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KCNV1_MOUSE
ID   KCNV1_MOUSE             Reviewed;         503 AA.
AC   Q8BZN2; Q8BK61; Q8BYS7; Q9CZR1;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Potassium voltage-gated channel subfamily V member 1;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv8.1;
GN   Name=Kcnv1;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain cortex, Diencephalon, Embryo, and Hypothalamus;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Potassium channel subunit that does not form functional
CC       channels by itself. Modulates KCNB1 and KCNB2 channel activity by
CC       shifting the threshold for inactivation to more negative values and by
CC       slowing the rate of inactivation. Can down-regulate the channel
CC       activity of KCNB1, KCNB2, KCNC4 and KCND1, possibly by trapping them in
CC       intracellular membranes (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heteromultimer with KCNB1 and KCNB2. Interacts with KCNC4 and
CC       KCND1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Note=Has to be associated with another potassium
CC       channel subunit to get inserted in the plasma membrane. Remains
CC       intracellular in the absence of KCNB2 (By similarity). {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. V (TC 1.A.1.2)
CC       subfamily. Kv8.1/KCNV1 sub-subfamily. {ECO:0000305}.
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DR   EMBL; AK012275; BAB28134.1; -; mRNA.
DR   EMBL; AK034091; BAC28581.1; -; mRNA.
DR   EMBL; AK038450; BAC30004.1; -; mRNA.
DR   EMBL; AK076120; BAC36198.1; -; mRNA.
DR   EMBL; AK139482; BAE24032.1; -; mRNA.
DR   EMBL; BC128477; AAI28478.1; -; mRNA.
DR   EMBL; BC128478; AAI28479.1; -; mRNA.
DR   CCDS; CCDS27459.1; -.
DR   RefSeq; NP_080476.2; NM_026200.3.
DR   RefSeq; XP_006521360.1; XM_006521297.3.
DR   AlphaFoldDB; Q8BZN2; -.
DR   SMR; Q8BZN2; -.
DR   BioGRID; 212230; 1.
DR   STRING; 10090.ENSMUSP00000022967; -.
DR   PhosphoSitePlus; Q8BZN2; -.
DR   PaxDb; Q8BZN2; -.
DR   PeptideAtlas; Q8BZN2; -.
DR   PRIDE; Q8BZN2; -.
DR   ProteomicsDB; 263505; -.
DR   Antibodypedia; 26632; 127 antibodies from 20 providers.
DR   DNASU; 67498; -.
DR   Ensembl; ENSMUST00000022967; ENSMUSP00000022967; ENSMUSG00000022342.
DR   GeneID; 67498; -.
DR   KEGG; mmu:67498; -.
DR   UCSC; uc007vql.2; mouse.
DR   CTD; 27012; -.
DR   MGI; MGI:1914748; Kcnv1.
DR   VEuPathDB; HostDB:ENSMUSG00000022342; -.
DR   eggNOG; KOG3713; Eukaryota.
DR   GeneTree; ENSGT00940000159740; -.
DR   HOGENOM; CLU_011722_4_1_1; -.
DR   InParanoid; Q8BZN2; -.
DR   OMA; LRINPCC; -.
DR   OrthoDB; 818306at2759; -.
DR   PhylomeDB; Q8BZN2; -.
DR   TreeFam; TF313103; -.
DR   Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR   BioGRID-ORCS; 67498; 1 hit in 70 CRISPR screens.
DR   PRO; PR:Q8BZN2; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q8BZN2; protein.
DR   Bgee; ENSMUSG00000022342; Expressed in lumbar dorsal root ganglion and 45 other tissues.
DR   Genevisible; Q8BZN2; MM.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR   GO; GO:0005267; F:potassium channel activity; ISO:MGI.
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; IPR003970; K_chnl_volt-dep_Kv8.1.
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   PANTHER; PTHR11537:SF38; PTHR11537:SF38; 1.
DR   Pfam; PF02214; BTB_2; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   PRINTS; PR01493; KV8CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Ion channel; Ion transport; Membrane; Potassium;
KW   Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..503
FT                   /note="Potassium voltage-gated channel subfamily V member
FT                   1"
FT                   /id="PRO_0000308353"
FT   TOPO_DOM        3..213
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..234
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        235..241
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        263..279
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        301..312
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..334
FT                   /note="Helical; Voltage-sensor; Name=Segment S4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        335..348
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        349..369
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        410..430
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        431..503
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           395..400
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        171..185
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        52
FT                   /note="R -> A (in Ref. 1; BAC36198)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95
FT                   /note="D -> G (in Ref. 1; BAC36198)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        272
FT                   /note="H -> R (in Ref. 1; BAC28581)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        335..368
FT                   /note="LRSLGMTITQCYEEVGLLLLFLSVGISIFSTIEY -> IHISLVPFNFAFKI
FT                   IFRYIGTEPPYILTHPPSIK (in Ref. 1; BAC30004)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        413
FT                   /note="F -> Y (in Ref. 1; BAC36198)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        462
FT                   /note="A -> V (in Ref. 1; BAC36198)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   503 AA;  56669 MW;  129B24D57EB69586 CRC64;
     MDLSPRNRPL LDSSSLDSGS LTSLDSSVFC SEGEGEPLAL GDCFTVNVGG SRFVLSQQAL
     SCFPHTRLGK LAVVVASYRR LGALAAAPSP LELCDDANPV DNEYFFDRSS QAFRYVLHYY
     RTGRLHVMEQ LCALSFLQEI QYWGIDELSI DSCCRDRYFR RKELSETLDF KKDTDDQESQ
     HESEQDFSKG PCPTVRQKLW DILEKPGSST AARIFGVISI IFVAVSIVNM ALMSAELSWL
     NLQLLEILEY VCISWFTGEF VLRFLCVKDR CHFLRKVPNI IDLLAILPFY ITLLVESLSG
     SHTTQELENV GRLVQVLRLL RALRMLKLGR HSTGLRSLGM TITQCYEEVG LLLLFLSVGI
     SIFSTIEYFA EQSIPDTTFT SVPCAWWWAT TSMTTVGYGD IRPDTTTGKI VAFMCILSGI
     LVLALPIAII NDRFSACYFT LKLKEAAVRQ REALKKLTKN IATDSYISVN LRDVYARSIM
     EMLRLKGRER ASTRSSGGDD FWF
 
 
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