DPP10_HUMAN
ID DPP10_HUMAN Reviewed; 796 AA.
AC Q8N608; A8K1Q2; J3KPP2; J3KQ46; Q0GLB8; Q53QT3; Q53S86; Q53SL8; Q53SS4;
AC Q6TTV4; Q86YR9; Q9P236;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Inactive dipeptidyl peptidase 10;
DE AltName: Full=Dipeptidyl peptidase IV-related protein 3;
DE Short=DPRP-3;
DE AltName: Full=Dipeptidyl peptidase X;
DE Short=DPP X;
DE AltName: Full=Dipeptidyl peptidase-like protein 2;
DE Short=DPL2;
GN Name=DPP10; Synonyms=DPRP3, KIAA1492;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS PRO-340 AND ILE-401.
RC TISSUE=Brain;
RX PubMed=12675227; DOI=10.1007/0-306-47920-6_10;
RA Chen T., Ajami K., McCaughan G.W., Gorrell M.D., Abbott C.A.;
RT "Dipeptidyl peptidase IV gene family. The DPIV family.";
RL Adv. Exp. Med. Biol. 524:79-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, LACK
RP OF ENZYME ACTIVITY, AND VARIANT ILE-401.
RC TISSUE=Hypothalamus;
RX PubMed=12662155; DOI=10.1042/bj20021914;
RA Qi S.Y., Riviere P.J., Trojnar J., Junien J.-L., Akinsanya K.O.;
RT "Cloning and characterization of dipeptidyl peptidase 10, a new member of
RT an emerging subgroup of serine proteases.";
RL Biochem. J. 373:179-189(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, SUBUNIT,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INVOLVEMENT IN ASTHMA, AND
RP VARIANT ILE-401.
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANT ILE-401, AND ALTERNATIVE
RP SPLICING.
RX PubMed=16899223; DOI=10.1016/j.bbrc.2006.07.157;
RA Takimoto K., Hayashi Y., Ren X., Yoshimura N.;
RT "Species and tissue differences in the expression of DPPY splicing
RT variants.";
RL Biochem. Biophys. Res. Commun. 348:1094-1100(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS PRO-340
RP AND ILE-401.
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-401.
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-401.
RC TISSUE=Brain;
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 [9]
RP FUNCTION, GLYCOSYLATION, AND INTERACTION WITH KCND1 AND KCND2.
RX PubMed=15454437; DOI=10.1529/biophysj.104.042358;
RA Jerng H.H., Qian Y., Pfaffinger P.J.;
RT "Modulation of Kv4.2 channel expression and gating by dipeptidyl peptidase
RT 10 (DPP10).";
RL Biophys. J. 87:2380-2396(2004).
RN [10]
RP FUNCTION.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-138 AND TYR-143, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP INVOLVEMENT IN SUSCEPTIBILITY TO ASTHMA.
RX PubMed=19237393; DOI=10.1136/thx.2008.102053;
RA Blakey J.D., Sayers I., Ring S.M., Strachan D.P., Hall I.P.;
RT "Positionally cloned asthma susceptibility gene polymorphisms and disease
RT risk in the British 1958 Birth Cohort.";
RL Thorax 64:381-387(2009).
RN [13]
RP GLYCOSYLATION AT ASN-90; ASN-111; ASN-119; ASN-257; ASN-342 AND ASN-748,
RP AND MUTAGENESIS OF ASN-257.
RX PubMed=22387313; DOI=10.1016/j.biocel.2012.02.011;
RA Cotella D., Radicke S., Cipriani V., Cavaletto M., Merlin S., Follenzi A.,
RA Ravens U., Wettwer E., Santoro C., Sblattero D.;
RT "N-glycosylation of the mammalian dipeptidyl aminopeptidase-like protein 10
RT (DPP10) regulates trafficking and interaction with Kv4 channels.";
RL Int. J. Biochem. Cell Biol. 44:876-885(2012).
CC -!- FUNCTION: Promotes cell surface expression of the potassium channel
CC KCND2 (PubMed:15454437). Modulates the activity and gating
CC characteristics of the potassium channel KCND2 (PubMed:15454437). Has
CC no dipeptidyl aminopeptidase activity (PubMed:12662155).
CC {ECO:0000269|PubMed:12662155, ECO:0000269|PubMed:15454437,
CC ECO:0000269|PubMed:15671030}.
CC -!- SUBUNIT: May form oligomers. Interacts with KCND1 (Probable). Interacts
CC with KCND2. {ECO:0000269|PubMed:14566338, ECO:0000269|PubMed:15454437,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6NXK7,
CC ECO:0000269|PubMed:14566338}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P42658}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist, which may have different
CC subcellular locations.;
CC Name=1;
CC IsoId=Q8N608-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N608-2; Sequence=VSP_013873;
CC Name=3;
CC IsoId=Q8N608-3; Sequence=VSP_044466;
CC Name=4;
CC IsoId=Q8N608-4; Sequence=VSP_047152;
CC -!- TISSUE SPECIFICITY: Found in serum, T-cells and brain (at protein
CC level). Expressed in brain, pancreas, spinal cord and adrenal glands.
CC {ECO:0000269|PubMed:12662155, ECO:0000269|PubMed:14566338}.
CC -!- PTM: N-glycosylation is important for cell surface expression,
CC specially at Asn-257, which is crucial. {ECO:0000269|PubMed:15454437,
CC ECO:0000269|PubMed:22387313}.
CC -!- DISEASE: Asthma (ASTHMA) [MIM:600807]: The most common chronic disease
CC affecting children and young adults. It is a complex genetic disorder
CC with a heterogeneous phenotype, largely attributed to the interactions
CC among many genes and between these genes and the environment. It is
CC characterized by recurrent attacks of paroxysmal dyspnea, with wheezing
CC due to spasmodic contraction of the bronchi.
CC {ECO:0000269|PubMed:14566338, ECO:0000269|PubMed:19237393}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA96016.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY387785; AAQ91190.1; -; mRNA.
DR EMBL; AY172661; AAO17263.2; -; mRNA.
DR EMBL; AB040925; BAA96016.2; ALT_INIT; mRNA.
DR EMBL; DQ857322; ABI16086.1; -; mRNA.
DR EMBL; AK289967; BAF82656.1; -; mRNA.
DR EMBL; AC010885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC012071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016721; AAY15025.1; -; Genomic_DNA.
DR EMBL; AC017040; AAY15032.1; -; Genomic_DNA.
DR EMBL; AC066593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC067947; AAY14685.1; -; Genomic_DNA.
DR EMBL; AC068542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105422; AAY24120.1; -; Genomic_DNA.
DR EMBL; AC116620; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC118276; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC118664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030832; AAH30832.1; -; mRNA.
DR CCDS; CCDS33278.1; -. [Q8N608-2]
DR CCDS; CCDS46400.1; -. [Q8N608-1]
DR CCDS; CCDS54388.1; -. [Q8N608-3]
DR CCDS; CCDS54389.1; -. [Q8N608-4]
DR RefSeq; NP_001004360.2; NM_001004360.3. [Q8N608-2]
DR RefSeq; NP_001171505.1; NM_001178034.1.
DR RefSeq; NP_001308835.1; NM_001321906.1. [Q8N608-2]
DR RefSeq; NP_001308840.1; NM_001321911.1. [Q8N608-4]
DR RefSeq; NP_001308841.1; NM_001321912.1.
DR RefSeq; NP_001308842.1; NM_001321913.1.
DR RefSeq; NP_001308843.1; NM_001321914.1.
DR RefSeq; NP_065919.2; NM_020868.4. [Q8N608-1]
DR PDB; 4WJL; X-ray; 3.40 A; A/B=65-783.
DR PDBsum; 4WJL; -.
DR AlphaFoldDB; Q8N608; -.
DR SMR; Q8N608; -.
DR BioGRID; 121672; 4.
DR CORUM; Q8N608; -.
DR IntAct; Q8N608; 2.
DR STRING; 9606.ENSP00000376855; -.
DR ESTHER; human-DPP10; DPP4N_Peptidase_S9.
DR MEROPS; S09.974; -.
DR TCDB; 8.A.51.1.2; the dipeptidyl-aminopeptidase-like protein 6 beta subunit of kv4 channels (dpp6) family.
DR GlyConnect; 2050; 1 N-Linked glycan (1 site).
DR GlyGen; Q8N608; 7 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q8N608; -.
DR PhosphoSitePlus; Q8N608; -.
DR BioMuta; DPP10; -.
DR DMDM; 296434483; -.
DR EPD; Q8N608; -.
DR MassIVE; Q8N608; -.
DR MaxQB; Q8N608; -.
DR PaxDb; Q8N608; -.
DR PeptideAtlas; Q8N608; -.
DR PRIDE; Q8N608; -.
DR ProteomicsDB; 72119; -. [Q8N608-1]
DR ProteomicsDB; 72120; -. [Q8N608-2]
DR Antibodypedia; 18224; 346 antibodies from 36 providers.
DR DNASU; 57628; -.
DR Ensembl; ENST00000310323.12; ENSP00000309066.8; ENSG00000175497.17. [Q8N608-2]
DR Ensembl; ENST00000393147.6; ENSP00000376855.2; ENSG00000175497.17. [Q8N608-3]
DR Ensembl; ENST00000409163.5; ENSP00000387038.1; ENSG00000175497.17. [Q8N608-4]
DR Ensembl; ENST00000410059.6; ENSP00000386565.1; ENSG00000175497.17. [Q8N608-1]
DR GeneID; 57628; -.
DR KEGG; hsa:57628; -.
DR MANE-Select; ENST00000410059.6; ENSP00000386565.1; NM_020868.6; NP_065919.3.
DR UCSC; uc002tla.3; human. [Q8N608-1]
DR CTD; 57628; -.
DR DisGeNET; 57628; -.
DR GeneCards; DPP10; -.
DR HGNC; HGNC:20823; DPP10.
DR HPA; ENSG00000175497; Tissue enhanced (adrenal gland, brain, pancreas).
DR MIM; 600807; phenotype.
DR MIM; 608209; gene.
DR neXtProt; NX_Q8N608; -.
DR OpenTargets; ENSG00000175497; -.
DR PharmGKB; PA134991647; -.
DR VEuPathDB; HostDB:ENSG00000175497; -.
DR eggNOG; KOG2100; Eukaryota.
DR GeneTree; ENSGT00940000154657; -.
DR HOGENOM; CLU_006105_4_1_1; -.
DR InParanoid; Q8N608; -.
DR OMA; DKMFYLV; -.
DR OrthoDB; 269253at2759; -.
DR PhylomeDB; Q8N608; -.
DR TreeFam; TF313309; -.
DR PathwayCommons; Q8N608; -.
DR SignaLink; Q8N608; -.
DR BioGRID-ORCS; 57628; 11 hits in 1067 CRISPR screens.
DR ChiTaRS; DPP10; human.
DR GeneWiki; DPP10; -.
DR GenomeRNAi; 57628; -.
DR Pharos; Q8N608; Tbio.
DR PRO; PR:Q8N608; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8N608; protein.
DR Bgee; ENSG00000175497; Expressed in adrenal tissue and 126 other tissues.
DR ExpressionAtlas; Q8N608; baseline and differential.
DR Genevisible; Q8N608; HS.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IPI:CAFA.
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; IPI:CAFA.
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: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 3D-structure; Alternative splicing; Asthma; Cell membrane; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..796
FT /note="Inactive dipeptidyl peptidase 10"
FT /id="PRO_0000122417"
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..56
FT /note="Mediates effects on KCND2"
FT MOD_RES 138
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 143
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22387313"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22387313"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22387313"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22387313"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22387313"
FT CARBOHYD 748
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22387313"
FT VAR_SEQ 1..50
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047152"
FT VAR_SEQ 1..20
FT /note="MNQTASVSHHIKCQPSKTIK -> MRKVESRGEGGRE (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:10819331,
FT ECO:0000303|PubMed:12675227"
FT /id="VSP_013873"
FT VAR_SEQ 1..20
FT /note="MNQTASVSHHIKCQPSKTIK -> MTAAKQEPQPTPGARASQAQPADQ (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16899223"
FT /id="VSP_044466"
FT VARIANT 340
FT /note="A -> P (in dbSNP:rs2053724)"
FT /evidence="ECO:0000269|PubMed:10819331,
FT ECO:0000269|PubMed:12675227"
FT /id="VAR_057061"
FT VARIANT 401
FT /note="V -> I (in dbSNP:rs1446495)"
FT /evidence="ECO:0000269|PubMed:10819331,
FT ECO:0000269|PubMed:12662155, ECO:0000269|PubMed:12675227,
FT ECO:0000269|PubMed:14566338, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16899223"
FT /id="VAR_059759"
FT VARIANT 517
FT /note="S -> N (in dbSNP:rs13421193)"
FT /id="VAR_057062"
FT MUTAGEN 257
FT /note="N->Q: Abolishes sorting to the cell surface and
FT dimerization."
FT /evidence="ECO:0000269|PubMed:22387313"
FT CONFLICT 288
FT /note="V -> M (in Ref. 2; AAO17263, 5; BAF82656 and 7;
FT AAH30832)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="F -> L (in Ref. 1; AAQ91190)"
FT /evidence="ECO:0000305"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:4WJL"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:4WJL"
FT TURN 119..125
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 136..147
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 153..164
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 199..208
FT /evidence="ECO:0007829|PDB:4WJL"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:4WJL"
FT HELIX 229..233
FT /evidence="ECO:0007829|PDB:4WJL"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 248..257
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 291..300
FT /evidence="ECO:0007829|PDB:4WJL"
FT TURN 312..316
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 319..338
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 343..350
FT /evidence="ECO:0007829|PDB:4WJL"
FT TURN 351..354
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 355..363
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 379..390
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 425..431
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 435..443
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 447..460
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 463..466
FT /evidence="ECO:0007829|PDB:4WJL"
FT TURN 467..473
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 479..482
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 487..492
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 495..498
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 501..507
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 513..516
FT /evidence="ECO:0007829|PDB:4WJL"
FT HELIX 519..527
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 534..540
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 543..550
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 557..559
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 561..566
FT /evidence="ECO:0007829|PDB:4WJL"
FT HELIX 584..590
FT /evidence="ECO:0007829|PDB:4WJL"
FT TURN 591..593
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 594..599
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 605..607
FT /evidence="ECO:0007829|PDB:4WJL"
FT TURN 608..611
FT /evidence="ECO:0007829|PDB:4WJL"
FT HELIX 612..615
FT /evidence="ECO:0007829|PDB:4WJL"
FT HELIX 621..635
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 637..650
FT /evidence="ECO:0007829|PDB:4WJL"
FT HELIX 651..660
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 669..675
FT /evidence="ECO:0007829|PDB:4WJL"
FT HELIX 680..682
FT /evidence="ECO:0007829|PDB:4WJL"
FT HELIX 685..692
FT /evidence="ECO:0007829|PDB:4WJL"
FT TURN 696..698
FT /evidence="ECO:0007829|PDB:4WJL"
FT HELIX 701..704
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 705..708
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 718..724
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 728..730
FT /evidence="ECO:0007829|PDB:4WJL"
FT HELIX 733..744
FT /evidence="ECO:0007829|PDB:4WJL"
FT STRAND 749..754
FT /evidence="ECO:0007829|PDB:4WJL"
FT HELIX 763..780
FT /evidence="ECO:0007829|PDB:4WJL"
FT CONFLICT Q8N608-3:4
FT /note="A -> M (in Ref. 4; ABI16086)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 796 AA; 90888 MW; 072CBD67D1FB478E CRC64;
MNQTASVSHH IKCQPSKTIK ELGSNSPPQR NWKGIAIALL VILVVCSLIT MSVILLTPDE
LTNSSETRLS LEDLFRKDFV LHDPEARWIN DTDVVYKSEN GHVIKLNIET NATTLLLENT
TFVTFKASRH SVSPDLKYVL LAYDVKQIFH YSYTASYVIY NIHTREVWEL NPPEVEDSVL
QYAAWGVQGQ QLIYIFENNI YYQPDIKSSS LRLTSSGKEE IIFNGIADWL YEEELLHSHI
AHWWSPDGER LAFLMINDSL VPTMVIPRFT GALYPKGKQY PYPKAGQVNP TIKLYVVNLY
GPTHTLELMP PDSFKSREYY ITMVKWVSNT KTVVRWLNRA QNISILTVCE TTTGACSKKY
EMTSDTWLSQ QNEEPVFSRD GSKFFMTVPV KQGGRGEFHH VAMFLIQSKS EQITVRHLTS
GNWEVIKILA YDETTQKIYF LSTESSPRGR QLYSASTEGL LNRQCISCNF MKEQCTYFDA
SFSPMNQHFL LFCEGPRVPV VSLHSTDNPA KYFILESNSM LKEAILKKKI GKPEIKILHI
DDYELPLQLS LPKDFMDRNQ YALLLIMDEE PGGQLVTDKF HIDWDSVLID MDNVIVARFD
GRGSGFQGLK ILQEIHRRLG SVEVKDQITA VKFLLKLPYI DSKRLSIFGK GYGGYIASMI
LKSDEKLFKC GSVVAPITDL KLYASAFSER YLGMPSKEES TYQAASVLHN VHGLKEENIL
IIHGTADTKV HFQHSAELIK HLIKAGVNYT MQVYPDEGHN VSEKSKYHLY STILKFFSDC
LKEEISVLPQ EPEEDE
