databases

ProteinModelPortalQ6V1X1.
SMRQ6V1X1. Positions 136-886.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120226. 14 interactions.
IntActQ6V1X1. 3 interactions.
MINTMINT-4539721.

Chemistry

BindingDBQ6V1X1.
ChEMBLCHEMBL4657.
GuidetoPHARMACOLOGY2356.

Protein family/group databases

MEROPSS09.018.

PTM databases

PhosphoSiteQ6V1X1.

Polymorphism databases

DMDM67460301.

Proteomic databases

MaxQBQ6V1X1.
PaxDbQ6V1X1.
PRIDEQ6V1X1.

Protocols and materials databases

DNASU54878.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300141; ENSP00000300141; ENSG00000074603. [Q6V1X1-3]
ENST00000321118; ENSP00000316373; ENSG00000074603. [Q6V1X1-5]
ENST00000321147; ENSP00000318111; ENSG00000074603. [Q6V1X1-2]
ENST00000341861; ENSP00000339208; ENSG00000074603. [Q6V1X1-1]
ENST00000358939; ENSP00000351817; ENSG00000074603. [Q6V1X1-4]
ENST00000559233; ENSP00000453954; ENSG00000074603. [Q6V1X1-1]
GeneID54878.
KEGGhsa:54878.
UCSCuc002aov.3. human. [Q6V1X1-1]
uc002aoy.3. human. [Q6V1X1-2]
uc002aoz.3. human. [Q6V1X1-4]

Organism-specific databases

CTD54878.
GeneCardsGC15M065734.
HGNCHGNC:16490. DPP8.
HPAHPA008706.
MIM606819. gene.
neXtProtNX_Q6V1X1.
PharmGKBPA27470.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1506.
HOVERGENHBG061620.
InParanoidQ6V1X1.
KOK08655.
OMASRHCDFF.
OrthoDBEOG7XWPN8.
PhylomeDBQ6V1X1.
TreeFamTF313309.

Enzyme and pathway databases

SABIO-RKQ6V1X1.

Gene expression databases

ArrayExpressQ6V1X1.
BgeeQ6V1X1.
GenevestigatorQ6V1X1.

Family and domain databases

Gene3D2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view]
PfamPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMSSF53474. SSF53474. 1 hit.
ProtoNetSearch...

Other

GeneWikiDPP8.
GenomeRNAi54878.
NextBio57817.
PROQ6V1X1.
SOURCESearch...

Entry information

Entry nameDPP8_HUMAN
AccessionPrimary (citable) accession number: Q6V1X1
Secondary accession number(s): Q7Z4C8 expand/collapse secondary AC list , Q7Z4D3, Q7Z4E1, Q8IWG7, Q8NEM5, Q96JX1, Q9HBM2, Q9HBM3, Q9HBM4, Q9HBM5, Q9NXF4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM