DPP6_MOUSE
ID DPP6_MOUSE Reviewed; 804 AA.
AC Q9Z218; Q9QWW2; Q9Z219;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Dipeptidyl aminopeptidase-like protein 6;
DE AltName: Full=DPPX;
DE AltName: Full=Dipeptidyl aminopeptidase-related protein;
DE AltName: Full=Dipeptidyl peptidase 6;
DE AltName: Full=Dipeptidyl peptidase IV-like protein;
DE AltName: Full=Dipeptidyl peptidase VI;
DE Short=DPP VI;
GN Name=Dpp6; Synonyms=Dpp-6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=9811881; DOI=10.1073/pnas.95.23.13800;
RA Hough R.B., Lengeling A., Bedian V., Lo C., Bucan M.;
RT "Rump white inversion in the mouse disrupts dipeptidyl aminopeptidase-like
RT protein 6 and causes dysregulation of kit expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:13800-13805(1998).
RN [2]
RP PROTEIN SEQUENCE OF 651-664, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=23832105; DOI=10.1016/j.ejmg.2013.06.008;
RA Liao C., Fu F., Li R., Yang W.Q., Liao H.Y., Yan J.R., Li J., Li S.Y.,
RA Yang X., Li D.Z.;
RT "Loss-of-function variation in the DPP6 gene is associated with autosomal
RT dominant microcephaly and mental retardation.";
RL Eur. J. Med. Genet. 56:484-489(2013).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22311982; DOI=10.1074/jbc.m111.324574;
RA Foeger N.C., Norris A.J., Wren L.M., Nerbonne J.M.;
RT "Augmentation of Kv4.2-encoded currents by accessory dipeptidyl peptidase 6
RT and 10 subunits reflects selective cell surface Kv4.2 protein
RT stabilization.";
RL J. Biol. Chem. 287:9640-9650(2012).
CC -!- FUNCTION: Promotes cell surface expression of the potassium channel
CC KCND2 (PubMed:22311982). Modulates the activity and gating
CC characteristics of the potassium channel KCND2 (PubMed:22311982). Has
CC no dipeptidyl aminopeptidase activity (By similarity).
CC {ECO:0000250|UniProtKB:P42658, ECO:0000269|PubMed:22311982}.
CC -!- SUBUNIT: Homodimer (in vitro). Interacts with KCND2. Identified in a
CC complex with KCND2 and KCNIP2. Forms an octameric complex composed of
CC four DPP6 subunits bound to the KCND2 tetramer.
CC {ECO:0000250|UniProtKB:P42658}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22311982};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in brain cortex (at protein level).
CC {ECO:0000269|PubMed:22311982}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P42658}.
CC -!- DISRUPTION PHENOTYPE: Knockdown animals obtained using siRNA technology
CC have smaller brains than their wild-type littermates. Performance on
CC the standard Morris water maze indicated spatial memory defects and
CC learning disabilities. {ECO:0000269|PubMed:23832105}.
CC -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
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DR EMBL; AF092507; AAC97366.1; -; mRNA.
DR EMBL; AF092506; AAC97365.1; -; mRNA.
DR EMBL; AF092505; AAC98381.1; -; Genomic_DNA.
DR CCDS; CCDS19139.1; -.
DR RefSeq; NP_034205.1; NM_010075.2.
DR RefSeq; NP_997165.2; NM_207282.3.
DR AlphaFoldDB; Q9Z218; -.
DR SMR; Q9Z218; -.
DR BioGRID; 199301; 9.
DR MINT; Q9Z218; -.
DR STRING; 10090.ENSMUSP00000113441; -.
DR ESTHER; mouse-DPP6; DPP4N_Peptidase_S9.
DR MEROPS; S09.973; -.
DR GlyConnect; 2255; 38 N-Linked glycans (6 sites).
DR GlyGen; Q9Z218; 8 sites, 37 N-linked glycans (6 sites).
DR iPTMnet; Q9Z218; -.
DR PhosphoSitePlus; Q9Z218; -.
DR SwissPalm; Q9Z218; -.
DR MaxQB; Q9Z218; -.
DR PaxDb; Q9Z218; -.
DR PRIDE; Q9Z218; -.
DR ProteomicsDB; 279480; -.
DR Antibodypedia; 33071; 241 antibodies from 27 providers.
DR DNASU; 13483; -.
DR Ensembl; ENSMUST00000071500; ENSMUSP00000071435; ENSMUSG00000061576.
DR GeneID; 13483; -.
DR KEGG; mmu:13483; -.
DR UCSC; uc008wtk.2; mouse.
DR CTD; 1804; -.
DR MGI; MGI:94921; Dpp6.
DR VEuPathDB; HostDB:ENSMUSG00000061576; -.
DR eggNOG; KOG2100; Eukaryota.
DR GeneTree; ENSGT00940000156280; -.
DR InParanoid; Q9Z218; -.
DR OMA; MYGERYM; -.
DR OrthoDB; 269253at2759; -.
DR PhylomeDB; Q9Z218; -.
DR BioGRID-ORCS; 13483; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Dpp6; mouse.
DR PRO; PR:Q9Z218; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9Z218; protein.
DR Bgee; ENSMUSG00000061576; Expressed in dentate gyrus of hippocampal formation granule cell and 151 other tissues.
DR ExpressionAtlas; Q9Z218; baseline and differential.
DR Genevisible; Q9Z218; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
DR GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0019228; P:neuronal action potential; IMP:MGI.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IMP:MGI.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IMP:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0043266; P:regulation of potassium ion transport; IMP:MGI.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..804
FT /note="Dipeptidyl aminopeptidase-like protein 6"
FT /id="PRO_0000122410"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..804
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 474
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 752
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 350..357
FT /evidence="ECO:0000250"
FT DISULFID 466..469
FT /evidence="ECO:0000250"
FT DISULFID 475..493
FT /evidence="ECO:0000250"
FT DISULFID 674..785
FT /evidence="ECO:0000250"
FT CONFLICT 440..455
FT /note="Missing (in Ref. 1; AAC98381)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="Q -> P (in Ref. 1; AAC97365)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 804 AA; 91260 MW; 09CFCE7AAD8A7168 CRC64;
MNQTAGASNN VRCPPGKGHK ELVGSNPPQR NWKGIAIALL VILVICSLIV TSVILLTPAE
DTSLSQKKKV TVEDLFSEDF KIHDPEAKWI SNKEFIYRER KGSVILRNVE TNNSTVLIEG
KKIESLRAIR YEISPDKEYV LFSYNVEPVY QHSHTGYYVL SKIPHGDPQS LDPPEVSNAK
LQYAGWGPKG QQLIFIFENN IYYCAHVGKQ AIRVVSTGKE GVIYNGLSDW LYEEEILKSH
IAHWWSPDGT RLAYATINDS RVPLMELPTY TGSVYPTVKP YHYPKAGSEN PSISLHVIGL
NGPTHDLEMM PPDDPRMREY YITMVKWATS TKVAVTWLNR AQNVSILTLC DATTGVCTKK
HEDESEAWLH RQNEEPVFSK DGRKFFFVRA IPQGGRGKFY HITVSSSQPN SSNDNIQSIT
SGDWDVTKIL SYDEKRNKIY FLSTEDLPRR RHLYSANTVD DFNRQCLSCD LVENCTYVSA
SFSHNMDFFL LKCEGPGVPT VTVHNTTDKR RMFDLEANEE VQKAINDRQM PKIEYRKIEV
EDYSLPMQIL KPATFTDTAH YPLLLVVDGT PGSQSVTERF EVTWETVLVS SHGAVVVKCD
GRGSGFQGTK LLQEVRRRLG FLEEKDQMEA VRTMLKEQYI DKTRVAVFGK DYGGYLSTYI
LPAKGENQGQ TFTCGSALSP ITDFKLYASA FSERYLGLHG LDNRAYEMTK LAHRVSALED
QQFLIIHATA DEKIHFQHTA ELITQLIKGK ANYSLQIYPD ESHYFHSVAL KQHLSRSIIG
FFVECFRVQD KLPTATAKEE EEED
