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Protein

Dipeptidyl aminopeptidase-like protein 6

Gene

Dpp6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Promotes cell surface expression of the potassium channel KCND2 (PubMed:22311982). Modulates the activity and gating characteristics of the potassium channel KCND2 (PubMed:22311982). Has no dipeptidyl aminopeptidase activity (By similarity).By similarity1 Publication

GO - Molecular functioni

  • potassium channel regulator activity Source: UniProtKB
  • serine-type peptidase activity Source: InterPro

GO - Biological processi

  • neuronal action potential Source: MGI
  • positive regulation of potassium ion transmembrane transport Source: MGI
  • protein localization to plasma membrane Source: UniProtKB
  • regulation of membrane potential Source: MGI
  • regulation of potassium ion transmembrane transport Source: UniProtKB
  • regulation of potassium ion transport Source: MGI
Complete GO annotation...

Protein family/group databases

ESTHERimouse-DPP6. DPP4N_Peptidase_S9.
MEROPSiS09.973.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidyl aminopeptidase-like protein 6
Alternative name(s):
DPPX
Dipeptidyl aminopeptidase-related protein
Dipeptidyl peptidase 6
Dipeptidyl peptidase IV-like protein
Dipeptidyl peptidase VI
Short name:
DPP VI
Gene namesi
Name:Dpp6
Synonyms:Dpp-6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:94921. Dpp6.

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 – 804749ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • integral component of membrane Source: MGI
  • membrane Source: MGI
  • plasma membrane Source: UniProtKB
  • voltage-gated potassium channel complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Knockdown animals obtained using siRNA technology have smaller brains than their wild-type littermates. Performance on the standard Morris water maze indicated spatial memory defects and learning disabilities.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 804804Dipeptidyl aminopeptidase-like protein 6PRO_0000122410Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi112 – 1121N-linked (GlcNAc...)Sequence analysis
Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence analysis
Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence analysis
Glycosylationi343 – 3431N-linked (GlcNAc...)Sequence analysis
Disulfide bondi350 ↔ 357By similarity
Glycosylationi410 – 4101N-linked (GlcNAc...)Sequence analysis
Disulfide bondi466 ↔ 469By similarity
Glycosylationi474 – 4741N-linked (GlcNAc...)Sequence analysis
Disulfide bondi475 ↔ 493By similarity
Glycosylationi505 – 5051N-linked (GlcNAc...)Sequence analysis
Disulfide bondi674 ↔ 785By similarity
Glycosylationi752 – 7521N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9Z218.
PaxDbiQ9Z218.
PRIDEiQ9Z218.

PTM databases

iPTMnetiQ9Z218.
PhosphoSiteiQ9Z218.
SwissPalmiQ9Z218.

Expressioni

Tissue specificityi

Detected in brain cortex (at protein level).1 Publication

Gene expression databases

BgeeiQ9Z218.
CleanExiMM_DPP6.
ExpressionAtlasiQ9Z218. baseline and differential.
GenevisibleiQ9Z218. MM.

Interactioni

Subunit structurei

Homodimer (in vitro). Interacts with KCND2. Identified in a complex with KCND2 and KCNIP2. Forms an octomeric complex composed of four DPP6 subunits bound to the KCND2 tetramer.By similarity

Protein-protein interaction databases

BioGridi199301. 4 interactions.
IntActiQ9Z218. 2 interactions.
MINTiMINT-1177199.
STRINGi10090.ENSMUSP00000113441.

Structurei

3D structure databases

ProteinModelPortaliQ9Z218.
SMRiQ9Z218. Positions 66-788.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9B family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2100. Eukaryota.
COG1506. LUCA.
GeneTreeiENSGT00760000119233.
HOGENOMiHOG000231875.
HOVERGENiHBG105877.
InParanoidiQ9Z218.
OrthoDBiEOG7H791M.
PhylomeDBiQ9Z218.

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.

Q9Z218-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNQTAGASNN VRCPPGKGHK ELVGSNPPQR NWKGIAIALL VILVICSLIV
60 70 80 90 100
TSVILLTPAE DTSLSQKKKV TVEDLFSEDF KIHDPEAKWI SNKEFIYRER
110 120 130 140 150
KGSVILRNVE TNNSTVLIEG KKIESLRAIR YEISPDKEYV LFSYNVEPVY
160 170 180 190 200
QHSHTGYYVL SKIPHGDPQS LDPPEVSNAK LQYAGWGPKG QQLIFIFENN
210 220 230 240 250
IYYCAHVGKQ AIRVVSTGKE GVIYNGLSDW LYEEEILKSH IAHWWSPDGT
260 270 280 290 300
RLAYATINDS RVPLMELPTY TGSVYPTVKP YHYPKAGSEN PSISLHVIGL
310 320 330 340 350
NGPTHDLEMM PPDDPRMREY YITMVKWATS TKVAVTWLNR AQNVSILTLC
360 370 380 390 400
DATTGVCTKK HEDESEAWLH RQNEEPVFSK DGRKFFFVRA IPQGGRGKFY
410 420 430 440 450
HITVSSSQPN SSNDNIQSIT SGDWDVTKIL SYDEKRNKIY FLSTEDLPRR
460 470 480 490 500
RHLYSANTVD DFNRQCLSCD LVENCTYVSA SFSHNMDFFL LKCEGPGVPT
510 520 530 540 550
VTVHNTTDKR RMFDLEANEE VQKAINDRQM PKIEYRKIEV EDYSLPMQIL
560 570 580 590 600
KPATFTDTAH YPLLLVVDGT PGSQSVTERF EVTWETVLVS SHGAVVVKCD
610 620 630 640 650
GRGSGFQGTK LLQEVRRRLG FLEEKDQMEA VRTMLKEQYI DKTRVAVFGK
660 670 680 690 700
DYGGYLSTYI LPAKGENQGQ TFTCGSALSP ITDFKLYASA FSERYLGLHG
710 720 730 740 750
LDNRAYEMTK LAHRVSALED QQFLIIHATA DEKIHFQHTA ELITQLIKGK
760 770 780 790 800
ANYSLQIYPD ESHYFHSVAL KQHLSRSIIG FFVECFRVQD KLPTATAKEE

EEED
Length:804
Mass (Da):91,260
Last modified:May 1, 1999 - v1
Checksum:i09CFCE7AAD8A7168
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti440 – 45516Missing in AAC98381 (PubMed:9811881).CuratedAdd
BLAST
Sequence conflicti638 – 6381Q → P in AAC97365 (PubMed:9811881).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF092507 mRNA. Translation: AAC97366.1.
AF092506 mRNA. Translation: AAC97365.1.
AF092505 Genomic DNA. Translation: AAC98381.1.
CCDSiCCDS19139.1.
RefSeqiNP_034205.1. NM_010075.2.
NP_997165.2. NM_207282.3.
UniGeneiMm.42078.

Genome annotation databases

EnsembliENSMUST00000071500; ENSMUSP00000071435; ENSMUSG00000061576.
GeneIDi13483.
KEGGimmu:13483.
UCSCiuc008wtk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF092507 mRNA. Translation: AAC97366.1.
AF092506 mRNA. Translation: AAC97365.1.
AF092505 Genomic DNA. Translation: AAC98381.1.
CCDSiCCDS19139.1.
RefSeqiNP_034205.1. NM_010075.2.
NP_997165.2. NM_207282.3.
UniGeneiMm.42078.

3D structure databases

ProteinModelPortaliQ9Z218.
SMRiQ9Z218. Positions 66-788.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199301. 4 interactions.
IntActiQ9Z218. 2 interactions.
MINTiMINT-1177199.
STRINGi10090.ENSMUSP00000113441.

Protein family/group databases

ESTHERimouse-DPP6. DPP4N_Peptidase_S9.
MEROPSiS09.973.

PTM databases

iPTMnetiQ9Z218.
PhosphoSiteiQ9Z218.
SwissPalmiQ9Z218.

Proteomic databases

MaxQBiQ9Z218.
PaxDbiQ9Z218.
PRIDEiQ9Z218.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000071500; ENSMUSP00000071435; ENSMUSG00000061576.
GeneIDi13483.
KEGGimmu:13483.
UCSCiuc008wtk.2. mouse.

Organism-specific databases

CTDi1804.
MGIiMGI:94921. Dpp6.

Phylogenomic databases

eggNOGiKOG2100. Eukaryota.
COG1506. LUCA.
GeneTreeiENSGT00760000119233.
HOGENOMiHOG000231875.
HOVERGENiHBG105877.
InParanoidiQ9Z218.
OrthoDBiEOG7H791M.
PhylomeDBiQ9Z218.

Miscellaneous databases

ChiTaRSiDpp6. mouse.
NextBioi283983.
PROiQ9Z218.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z218.
CleanExiMM_DPP6.
ExpressionAtlasiQ9Z218. baseline and differential.
GenevisibleiQ9Z218. MM.

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

« Hide 'large scale' publications
  1. "Rump white inversion in the mouse disrupts dipeptidyl aminopeptidase-like protein 6 and causes dysregulation of kit expression."
    Hough R.B., Lengeling A., Bedian V., Lo C., Bucan M.
    Proc. Natl. Acad. Sci. U.S.A. 95:13800-13805(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.
  2. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 651-664, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  4. "Loss-of-function variation in the DPP6 gene is associated with autosomal dominant microcephaly and mental retardation."
    Liao C., Fu F., Li R., Yang W.Q., Liao H.Y., Yan J.R., Li J., Li S.Y., Yang X., Li D.Z.
    Eur. J. Med. Genet. 56:484-489(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  5. "Augmentation of Kv4.2-encoded currents by accessory dipeptidyl peptidase 6 and 10 subunits reflects selective cell surface Kv4.2 protein stabilization."
    Foeger N.C., Norris A.J., Wren L.M., Nerbonne J.M.
    J. Biol. Chem. 287:9640-9650(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiDPP6_MOUSE
AccessioniPrimary (citable) accession number: Q9Z218
Secondary accession number(s): Q9QWW2, Q9Z219
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: May 1, 1999
Last modified: May 11, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.