DPP10_RAT
ID DPP10_RAT Reviewed; 796 AA.
AC Q6Q629;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Inactive dipeptidyl peptidase 10;
DE AltName: Full=Dipeptidyl peptidase X;
DE Short=DPP X;
DE AltName: Full=Kv4 potassium channel auxiliary subunit;
GN Name=Dpp10;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Ren X., Hayashi Y., Yoshimura N., Takimoto K.;
RT "A DPPX homolog is highly expressed in peripheral neurons and regulates Kv4
RT channel expression and gating.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH KCND2, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KCND2 AND KCNIP3, AND
RP TISSUE SPECIFICITY.
RX PubMed=16123112; DOI=10.1113/jphysiol.2005.087858;
RA Jerng H.H., Kunjilwar K., Pfaffinger P.J.;
RT "Multiprotein assembly of Kv4.2, KChIP3 and DPP10 produces ternary channel
RT complexes with ISA-like properties.";
RL J. Physiol. (Lond.) 568:767-788(2005).
RN [4]
RP FUNCTION.
RX PubMed=19901547; DOI=10.4161/chan.3.6.10216;
RA Jerng H.H., Dougherty K., Covarrubias M., Pfaffinger P.J.;
RT "A novel N-terminal motif of dipeptidyl peptidase-like proteins produces
RT rapid inactivation of KV4.2 channels by a pore-blocking mechanism.";
RL Channels 3:448-461(2009).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-748, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
CC -!- FUNCTION: Promotes cell surface expression of the potassium channel
CC KCND2. Modulates the activity and gating characteristics of the
CC potassium channel KCND2 (PubMed:16123112, PubMed:19901547). Has no
CC dipeptidyl aminopeptidase activity (Probable).
CC {ECO:0000250|UniProtKB:Q8N608, ECO:0000269|PubMed:16123112,
CC ECO:0000269|PubMed:19901547, ECO:0000305}.
CC -!- SUBUNIT: May form oligomers. Interacts with KCND1 (By similarity).
CC Interacts with KCND2 (PubMed:15671030, PubMed:16123112). Identified in
CC a complex with KCND2 and KCNIP3 (PubMed:16123112).
CC {ECO:0000250|UniProtKB:Q8N608, ECO:0000269|PubMed:15671030,
CC ECO:0000269|PubMed:16123112}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16123112};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in brain cortex, hippocampus, thalamus and
CC cerebellum Purkinje cells (at protein level) (PubMed:16123112).
CC {ECO:0000269|PubMed:16123112}.
CC -!- PTM: N-glycosylation is important for cell surface expression,
CC specially at Asn-257, which is crucial. {ECO:0000250|UniProtKB:Q8N608}.
CC -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Gly-651 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}.
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DR EMBL; AY557199; AAS64749.1; -; mRNA.
DR RefSeq; NP_001012205.1; NM_001012205.1.
DR AlphaFoldDB; Q6Q629; -.
DR SMR; Q6Q629; -.
DR CORUM; Q6Q629; -.
DR STRING; 10116.ENSRNOP00000003527; -.
DR ESTHER; ratno-q6q629; DPP4N_Peptidase_S9.
DR MEROPS; S09.974; -.
DR GlyGen; Q6Q629; 7 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q6Q629; -.
DR PaxDb; Q6Q629; -.
DR PRIDE; Q6Q629; -.
DR Ensembl; ENSRNOT00000112799; ENSRNOP00000083925; ENSRNOG00000002595.
DR GeneID; 363972; -.
DR KEGG; rno:363972; -.
DR UCSC; RGD:1306427; rat.
DR CTD; 57628; -.
DR RGD; 1306427; Dpp10.
DR eggNOG; KOG2100; Eukaryota.
DR GeneTree; ENSGT00940000154657; -.
DR InParanoid; Q6Q629; -.
DR PRO; PR:Q6Q629; -.
DR Proteomes; UP000002494; Chromosome 13.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:RGD.
DR GO; GO:0015459; F:potassium channel regulator activity; ISS:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; ISS: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..796
FT /note="Inactive dipeptidyl peptidase 10"
FT /id="PRO_0000122419"
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..796
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..55
FT /note="Mediates effects on KCND2"
FT /evidence="ECO:0000250"
FT MOD_RES 138
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8N608"
FT MOD_RES 143
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8N608"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 748
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
SQ SEQUENCE 796 AA; 90891 MW; E1F20C00D04FA54A CRC64;
MNQTASVSHH IKCQPSKTIK ELGSNSPPQR NWKGIAIALL VILVVCSLIT MSVILLTPDE
LTNSSETRLS LEELLGKGFG LHNPEARWIN DTDVVYKTDN GHVMKLNAET NATTLLLDNS
TFVTFKASRH SLSPDLKYVL LAYDVKQIFH YSFTASYLIY NIHTGEVWEL NPPEVEDSVL
QYAAWGVQGQ QLIYIFENNI YYQPDIKSSS LRLTSSGKEG IVFNGIADWL YEEELLHSHI
AHWWSPDGER LAFLMINDSL VPNMVIPRFT GALYPKAKQY PYPKAGQANP SVKLYVVNLY
GPTHTLELMP PDIFKSREYY ITMVKWVSNT RTVVRWLNRP QNISILTVCE STTGACSRKY
EMTSDTWISK QNEEPVFSRD GSKFFMTVPV KQGGRGEFHH IAMFLVQSKS EQITVRHLTS
GNWEVIRILA YDETTQKIYF LSTEFSPRGR QLYSASTEGL LSRDCISCNF RKEDCTYFDA
SFSPMNQHFL LFCEGPKVPM VSLHSTDNPS NYYILERNSM MKETIQKKKL AKREIRILHI
DDYELPLQLS FPKDFLEKNQ YALLLIIDEE PGGQMVTEKF HVDWDSVLID TDNVIVARFD
GRGSGFQGLK VLQEIHRRTG SVEAKDQIAA IKYLLKQPYI DSKRLSIFGK GYGGYIASMI
LKSDEKFFKC GTVVAPISDM KLYASAFSER YLGMPSKEES TYQASSVLHN IHGLKEENLL
IIHGTADTKV HFQHSAELIK HLIKAGVNYT LQVYPDEGYH ISDKSKHHFY STILRFFSDC
LKEEVSVLPQ EPEEDE
