KVS4_CAEEL
ID KVS4_CAEEL Reviewed; 503 AA.
AC Q9XXD1; Q6EUU0;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Probable voltage-gated potassium channel subunit kvs-4 {ECO:0000305};
GN Name=kvs-4 {ECO:0000312|WormBase:Y48A6B.6a};
GN ORFNames=Y48A6B.6 {ECO:0000312|WormBase:Y48A6B.6a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP INTERACTION WITH UNC-101, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN,
RP AND MUTAGENESIS OF 217-TRP--GLU-221; 217-TRP--ILE-219; ILE-219;
RP 496-GLU--LEU-500 AND 497-GLN--MET-498.
RX PubMed=26762178; DOI=10.1002/1873-3468.12043;
RA Zhou X., Zeng J., Ouyang C., Luo Q., Yu M., Yang Z., Wang H., Shen K.,
RA Shi A.;
RT "A novel bipartite UNC-101/AP-1 mu1 binding signal mediates KVS-4/Kv2.1
RT somatodendritic distribution in Caenorhabditis elegans.";
RL FEBS Lett. 590:76-92(2016).
CC -!- FUNCTION: Voltage-gated potassium channel that mediates transmembrane
CC potassium transport in excitable membranes.
CC {ECO:0000250|UniProtKB:P63142}.
CC -!- SUBUNIT: Homotetramer or heterotetramer (Probable). Interacts with unc-
CC 101 (via N-terminus); which targets kvs-4 to dendrites
CC (PubMed:26762178). {ECO:0000269|PubMed:26762178, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}. Perikaryon {ECO:0000269|PubMed:26762178}. Cell
CC projection, axon {ECO:0000269|PubMed:26762178}. Cell projection,
CC dendrite {ECO:0000269|PubMed:26762178}. Note=Association with unc-101
CC is required for dendritic localization. {ECO:0000305|PubMed:26762178}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:Y48A6B.6a};
CC IsoId=Q9XXD1-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y48A6B.6b};
CC IsoId=Q9XXD1-2; Sequence=VSP_059007, VSP_059008;
CC -!- TISSUE SPECIFICITY: Expressed in the cholinergic motor neuron DA9,
CC mechanosensory neurons ALM and PLM, and the interneuron PVPL.
CC {ECO:0000269|PubMed:26762178}.
CC -!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position. Channel opening and closing is effected by a
CC conformation change that affects the position and orientation of the
CC voltage-sensor paddle formed by S3 and S4 within the membrane. A
CC transmembrane electric field that is positive inside would push the
CC positively charged S4 segment outwards, thereby opening the pore, while
CC a field that is negative inside would pull the S4 segment inwards and
CC close the pore. Changes in the position and orientation of S4 are then
CC transmitted to the activation gate formed by the inner helix bundle via
CC the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}.
CC -!- DOMAIN: The EQMIL and WNIIE motifs are required for dendritic
CC localization. {ECO:0000269|PubMed:26762178}.
CC -!- SIMILARITY: Belongs to the potassium channel family. B (Shab) (TC
CC 1.A.1.2) subfamily. Kv2.2/KCNB2 sub-subfamily. {ECO:0000305}.
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DR EMBL; BX284603; CAA19530.3; -; Genomic_DNA.
DR EMBL; BX284603; CAH04760.1; -; Genomic_DNA.
DR PIR; T26983; T26983.
DR RefSeq; NP_001022888.1; NM_001027717.2. [Q9XXD1-1]
DR RefSeq; NP_001022889.1; NM_001027718.3.
DR AlphaFoldDB; Q9XXD1; -.
DR SMR; Q9XXD1; -.
DR IntAct; Q9XXD1; 1.
DR MINT; Q9XXD1; -.
DR STRING; 6239.Y48A6B.6b; -.
DR EnsemblMetazoa; Y48A6B.6a.1; Y48A6B.6a.1; WBGene00012967. [Q9XXD1-1]
DR EnsemblMetazoa; Y48A6B.6b.1; Y48A6B.6b.1; WBGene00012967.
DR GeneID; 190011; -.
DR UCSC; Y48A6B.6b; c. elegans.
DR CTD; 190011; -.
DR WormBase; Y48A6B.6a; CE36457; WBGene00012967; kvs-4. [Q9XXD1-1]
DR WormBase; Y48A6B.6b; CE36458; WBGene00012967; kvs-4. [Q9XXD1-2]
DR eggNOG; KOG3713; Eukaryota.
DR HOGENOM; CLU_011722_4_1_1; -.
DR OMA; TGQIHQP; -.
DR OrthoDB; 818306at2759; -.
DR Reactome; R-CEL-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR SignaLink; Q9XXD1; -.
DR PRO; PR:Q9XXD1; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00012967; Expressed in larva and 1 other tissue.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IBA:GO_Central.
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; IPR005821; Ion_trans_dom.
DR InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR InterPro; IPR003971; K_chnl_volt-dep_Kv9.
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; PF00520; Ion_trans; 1.
DR PRINTS; PR01494; KV9CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..503
FT /note="Probable voltage-gated potassium channel subunit
FT kvs-4"
FT /evidence="ECO:0000305"
FT /id="PRO_0000440898"
FT TOPO_DOM 1..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 232..252
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..275
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 276..296
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 314..334
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..346
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 347..366
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 367..383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 384..404
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..417
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 418..429
FT /note="Helical; Name=Pore helix"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 430..434
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 435..445
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 446..466
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..503
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 368..383
FT /note="S4-S5 linker"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT MOTIF 217..219
FT /note="Required for dendritic localization"
FT /evidence="ECO:0000269|PubMed:26762178"
FT MOTIF 430..435
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT MOTIF 496..500
FT /note="Required for dendritic localization"
FT /evidence="ECO:0000269|PubMed:26762178"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT VAR_SEQ 1..47
FT /note="MNSAIMQGAAMATSHGIARLNRHNAQRNHFHIPTANRLFYQLQTPCT -> M
FT SHQASHFGVKKKWKANGSSGGGGLSAFARMKPVLDPSADRIWTIGQIIYQRHQAFNRNS
FT AIKSQDNGSFDYIDMVSQSSLDR (in isoform b)"
FT /id="VSP_059007"
FT VAR_SEQ 452..478
FT /note="Missing (in isoform b)"
FT /id="VSP_059008"
FT MUTAGEN 217..221
FT /note="WNIIE->AAAAA: Disrupts dendritic localization."
FT /evidence="ECO:0000269|PubMed:26762178"
FT MUTAGEN 217..219
FT /note="WNI->ANA: Disrupts dendritic localization."
FT /evidence="ECO:0000269|PubMed:26762178"
FT MUTAGEN 219
FT /note="I->A: Disrupts dendritic localization."
FT /evidence="ECO:0000269|PubMed:26762178"
FT MUTAGEN 496..500
FT /note="EQMIL->AAAAA: Disrupts dendritic localization."
FT /evidence="ECO:0000269|PubMed:26762178"
FT MUTAGEN 497..498
FT /note="QM->AA: Disrupts dendritic localization."
FT /evidence="ECO:0000269|PubMed:26762178"
SQ SEQUENCE 503 AA; 56966 MW; 1611A5E0417E016C CRC64;
MNSAIMQGAA MATSHGIARL NRHNAQRNHF HIPTANRLFY QLQTPCTSTE EERRTVQTDD
VAEIGMQRPD YQMYCGEEEI SEQFVKLNVG GQRFMLRKDT IRRRGVGRLL DLINKPVADS
NADAFFSSTS EFYFERPPSL FHIVYQFYLN GVIHQPSNLC PVDIIEELEY WRIIPDQYLA
SCCCAQQIDD DDEEVEEQDK PNLFKTLRFG EIRRCVWNII EEPASSGKAQ AFAVCSVVFV
LISISGLVLG SLPELQVATK QRNNLTGEEF TEMEPMPILG YIEYVCIVWF TMEYGLKMLV
SAERSKTFRQ LLNIIDLLAI LPFIIEMLLL IFGISTEQLR DLKGAFLVIR ILRVLRVIRV
LKLGRYSSGL QMFGKTLKAS FRQLGMMAMV VMTGVIFFST LVYFLEKDEP ASKFHSIPAA
CWWCIVTMTT VGYGDLTPVT VPGKLVATGA IACGVLVLAL PITIIVDNFM KVAETERPAG
GNRYRTSQYP KATKSEQMIL KVT
