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Protein

Inactive dipeptidyl peptidase 10

Gene

Dpp10

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Promotes cell surface expression of the potassium channel KCND2. Modulates the activity and gating characteristics of the potassium channel KCND2 (PubMed:16123112, PubMed:19901547). Has no dipeptidyl aminopeptidase activity (Probable).By similarityCurated2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Protein family/group databases

ESTHERiratno-q6q629. DPP4N_Peptidase_S9.
MEROPSiS09.974.

Names & Taxonomyi

Protein namesi
Recommended name:
Inactive dipeptidyl peptidase 10
Alternative name(s):
Dipeptidyl peptidase X
Short name:
DPP X
Kv4 potassium channel auxiliary subunit
Gene namesi
Name:Dpp10
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi1306427. Dpp10.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3434CytoplasmicSequence analysisAdd
BLAST
Transmembranei35 – 5521Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini56 – 796741ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: RGD
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 796796Inactive dipeptidyl peptidase 10PRO_0000122419Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi63 – 631N-linked (GlcNAc...)Sequence analysis
Glycosylationi90 – 901N-linked (GlcNAc...)Sequence analysis
Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence analysis
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence analysis
Modified residuei138 – 1381PhosphotyrosineBy similarity
Modified residuei143 – 1431PhosphotyrosineBy similarity
Glycosylationi257 – 2571N-linked (GlcNAc...)Sequence analysis
Glycosylationi342 – 3421N-linked (GlcNAc...)Sequence analysis
Glycosylationi748 – 7481N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylation is important for cell surface expression, specially at Asn-257, which is crucial.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ6Q629.
PRIDEiQ6Q629.

PTM databases

UniCarbKBiQ6Q629.

Expressioni

Tissue specificityi

Detected in brain cortex, hippocampus, thalamus and cerebellum Purkinje cells (at protein level) (PubMed:16123112).1 Publication

Interactioni

Subunit structurei

May form oligomers. Interacts with KCND1 (By similarity). Interacts with KCND2 (PubMed:15671030, PubMed:16123112). Identified in a complex with KCND2 and KCNIP3 (PubMed:16123112).By similarity2 Publications

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003527.

Structurei

3D structure databases

ProteinModelPortaliQ6Q629.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 5555Mediates effects on KCND2By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S9B family. DPPIV subfamily.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2100. Eukaryota.
COG1506. LUCA.
HOVERGENiHBG105877.
InParanoidiQ6Q629.

Family and domain databases

Gene3Di2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B_N.
[Graphical view]
PfamiPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6Q629-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNQTASVSHH IKCQPSKTIK ELGSNSPPQR NWKGIAIALL VILVVCSLIT
60 70 80 90 100
MSVILLTPDE LTNSSETRLS LEELLGKGFG LHNPEARWIN DTDVVYKTDN
110 120 130 140 150
GHVMKLNAET NATTLLLDNS TFVTFKASRH SLSPDLKYVL LAYDVKQIFH
160 170 180 190 200
YSFTASYLIY NIHTGEVWEL NPPEVEDSVL QYAAWGVQGQ QLIYIFENNI
210 220 230 240 250
YYQPDIKSSS LRLTSSGKEG IVFNGIADWL YEEELLHSHI AHWWSPDGER
260 270 280 290 300
LAFLMINDSL VPNMVIPRFT GALYPKAKQY PYPKAGQANP SVKLYVVNLY
310 320 330 340 350
GPTHTLELMP PDIFKSREYY ITMVKWVSNT RTVVRWLNRP QNISILTVCE
360 370 380 390 400
STTGACSRKY EMTSDTWISK QNEEPVFSRD GSKFFMTVPV KQGGRGEFHH
410 420 430 440 450
IAMFLVQSKS EQITVRHLTS GNWEVIRILA YDETTQKIYF LSTEFSPRGR
460 470 480 490 500
QLYSASTEGL LSRDCISCNF RKEDCTYFDA SFSPMNQHFL LFCEGPKVPM
510 520 530 540 550
VSLHSTDNPS NYYILERNSM MKETIQKKKL AKREIRILHI DDYELPLQLS
560 570 580 590 600
FPKDFLEKNQ YALLLIIDEE PGGQMVTEKF HVDWDSVLID TDNVIVARFD
610 620 630 640 650
GRGSGFQGLK VLQEIHRRTG SVEAKDQIAA IKYLLKQPYI DSKRLSIFGK
660 670 680 690 700
GYGGYIASMI LKSDEKFFKC GTVVAPISDM KLYASAFSER YLGMPSKEES
710 720 730 740 750
TYQASSVLHN IHGLKEENLL IIHGTADTKV HFQHSAELIK HLIKAGVNYT
760 770 780 790
LQVYPDEGYH ISDKSKHHFY STILRFFSDC LKEEVSVLPQ EPEEDE
Length:796
Mass (Da):90,891
Last modified:July 5, 2004 - v1
Checksum:iE1F20C00D04FA54A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY557199 mRNA. Translation: AAS64749.1.
RefSeqiNP_001012205.1. NM_001012205.1.
UniGeneiRn.59993.

Genome annotation databases

GeneIDi363972.
KEGGirno:363972.
UCSCiRGD:1306427. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY557199 mRNA. Translation: AAS64749.1.
RefSeqiNP_001012205.1. NM_001012205.1.
UniGeneiRn.59993.

3D structure databases

ProteinModelPortaliQ6Q629.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003527.

Protein family/group databases

ESTHERiratno-q6q629. DPP4N_Peptidase_S9.
MEROPSiS09.974.

PTM databases

UniCarbKBiQ6Q629.

Proteomic databases

PaxDbiQ6Q629.
PRIDEiQ6Q629.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi363972.
KEGGirno:363972.
UCSCiRGD:1306427. rat.

Organism-specific databases

CTDi57628.
RGDi1306427. Dpp10.

Phylogenomic databases

eggNOGiKOG2100. Eukaryota.
COG1506. LUCA.
HOVERGENiHBG105877.
InParanoidiQ6Q629.

Miscellaneous databases

NextBioi684570.
PROiQ6Q629.

Family and domain databases

Gene3Di2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B_N.
[Graphical view]
PfamiPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "A DPPX homolog is highly expressed in peripheral neurons and regulates Kv4 channel expression and gating."
    Ren X., Hayashi Y., Yoshimura N., Takimoto K.
    Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
  2. Cited for: INTERACTION WITH KCND2, IDENTIFICATION BY MASS SPECTROMETRY.
  3. "Multiprotein assembly of Kv4.2, KChIP3 and DPP10 produces ternary channel complexes with ISA-like properties."
    Jerng H.H., Kunjilwar K., Pfaffinger P.J.
    J. Physiol. (Lond.) 568:767-788(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KCND2 AND KCNIP3, TISSUE SPECIFICITY.
  4. "A novel N-terminal motif of dipeptidyl peptidase-like proteins produces rapid inactivation of KV4.2 channels by a pore-blocking mechanism."
    Jerng H.H., Dougherty K., Covarrubias M., Pfaffinger P.J.
    Channels 3:448-461(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiDPP10_RAT
AccessioniPrimary (citable) accession number: Q6Q629
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: March 16, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Gly-651 is present instead of the conserved Ser which is expected to be an active site residue suggesting that this protein has no peptidase activity.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.