DPP6_PANTR
ID DPP6_PANTR Reviewed; 803 AA.
AC Q5IS50;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Dipeptidyl aminopeptidase-like protein 6;
DE AltName: Full=Dipeptidyl peptidase 6;
DE AltName: Full=Dipeptidyl peptidase VI;
DE Short=DPP VI;
GN Name=DPP6;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT "Accelerated evolution of nervous system genes in the origin of Homo
RT sapiens.";
RL Cell 119:1027-1040(2004).
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 -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P42658}.
CC -!- SIMILARITY: Belongs to the peptidase S9B family. {ECO:0000305}.
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DR EMBL; AY665278; AAV74316.1; -; mRNA.
DR RefSeq; NP_001029333.1; NM_001034161.1.
DR AlphaFoldDB; Q5IS50; -.
DR SMR; Q5IS50; -.
DR STRING; 9598.ENSPTRP00000058036; -.
DR ESTHER; pantr-dpp6; DPP4N_Peptidase_S9.
DR MEROPS; S09.973; -.
DR PaxDb; Q5IS50; -.
DR GeneID; 463835; -.
DR KEGG; ptr:463835; -.
DR CTD; 1804; -.
DR eggNOG; KOG2100; Eukaryota.
DR InParanoid; Q5IS50; -.
DR OrthoDB; 269253at2759; -.
DR Proteomes; UP000002277; Unplaced.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Membrane; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..803
FT /note="Dipeptidyl aminopeptidase-like protein 6"
FT /id="PRO_0000122411"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..803
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 111
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 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 751
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 349..356
FT /evidence="ECO:0000250"
FT DISULFID 465..468
FT /evidence="ECO:0000250"
FT DISULFID 474..492
FT /evidence="ECO:0000250"
FT DISULFID 673..784
FT /evidence="ECO:0000250"
SQ SEQUENCE 803 AA; 91412 MW; 5048D4A1EDEC0938 CRC64;
MTTAKEPSAS GKSVQQQEQE LVGSNPPQRN WKGIAIALLV ILVICSLIVT SVILLTPAED
NSLSQKKKVT VEDLFSEDFK IHDPEAKWIS DTEFIYREQK GTVRLWNVET NISTVLIEGK
KIESLRAIRY EISPDREYAL FSYNVEPIYQ HSYTGYYVLS KIPHGDPQSL DPPEVSNAKL
QYAGWGPKGQ QLIFIFENNI YYCAHVGKQA IRVVSTGKEG VIYNGLSDWL YEEEILKTHI
AHWWSPDGTR LAYATINDSR VPIMELPTYT GSIYPTVKPY HYPKAGSENP SISLHVIGLN
GPTHDLEMMP PDDPRMREYY ITMVKWATST KVAVTWLNRA QNVSILTLCD ATTGVCTKKH
EDESEAWLHR QNEEPVFSKD GRKFFFIRAI PQGGRGKFYH ITMSLSQPNS SNDNIQSITS
GDWDVTKILA YDEKGNKIYF LSTEDLPRRR QLYSANTVGN FNRQCLSCDL VDNCTYFSAS
FSHSMDFFLL KCEGPGVPMV TVHNTTDKKK MFDLETNEHV KKAINDRQMP KVEYRDIEID
DYNLPMQILK PATFTDTTHY PLLLVVDGTP GSQSVAEKFE VSWETVMVSS HGAVVVKCDG
RGSGFQGTKL LHEVRRRLGL LEEKDQMEAV RTMLKEQYID RTRVAVFGKD YGGYLSTYIL
PAKGENQGQT FTCGSALSPI TDFKLYASAF SERYLGLHGL DNRAYEMTKV AHRVSALEEQ
QFLIIHPTAD EKIHFQHTAE LITQLIRGKA NYSLQIYPDE SHYFTSSSLK QHLYRSIINF
FVECFRIQDK LPTVTAKEDE EED
