DPP6_RAT
ID DPP6_RAT Reviewed; 859 AA.
AC P46101;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 143.
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;
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] (ISOFORMS DPPX-L AND DPPX-S), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=1729689; DOI=10.1073/pnas.89.1.197;
RA Wada K., Yokotani N., Hunter C., Doi K., Wenthold R.J., Shimasaki S.;
RT "Differential expression of two distinct forms of mRNA encoding members of
RT a dipeptidyl aminopeptidase family.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:197-201(1992).
RN [2]
RP FUNCTION, INTERACTION WITH KCND2, AND SUBCELLULAR LOCATION.
RX PubMed=12575952; DOI=10.1016/s0896-6273(02)01185-6;
RA Nadal M.S., Ozaita A., Amarillo Y., Vega-Saenz de Miera E., Ma Y., Mo W.,
RA Goldberg E.M., Misumi Y., Ikehara Y., Neubert T.A., Rudy B.;
RT "The CD26-related dipeptidyl aminopeptidase-like protein DPPX is a critical
RT component of neuronal A-type K+ channels.";
RL Neuron 37:449-461(2003).
RN [3]
RP FUNCTION, AND 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 FUNCTION.
RX PubMed=19279261; DOI=10.1523/jneurosci.4767-08.2009;
RA Kaulin Y.A., De Santiago-Castillo J.A., Rocha C.A., Nadal M.S., Rudy B.,
RA Covarrubias M.;
RT "The dipeptidyl-peptidase-like protein DPP6 determines the unitary
RT conductance of neuronal Kv4.2 channels.";
RL J. Neurosci. 29:3242-3251(2009).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-167; ASN-313; ASN-560 AND
RP ASN-807, AND IDENTIFICATION BY MASS 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 (PubMed:12575952). Modulates the activity and gating
CC characteristics of the potassium channel KCND2 (PubMed:12575952,
CC PubMed:16123112, PubMed:19279261, PubMed:19901547). Has no dipeptidyl
CC aminopeptidase activity (By similarity). {ECO:0000250|UniProtKB:P42658,
CC ECO:0000269|PubMed:12575952, ECO:0000269|PubMed:16123112,
CC ECO:0000269|PubMed:19279261, ECO:0000269|PubMed:19901547}.
CC -!- SUBUNIT: Homodimer (in vitro) (By similarity). Interacts with KCND2
CC (PubMed:12575952). Identified in a complex with KCND2 and KCNIP2. Forms
CC an octameric complex composed of four DPP6 subunits bound to the KCND2
CC tetramer. {ECO:0000250|UniProtKB:P42658, ECO:0000269|PubMed:12575952}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12575952};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:P42658}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=DPPX-L;
CC IsoId=P46101-1; Sequence=Displayed;
CC Name=DPPX-S;
CC IsoId=P46101-2; Sequence=VSP_005366;
CC -!- TISSUE SPECIFICITY: Detected in brain cortex, hippocampus, thalamus and
CC cerebellum granule cells (at protein level) (PubMed:16123112). Isoform
CC DPPX-S is expressed in brain and some peripheral tissues including
CC kidney, ovary, and testis; in contrast isoform DPPX-L is expressed
CC almost exclusively in brain. {ECO:0000269|PubMed:16123112,
CC ECO:0000269|PubMed:1729689}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P42658}.
CC -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M76426; AAC42061.1; -; mRNA.
DR EMBL; M76427; AAC42062.1; -; mRNA.
DR RefSeq; NP_074041.1; NM_022850.1. [P46101-1]
DR AlphaFoldDB; P46101; -.
DR SMR; P46101; -.
DR BioGRID; 247943; 1.
DR CORUM; P46101; -.
DR STRING; 10116.ENSRNOP00000043113; -.
DR ESTHER; ratno-dpp6; DPP4N_Peptidase_S9.
DR MEROPS; S09.973; -.
DR GlyGen; P46101; 8 sites, 16 N-linked glycans (4 sites).
DR iPTMnet; P46101; -.
DR PhosphoSitePlus; P46101; -.
DR PaxDb; P46101; -.
DR PRIDE; P46101; -.
DR GeneID; 29272; -.
DR KEGG; rno:29272; -.
DR CTD; 1804; -.
DR RGD; 68402; Dpp6.
DR eggNOG; KOG2100; Eukaryota.
DR InParanoid; P46101; -.
DR OrthoDB; 269253at2759; -.
DR PhylomeDB; P46101; -.
DR PRO; PR:P46101; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA: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:0019228; P:neuronal action potential; ISO:RGD.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; ISO:RGD.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; IMP:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:CACAO.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0043266; P:regulation of potassium ion transport; ISO:RGD.
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 Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Membrane; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..859
FT /note="Dipeptidyl aminopeptidase-like protein 6"
FT /id="PRO_0000122412"
FT TOPO_DOM 1..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..859
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 807
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT DISULFID 405..412
FT /evidence="ECO:0000250"
FT DISULFID 521..524
FT /evidence="ECO:0000250"
FT DISULFID 530..548
FT /evidence="ECO:0000250"
FT DISULFID 729..840
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..75
FT /note="MASLYQRFTGKINTSRSFPAPPEASHLLGGQGPEEDAGSKPLGPQAQAVAPR
FT ERGGAGGRPRFQYQARSDCDEED -> MTTAKEPSASGKSVQQQDQ (in isoform
FT DPPX-S)"
FT /evidence="ECO:0000303|PubMed:1729689"
FT /id="VSP_005366"
SQ SEQUENCE 859 AA; 97302 MW; CE26856D26ED126B CRC64;
MASLYQRFTG KINTSRSFPA PPEASHLLGG QGPEEDAGSK PLGPQAQAVA PRERGGAGGR
PRFQYQARSD CDEEDELVGS NPPQRNWKGI AIALLVILVI CSLIVTSVIL LTPAEDTSLS
QKKKVTVEDL FSEDFKIHDP EAKWISDKEF IYRERKGSVI LRNVETNNST VLIEGKKIES
LRAIRYEISP DKEYALFSYN VEPVYQHSHT GYYVLSKIPH GDPQSLDPPE VSNAKLQYAG
WGPKGQQLIF IFENNIYYCA HVGKQAIRVV STGKEGVIYN GLSDWLYEEE ILKSHIAHWW
SPDGTRLAYA TINDSRVPLM ELPTYTGSVY PTVKPYHYPK AGSENPSISL HVIGLNGPTH
DLEMMPPDDP RMREYYITMV KWATSTKVAV TWLNRAQNVS ILTLCDATTG VCTKKHEDES
EAWLHRQNEE PVFSKDGRKF FFVRAIPQGG RGKFYHITVS SSQPNSSNDN IQSITSGDWD
VTEILTYDEK RNKLYFLSTE DLPRRRHLYS ANTVDDFNRQ CLSCDLVENC TYVSASFSHN
MDFFLLKCEG PGVPTVTVHN TTDKRRMFDL EANEQVQKAI YDRQMPKIEY RKIEVEDYSL
PMQILKPATF TDTAHYPLLL VVDGTPGSQS VSERFEVTWE TVLVSSHGAV VVKCDGRGSG
FQGTKLLHEV RRRLGFLEEK DQMEAVRTML KEQYIDKTRV AVFGKDYGGY LSTYILPAKG
ENQGQTFTCG SALSPITDFK LYASAFSERY LGLHGLDNRA YEMTKLAHRV SALEDQQFLI
IHATADEKIH FQHTAELITQ LIKGKANYSL QIYPDESHYF HSVALKQHLY RSIIGFFVEC
FRIQDKLPTA TAKEDEEED
