DPP10_MOUSE
ID DPP10_MOUSE Reviewed; 797 AA.
AC Q6NXK7; Q6P554; Q8K1H0;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Inactive dipeptidyl peptidase 10;
DE AltName: Full=Dipeptidyl peptidase X;
DE Short=DPP X;
GN Name=Dpp10;
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 [MRNA].
RX PubMed=14566338; DOI=10.1038/ng1256;
RA Allen M., Heinzmann A., Noguchi E., Abecasis G., Broxholme J.,
RA Ponting C.P., Bhattacharyya S., Tinsley J., Zhang Y., Holt R., Jones E.Y.,
RA Lench N., Carey A., Jones H., Dickens N.J., Dimon C., Nicholls R.,
RA Baker C., Xue L., Townsend E., Kabesch M., Weiland S.K., Carr D.,
RA von Mutius E., Adcock I.M., Barnes P.J., Lathrop G.M., Edwards M.,
RA Moffatt M.F., Cookson W.O.C.M.;
RT "Positional cloning of a novel gene influencing asthma from chromosome
RT 2q14.";
RL Nat. Genet. 35:258-263(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=15671030; DOI=10.1074/jbc.m410613200;
RA Zagha E., Ozaita A., Chang S.Y., Nadal M.S., Lin U., Saganich M.J.,
RA McCormack T., Akinsanya K.O., Qi S.Y., Rudy B.;
RT "DPP10 modulates Kv4-mediated A-type potassium channels.";
RL J. Biol. Chem. 280:18853-18861(2005).
RN [4]
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 [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 (Probable).
CC {ECO:0000250|UniProtKB:Q8N608, ECO:0000269|PubMed:22311982,
CC ECO:0000305}.
CC -!- SUBUNIT: May form oligomers. Interacts with KCND1 and KCND2 (By
CC similarity). {ECO:0000250|UniProtKB:Q8N608}.
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 (PubMed:22311982). Expressed in the brain, predominantly by neurons and
CC not by glia. {ECO:0000269|PubMed:15671030,
CC ECO:0000269|PubMed:22311982}.
CC -!- PTM: N-glycosylation is important for cell surface expression,
CC specially at Asn-258, which is crucial. {ECO:0000250|UniProtKB:Q8N608}.
CC -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Gly-652 is present instead of the conserved Ser which is
CC expected to be an active site residue suggesting that this protein has
CC no peptidase activity. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH63074.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC029696; AAH29696.1; -; mRNA.
DR EMBL; BC063074; AAH63074.1; ALT_INIT; mRNA.
DR EMBL; BC067026; AAH67026.1; -; mRNA.
DR RefSeq; NP_950186.3; NM_199021.3.
DR AlphaFoldDB; Q6NXK7; -.
DR SMR; Q6NXK7; -.
DR BioGRID; 234607; 4.
DR STRING; 10090.ENSMUSP00000108225; -.
DR ESTHER; mouse-dpp10; DPP4N_Peptidase_S9.
DR MEROPS; S09.974; -.
DR GlyConnect; 2385; 8 N-Linked glycans (5 sites).
DR GlyGen; Q6NXK7; 8 sites, 8 N-linked glycans (5 sites).
DR iPTMnet; Q6NXK7; -.
DR PhosphoSitePlus; Q6NXK7; -.
DR MaxQB; Q6NXK7; -.
DR PaxDb; Q6NXK7; -.
DR PRIDE; Q6NXK7; -.
DR ProteomicsDB; 277599; -.
DR DNASU; 269109; -.
DR GeneID; 269109; -.
DR KEGG; mmu:269109; -.
DR CTD; 57628; -.
DR MGI; MGI:2442409; Dpp10.
DR eggNOG; KOG2100; Eukaryota.
DR InParanoid; Q6NXK7; -.
DR OrthoDB; 269253at2759; -.
DR PhylomeDB; Q6NXK7; -.
DR BioGRID-ORCS; 269109; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Dpp10; mouse.
DR PRO; PR:Q6NXK7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6NXK7; protein.
DR GO; GO:0016020; C:membrane; 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:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IDA:UniProtKB.
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; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..797
FT /note="Inactive dipeptidyl peptidase 10"
FT /id="PRO_0000122418"
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..797
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 139
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8N608"
FT MOD_RES 144
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8N608"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
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 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 797 AA; 90827 MW; 46808DCF364763DE CRC64;
MKQEQQPTPG ARATQSQPAD QELGSNSPPQ RNWKGIAIAL LVILVVCSLI TMSVILLTPD
ELTNSSETRL SLEELLGKGF GLHNPEPRWI NDTVVVYKTN NGHVMKLNTE SNASTLLLDN
STFVTFKASR HSLSPDLKYV LLAYDVKQIF HYSFTASYLI YNIHTGEVWE LNPPEVEDSV
LQYAAWGVQG QQLIYIFENN IYYQPDIKSS SLRLTSSGKE GIIFNGIADW LYEEELLHSH
IAHWWSPDGE RLAFLMINDS LVPNMIIPRF TGALYPKAKQ YPYPKAGQAN PSVKLYVVNL
YGPTHTLELM PPDIFKSREY YITMVKWVSN TRTVVRWLNR PQNISILTLC ESTTGACSRK
YEMTSDTWLS KQNEEPVFSR DGSKFFMTVP VKQGGRGEFH HIAMFLVQSK SEQITVRHLT
SGNWEVIRIL AYDETTQKIY FLSTESSPQG RQLYSASTEG LLNRDCISCN FMKEDCTYFD
ASFSPMNQHF LLFCEGPKVP VVSLHITDNP SRYFLLENNS VMKETIQKKK LAKRETRILH
IDDYELPLQL SFPKDFMEKN QYALLLIMDE EPGGQMVTDK FHVDWDSVLI DTDNVIVARF
DGRGSGFQGL KVLQEIHRRI GSVEAKDQVA AVKYLLKQPY IDSKRLSIFG KGYGGYIASM
ILKSDEKFFK CGAVVAPISD MKLYASAFSE RYLGMPSKEE STYQASSVLH NIHGLKEENL
LIIHGTADTK VHFQHSAELI KHLIKAGVNY TLQVYPDEGY HISDKSKHHF YSTILRFFSD
CLKEEVSVLP QEPEEDE