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KCA10_CHICK
ID   KCA10_CHICK             Reviewed;         516 AA.
AC   Q7T199;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Potassium voltage-gated channel subfamily A member 10;
GN   Name=KCNA10;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC   TISSUE=Cochlear duct;
RX   PubMed=14969738; DOI=10.1016/j.molbrainres.2003.10.022;
RA   Duzhyy D.E., Sakai Y., Sokolowski B.H.;
RT   "Cloning and developmental expression of Shaker potassium channels in the
RT   cochlea of the chicken.";
RL   Brain Res. Mol. Brain Res. 121:70-85(2004).
CC   -!- FUNCTION: Mediates voltage-dependent potassium ion permeability of
CC       excitable membranes. Assuming opened or closed conformations in
CC       response to the voltage difference across the membrane, the protein
CC       forms a potassium-selective channel through which potassium ions may
CC       pass in accordance with their electrochemical gradient. The channel
CC       activity is up-regulated by cAMP (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Detected in brain, cochlear sensory epithelium,
CC       cochlear ganglion, tegumentum vasculosum. Detected at low levels in
CC       cochlear lagena. {ECO:0000269|PubMed:14969738}.
CC   -!- DEVELOPMENTAL STAGE: First detected at very low levels at embryonic day
CC       6. Detected at embryonic day 9 and 14, and 3 days after hatching.
CC       {ECO:0000269|PubMed:14969738}.
CC   -!- DOMAIN: The N-terminus may be important in determining the rate of
CC       inactivation of the channel while the tail may play a role in
CC       modulation of channel activity and/or targeting of the channel to
CC       specific subcellular compartments. {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. A (Shaker) (TC
CC       1.A.1.2) subfamily. Kv1.8/KCNA10 sub-subfamily. {ECO:0000305}.
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DR   EMBL; AY329362; AAP94024.1; -; mRNA.
DR   RefSeq; NP_989793.1; NM_204462.1.
DR   AlphaFoldDB; Q7T199; -.
DR   SMR; Q7T199; -.
DR   STRING; 9031.ENSGALP00000000597; -.
DR   PaxDb; Q7T199; -.
DR   Ensembl; ENSGALT00000000598; ENSGALP00000000597; ENSGALG00000000441.
DR   GeneID; 395116; -.
DR   KEGG; gga:395116; -.
DR   CTD; 3744; -.
DR   VEuPathDB; HostDB:geneid_395116; -.
DR   eggNOG; KOG1545; Eukaryota.
DR   GeneTree; ENSGT00940000159534; -.
DR   HOGENOM; CLU_011722_4_0_1; -.
DR   InParanoid; Q7T199; -.
DR   OMA; TACIAWF; -.
DR   OrthoDB; 695337at2759; -.
DR   PhylomeDB; Q7T199; -.
DR   TreeFam; TF313103; -.
DR   Reactome; R-GGA-1296072; Voltage gated Potassium channels.
DR   PRO; PR:Q7T199; -.
DR   Proteomes; UP000000539; Chromosome 26.
DR   Bgee; ENSGALG00000000441; Expressed in cerebellum.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003972; K_chnl_volt-dep_Kv1.
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; PR01491; KVCHANNEL.
DR   PRINTS; PR01496; SHAKERCHANEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Ion channel; Ion transport; Membrane; Potassium;
KW   Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..516
FT                   /note="Potassium voltage-gated channel subfamily A member
FT                   10"
FT                   /id="PRO_0000308276"
FT   TRANSMEM        223..244
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..296
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..363
FT                   /note="Helical; Voltage-sensor; Name=Segment S4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        441..461
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000255"
FT   MOTIF           426..431
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        261
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        339
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        503
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   516 AA;  58983 MW;  8DDF48AA407B9153 CRC64;
     MMDVSSWKEM EVALVSFDNA DQIVEDPCYS NDLSPASQSR KGHPSCANLL SNWRILINSE
     NANNETIFSR FSAEFSEHLV GERVGMEEGD QRVIINIAGL RFETRLKTLN QFPETLLGDP
     EKRMRYFDSM RNEYFFDRNR PSFDGILYYY QSGGKIRRPA NVPIDVFADE ITFYELGDEA
     MDQFREDEGF IKDPETLLPT NDFHRQFWLL FEYPESSSAA RGVALVSVLV IVISIIIFCM
     ETLPEFREER EYKSTQELSK NTTDTLLAHS TFTDPFFVIE TACIIWFSFE LFVRFIVCPS
     KTEFFKNIMN IIDIVSIIPY FVTLTTELIQ QSELNGQQNM SLAILRIIRL VRVFRIFKLS
     RHSKGLQILG QTLKASMREL GLLIFFLFIG VILFSSAVYF AEVDEPQSHF SSIPDGFWWA
     VVTMTTVGYG DMCPTTLGGK IVGTLCAIAG VLTIALPVPV IVSNFNYFYH RETENEEKQI
     LPGEVERILN SVVTGNDSME SLNKTNGGYP RDKAKK
 
 
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