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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
 
 
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