KCND1_MOUSE
ID KCND1_MOUSE Reviewed; 651 AA.
AC Q03719; Q8CC68;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Potassium voltage-gated channel subfamily D member 1;
DE AltName: Full=Voltage-gated potassium channel subunit Kv4.1;
DE Short=mShal;
GN Name=Kcnd1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=2034678; DOI=10.1073/pnas.88.10.4386;
RA Pak M.D., Baker K., Covarrubias M., Butler A., Ratcliffe A., Salkoff L.;
RT "mShal, a subfamily of A-type K+ channel cloned from mammalian brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4386-4390(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 145-647.
RC STRAIN=C57BL/6J; TISSUE=Epididymis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP INTERACTION WITH KCNIP1.
RX PubMed=11423117; DOI=10.1016/s0014-5793(01)02560-1;
RA Nakamura T.Y., Nandi S., Pountney D.J., Artman M., Rudy B., Coetzee W.A.;
RT "Different effects of the Ca(2+)-binding protein, KChIP1, on two Kv4
RT subfamily members, Kv4.1 and Kv4.2.";
RL FEBS Lett. 499:205-209(2001).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458 AND SER-555, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated rapidly
CC inactivating A-type potassium channels. May contribute to I(To) current
CC in the heart and I(Sa) current in neurons. Channel properties are
CC modulated by subunit assembly. {ECO:0000269|PubMed:2034678}.
CC -!- SUBUNIT: Homotetramer or heterotetramer with KCND2 and/or KCND3.
CC Associates with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and
CC KCNIP4. Interacts with DPP10 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell
CC projection, dendrite {ECO:0000250}.
CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position.
CC -!- SIMILARITY: Belongs to the potassium channel family. D (Shal) (TC
CC 1.A.1.2) subfamily. Kv4.1/KCND1 sub-subfamily. {ECO:0000305}.
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DR EMBL; M64226; AAA39745.1; -; mRNA.
DR EMBL; AK033805; BAC28480.1; -; mRNA.
DR CCDS; CCDS29974.1; -.
DR PIR; A39372; A39372.
DR RefSeq; NP_032449.1; NM_008423.2.
DR AlphaFoldDB; Q03719; -.
DR SMR; Q03719; -.
DR BioGRID; 200889; 2.
DR IntAct; Q03719; 1.
DR MINT; Q03719; -.
DR STRING; 10090.ENSMUSP00000009875; -.
DR GuidetoPHARMACOLOGY; 552; -.
DR GlyGen; Q03719; 1 site.
DR iPTMnet; Q03719; -.
DR PhosphoSitePlus; Q03719; -.
DR MaxQB; Q03719; -.
DR PaxDb; Q03719; -.
DR PRIDE; Q03719; -.
DR ProteomicsDB; 269260; -.
DR Antibodypedia; 370; 263 antibodies from 31 providers.
DR DNASU; 16506; -.
DR Ensembl; ENSMUST00000009875; ENSMUSP00000009875; ENSMUSG00000009731.
DR GeneID; 16506; -.
DR KEGG; mmu:16506; -.
DR UCSC; uc009sms.1; mouse.
DR CTD; 3750; -.
DR MGI; MGI:96671; Kcnd1.
DR VEuPathDB; HostDB:ENSMUSG00000009731; -.
DR eggNOG; KOG4390; Eukaryota.
DR GeneTree; ENSGT00940000162057; -.
DR HOGENOM; CLU_011722_9_1_1; -.
DR InParanoid; Q03719; -.
DR OMA; FPTAFFC; -.
DR OrthoDB; 469107at2759; -.
DR PhylomeDB; Q03719; -.
DR TreeFam; TF313103; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR Reactome; R-MMU-5576894; Phase 1 - inactivation of fast Na+ channels.
DR BioGRID-ORCS; 16506; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Kcnd1; mouse.
DR PRO; PR:Q03719; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q03719; protein.
DR Bgee; ENSMUSG00000009731; Expressed in lumbar dorsal root ganglion and 78 other tissues.
DR ExpressionAtlas; Q03719; baseline and differential.
DR Genevisible; Q03719; MM.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR GO; GO:0005250; F:A-type (transient outward) potassium channel activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.350; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR InterPro; IPR003975; K_chnl_volt-dep_Kv4.
DR InterPro; IPR004054; K_chnl_volt-dep_Kv4.1.
DR InterPro; IPR024587; K_chnl_volt-dep_Kv4_C.
DR InterPro; IPR021645; Shal-type_N.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR028325; VG_K_chnl.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF11879; DUF3399; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF11601; Shal-type; 1.
DR PRINTS; PR01516; KV41CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01497; SHALCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW Cell projection; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Metal-binding; Phosphoprotein; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel; Zinc.
FT CHAIN 1..651
FT /note="Potassium voltage-gated channel subfamily D member
FT 1"
FT /id="PRO_0000054062"
FT TOPO_DOM 1..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT INTRAMEM 365..385
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..651
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 2..20
FT /note="Interaction with KCNIP2"
FT /evidence="ECO:0000250"
FT REGION 144..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..489
FT /note="Mediates dendritic targeting"
FT /evidence="ECO:0000250"
FT REGION 566..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 372..377
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 568..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 651 AA; 71698 MW; 801DECC3C56C721F CRC64;
MAAGVATWLP FARAAAVGWL PLAQQPLPPA PEVKASRGDE VLVVNVSGRR FETWKNTLDR
YPDTLLGSSE KEFFYDAESG EYFFDRDPDM FRHVLNFYRT GRLHCPRQEC IQAFDEELAF
YGLVPELVGD CCLEEYRDRK KENAERLAED EEAEQAGEGP ALPAGSSLRQ RLWRAFENPH
TSTAALVFYY VTGFFIAVSV IANVVETIPC RGTPRWPSKE QSCGDRFPTA FFCMDTACVL
IFTGEYLLRL FAAPSRCRFL RSVMSLIDVV AILPYYIGLF VPKNDDVSGA FVTLRVFRVF
RIFKFSRHSQ GLRILGYTLK SCASELGFLL FSLTMAIIIF ATVMFYAEKG TSKTNFTSIP
AAFWYTIVTM TTLGYGDMVP STIAGKIFGS ICSLSGVLVI ALPVPVIVSN FSRIYHQNQR
ADKRRAQQKV RLARIRLAKS GTTNAFLQYK QNGGLEDSGS GDGQMLCVRS RSAFEQQHHH
LLHCLEKTTC HEFTDELTFS EALGAVSLGG RTSRSTSVSS QPMGPGSLFS SCCSRRVNRR
AIRLANSTAS VSRGSMQELD TLAGLRRSPA PQTRSSLNAK PHDSLDLNCD SRDFVAAIIS
IPTPPANTPD ESQPSSPSGG GGSGGTPNTT LRNSSLGTPC LLPETVKISS L
