KCND1_BOVIN
ID KCND1_BOVIN Reviewed; 648 AA.
AC Q52PG9;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Potassium voltage-gated channel subfamily D member 1;
DE AltName: Full=Voltage-gated potassium channel subunit Kv4.1;
GN Name=KCND1;
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].
RC TISSUE=Lens epithelium;
RA Rae J.L.;
RT "Ion channels in ocular epithelia.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated rapidly
CC inactivating A-type potassium channels. May contribute to I(To) current
CC in heart and I(Sa) current in neurons. Channel properties are modulated
CC by interactions with other alpha subunits and with regulatory subunits
CC (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
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; AY989810; AAX89129.1; -; mRNA.
DR RefSeq; NP_001019724.1; NM_001024553.1.
DR RefSeq; XP_010820207.1; XM_010821905.2.
DR AlphaFoldDB; Q52PG9; -.
DR SMR; Q52PG9; -.
DR STRING; 9913.ENSBTAP00000011882; -.
DR PaxDb; Q52PG9; -.
DR PRIDE; Q52PG9; -.
DR Ensembl; ENSBTAT00000011882; ENSBTAP00000011882; ENSBTAG00000009024.
DR GeneID; 518384; -.
DR KEGG; bta:518384; -.
DR CTD; 3750; -.
DR VEuPathDB; HostDB:ENSBTAG00000009024; -.
DR VGNC; VGNC:30434; KCND1.
DR eggNOG; KOG4390; Eukaryota.
DR GeneTree; ENSGT00940000162057; -.
DR HOGENOM; CLU_011722_9_1_1; -.
DR InParanoid; Q52PG9; -.
DR OMA; FPTAFFC; -.
DR OrthoDB; 469107at2759; -.
DR TreeFam; TF313103; -.
DR Reactome; R-BTA-1296072; Voltage gated Potassium channels.
DR Reactome; R-BTA-5576894; Phase 1 - inactivation of fast Na+ channels.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000009024; Expressed in thymus and 97 other tissues.
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: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 2: Evidence at transcript 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..648
FT /note="Potassium voltage-gated channel subfamily D member
FT 1"
FT /id="PRO_0000244029"
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..648
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 601..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 372..377
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 612..636
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:0000250|UniProtKB:Q03719"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62897"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 648 AA; 71378 MW; C2DDFB3A4D4A2D59 CRC64;
MAAGVATWLP FARAAAVGWL PLAQQPLPPA PGVKASRGDE VLVVNVSGRR FETWKNTLDR
YPDTLLGSSE KEFFYNADSG EYFFDRDPDM FRHVLNFYRT GRLHCPRQEC IQAFDEELAF
YGLVPELVGD CCLEEYRDRK KENAERLAED EEAEQAGDGP TLPAGSSLRQ RLWRAFENPH
TSTAALVFYY VTGFFIAVSV IANVVETIPC RSPTRRPPRE QPCGDRFPLA FFCMDTACVL
IFTGEYLLRL FAAPSRCRFL RSVMSLIDVV AILPYYIGLF MPKNEDVSGA FVTLRVFRVF
RIFKFSRHSQ GLRILGYTLK SCASELGFLL FSLTMAIIIF ATVMFYAEKG TNKTNFTSIP
AAFWYTIVTM TTLGYGDMVP STIAGKIFGS ICSLSGVLVI ALPVPVIVSN FSRIYHQNQR
ADKRRAQQKV RLARIRLAKS GTTNAFLQYK QNGSLEDSGG GEEQALCVRN RSAFEQQHHH
LLHCLEKTTC HEFTDELTFS EALGAVSLGS RTSRSTSVSS QPVGAGSLLS SCCPRRAKRR
AIRLANSTAS VSRGSMQELD TLAGLRRSPA PQSRSSLNAK PHDSLDLTCD SRDFVAAIIS
IPTPPANTPD ESQPSSPGGG GGGASSTLRN SSLGTPCLLP ETVKISSL
