DPP6_BOVIN
ID DPP6_BOVIN Reviewed; 863 AA.
AC P42659;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 121.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS DPPX-L AND DPPX-S), PARTIAL PROTEIN
RP SEQUENCE, AND TISSUE 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).
CC -!- FUNCTION: Promotes cell surface expression of the potassium channel
CC KCND2. Modulates the activity and gating characteristics of the
CC potassium channel KCND2. Has no dipeptidyl aminopeptidase activity.
CC {ECO:0000250|UniProtKB:P42658}.
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:0000250|UniProtKB:P42658};
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=P42659-1; Sequence=Displayed;
CC Name=DPPX-S;
CC IsoId=P42659-2; Sequence=VSP_005364;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the brain. Isoform DPPX-
CC L is expressed exclusively in the brain whereas isoform DPPX-S is found
CC in brain, kidney, ovary and testis. {ECO:0000269|PubMed:1729689}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P42658}.
CC -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
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DR EMBL; M76428; AAC41622.1; -; mRNA.
DR EMBL; M76429; AAC41623.1; -; mRNA.
DR PIR; A41793; A41793.
DR PIR; B41793; B41793.
DR RefSeq; NP_776465.1; NM_174040.2. [P42659-1]
DR AlphaFoldDB; P42659; -.
DR SMR; P42659; -.
DR STRING; 9913.ENSBTAP00000029251; -.
DR ESTHER; bovin-dpp6; DPP4N_Peptidase_S9.
DR MEROPS; S09.973; -.
DR PaxDb; P42659; -.
DR PRIDE; P42659; -.
DR Ensembl; ENSBTAT00000029251; ENSBTAP00000029251; ENSBTAG00000021941. [P42659-1]
DR Ensembl; ENSBTAT00000043677; ENSBTAP00000041231; ENSBTAG00000021941. [P42659-2]
DR GeneID; 281123; -.
DR KEGG; bta:281123; -.
DR CTD; 1804; -.
DR VEuPathDB; HostDB:ENSBTAG00000021941; -.
DR eggNOG; KOG2100; Eukaryota.
DR GeneTree; ENSGT00940000156280; -.
DR InParanoid; P42659; -.
DR OMA; MYGERYM; -.
DR OrthoDB; 269253at2759; -.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000021941; Expressed in floor plate of diencephalon and 66 other tissues.
DR ExpressionAtlas; P42659; baseline.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
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: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 Alternative splicing; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..863
FT /note="Dipeptidyl aminopeptidase-like protein 6"
FT /id="PRO_0000122408"
FT TOPO_DOM 1..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..863
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..86
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 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 811
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 409..416
FT /evidence="ECO:0000250"
FT DISULFID 525..528
FT /evidence="ECO:0000250"
FT DISULFID 534..552
FT /evidence="ECO:0000250"
FT DISULFID 733..844
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..79
FT /note="MASLYQRFTGKINTSRSFPAPPEASRLLGGQGPEEDGAGPKPLGAQAPAAAP
FT RERGGGGGAGGRPRFQYQARSDCDDED -> MTTAKEPNASGKSVQQQEQ (in
FT isoform DPPX-S)"
FT /evidence="ECO:0000303|PubMed:1729689"
FT /id="VSP_005364"
SQ SEQUENCE 863 AA; 96557 MW; 23DBA792B841A39D CRC64;
MASLYQRFTG KINTSRSFPA PPEASRLLGG QGPEEDGAGP KPLGAQAPAA APRERGGGGG
AGGRPRFQYQ ARSDCDDEDE LVGSNPPQRN WKGIAIALLV ILVICSLIVT SVILLTPAED
NSLSQKKKVT VEDLFSEDFK IHDPEAKWIS DKEFIYREQK GSVILRNVET NTSTVLIEGK
KIESLRAIRY EISPDREYAL FSYNVEPIYQ HSYTGYYVLS KIPHGDPQSL DPPEVSNAKL
QYAGWGPKGQ QLIFIFENNI YYCAHVGKQA IRVVSTGKEG VIYNGLSDWL YEEEILKTHI
AHWWSPDGTR LAYATINDSR VPVMELPTYT GSVYPTAKPY HYPKAGCENP SISLHVIGLN
GPTHDLEMTP PDDPRMREYY ITMVKWATST KVAVNWLSRA QNVSILTLCD ATTGVCTKKH
EDESEAWLHR QNEEPVFSKD GRKFFFVRAI PQGGQGKFYH ITVSSSQPNS SNDNIQSITS
GDWDVTKILS YDEKRSQIYF LSTEDLPRRR QLYSASTVGS FNRQCLSCDL VDNCTYFSAS
FSPGADFFLL KCEGPGVPTV SVHNTTDKKK MFDLETNEHV QKAISDRQMP KVEYRKIETD
DYNLPIQILK PATFTDTAHY PLLLVVDGTP GSQSVAEKFA VTWETVMVSS HGAVVVKCDG
RGSGFQGTRL LHEVRRRLGS LEEKDQMEAV RVMLKEPYID KTRVAVFGKD YGGYLSTYLL
PAKGDGQAPV FSCGSALSPI TDFKLYASAF SERYLGLHGL DNRAYEMAKV AHRVSALEGQ
QFLVIHATAD EKIHFQHTAE LITQLIKGKA NYSLQIYPDE SHYFSSAALQ QHLHRSILGF
FVECFRIQDK LPAVTAREDE EED
