KCND3_RABIT
ID KCND3_RABIT Reviewed; 655 AA.
AC Q9TTT5;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Potassium voltage-gated channel subfamily D member 3;
DE AltName: Full=Voltage-gated potassium channel subunit Kv4.3;
GN Name=KCND3;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=New Zealand white; TISSUE=Corneal endothelium;
RA Rae J.L.;
RT "Ion channels in cornea endothelium.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 73-645 (ISOFORM 2), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12122138; DOI=10.1113/jphysiol.2002.018382;
RA Sanchez D., Lopez-Lopez J.R., Perez-Garcia M.T., Sanz-Alfayate G.,
RA Obeso A., Ganfornina M.D., Gonzalez C.;
RT "Molecular identification of Kv alpha subunits that contribute to the
RT oxygen-sensitive K(+) current of chemoreceptor cells of the rabbit carotid
RT body.";
RL J. Physiol. (Lond.) 542:369-382(2002).
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 {ECO:0000269|PubMed:12122138}.
CC -!- SUBUNIT: Homotetramer or heterotetramer with KCND1 and/or KCND2.
CC Associates with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and
CC KCNIP4. Interacts with DLG1, KCNE1, KCNE2, SCN1B and KCNAB1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q62897};
CC Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:Q62897}; Multi-pass membrane protein
CC {ECO:0000255}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q62897}. Note=Interaction with palmitoylated
CC KCNIP2 and KCNIP3 enhances cell surface expression.
CC {ECO:0000250|UniProtKB:Q62897}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long;
CC IsoId=Q9TTT5-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q9TTT5-2; Sequence=VSP_008830;
CC -!- TISSUE SPECIFICITY: Detected in carotid body chemoreceptor cells and in
CC frontal cortex. {ECO:0000269|PubMed:12122138}.
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 -!- PTM: Regulated through phosphorylation at Ser-569 by CaMK2D.
CC -!- SIMILARITY: Belongs to the potassium channel family. D (Shal) (TC
CC 1.A.1.2) subfamily. Kv4.3/KCND3 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF198445; AAF06021.1; -; mRNA.
DR EMBL; AF493549; AAM46843.1; -; mRNA.
DR RefSeq; NP_001076186.1; NM_001082717.1. [Q9TTT5-1]
DR AlphaFoldDB; Q9TTT5; -.
DR SMR; Q9TTT5; -.
DR STRING; 9986.ENSOCUP00000012275; -.
DR PRIDE; Q9TTT5; -.
DR GeneID; 100009472; -.
DR KEGG; ocu:100009472; -.
DR CTD; 3752; -.
DR eggNOG; KOG4390; Eukaryota.
DR InParanoid; Q9TTT5; -.
DR OrthoDB; 469107at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
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; IPR004056; K_chnl_volt-dep_Kv4.3.
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; PR01518; KV43CHANNEL.
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 Alternative splicing; Cell membrane; Cell projection; Ion channel;
KW Ion transport; Membrane; Metal-binding; Phosphoprotein; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel; Zinc.
FT CHAIN 1..655
FT /note="Potassium voltage-gated channel subfamily D member
FT 3"
FT /id="PRO_0000054070"
FT TOPO_DOM 1..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT INTRAMEM 360..380
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..655
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 2..20
FT /note="Interaction with KCNIP2"
FT /evidence="ECO:0000250"
FT REGION 474..489
FT /note="Mediates dendritic targeting"
FT /evidence="ECO:0000250"
FT REGION 618..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 367..372
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 624..639
FT /note="Pro 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 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0V1"
FT MOD_RES 459
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0V1"
FT MOD_RES 569
FT /note="Phosphoserine; by CaMK2D"
FT /evidence="ECO:0000250|UniProtKB:Q62897"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0V1"
FT VAR_SEQ 488..506
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12122138"
FT /id="VSP_008830"
SQ SEQUENCE 655 AA; 73380 MW; C6AE9E895415FAF9 CRC64;
MAAGVAAWLP FARAAAIGWM PVANCPMPLA PADKSKRQDE LIVLNVSGRR FQTWRTTLER
YPDTLLGSTE KEFFFNEDTK EYFFDRDPEV FRCVLNFYRT GKLHYPRYEC ISAYDDELAF
YGILPEIIGD CCYEEYKDRK RENAERLMDD NDSENNQESM PSLSFRQTMW RAFENPHTST
LALVFYYVTG FFIAVSVITN VVETVPCGTV PGSKELPCGE RYSVAFFCLD TACVMIFTVE
YLLRLFAAPS RYRFIRSVMS IIDVVAIMPY YIGLVMTNNE DVSGAFVTLR VFRVFRIFKF
SRHSQGLRIL GYTLKSCASE LGFLLFSLTM AIIIFATVMF YAEKGSSASK FTSIPASFWY
TIVTMTTLGY GDMVPKTIAG KIFGSICSLS GVLVIALPVP VIVSNFSRIY HQNQRADKRR
AQKKARLARI RVAKTGSSNA YLHSKRNGLL NEALELTGTP EEEHMGKTAS LIESQHHHLL
HCLEKTTGLS YLVDDPLLSV RTSTIKNHEF IDEQMFEQNC MESSMQNYPS TRSPSLSSHA
GLTTTCCSRR SKKTTHLPNS NLPATRLRSM QELSTIHIQG SEQPSLTTSR SSLNLKADDG
LRPNCKTSQI TTAIISIPAP PALTPEGETR PPPASPGPNT NIPSIASNVV KVSVL
