GenomeNet

Database: UniProt
Entry: A0A0G2JVW2_RAT
LinkDB: A0A0G2JVW2_RAT
Original site: A0A0G2JVW2_RAT 
ID   A0A0G2JVW2_RAT          Unreviewed;      1960 AA.
AC   A0A0G2JVW2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-SEP-2017, entry version 18.
DE   RecName: Full=Voltage-dependent R-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=Cacna1e {ECO:0000313|Ensembl:ENSRNOP00000069641,
GN   ECO:0000313|RGD:2246};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000069641, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000069641, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069641,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000213|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000069641}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069641};
RG   Ensembl;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the
CC       entry of calcium ions into excitable cells and are also involved
CC       in a variety of calcium-dependent processes, including muscle
CC       contraction, hormone or neurotransmitter release, gene expression,
CC       cell motility, cell division and cell death. The isoform alpha-1E
CC       gives rise to R-type calcium currents. R-type calcium channels
CC       belong to the 'high-voltage activated' (HVA) group and are blocked
CC       by nickel, and partially by omega-agatoxin-IIIA (omega-Aga-IIIA).
CC       They are however insensitive to dihydropyridines (DHP), omega-
CC       conotoxin-GVIA (omega-CTx-GVIA), and omega-agatoxin-IVA (omega-
CC       Aga-IVA). Calcium channels containing alpha-1E subunit could be
CC       involved in the modulation of firing patterns of neurons which is
CC       important for information processing.
CC       {ECO:0000256|RuleBase:RU003808}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003808};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU003808}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family. {ECO:0000256|RuleBase:RU003808}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00448}.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSRNOP00000069641}.
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DR   EMBL; AABR07021443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07021444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07021445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07021446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR07021447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSRNOT00000090544; ENSRNOP00000069641; ENSRNOG00000002863.
DR   RGD; 2246; Cacna1e.
DR   GeneTree; ENSGT00830000128247; -.
DR   Reactome; R-RNO-112308; Presynaptic depolarization and calcium channel opening.
DR   Reactome; R-RNO-422356; Regulation of insulin secretion.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000002863; -.
DR   ExpressionAtlas; A0A0G2JVW2; baseline.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005449; VDCC_R_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF253; PTHR10037:SF253; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 3.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01633; RVDCCALPHA1.
DR   SMART; SM01062; Ca_chan_IQ; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   1: Evidence at protein level;
KW   Calcium {ECO:0000256|RuleBase:RU003808};
KW   Calcium channel {ECO:0000256|RuleBase:RU003808};
KW   Calcium transport {ECO:0000256|RuleBase:RU003808};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002494};
KW   Ion channel {ECO:0000256|RuleBase:RU003808};
KW   Ion transport {ECO:0000256|RuleBase:RU003808};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU003808};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003808}.
FT   TRANSMEM     17     39       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    166    186       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    192    210       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    292    314       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    369    392       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    842    861       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    914    931       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    980   1002       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1092   1117       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1173   1191       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1203   1226       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1232   1250       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1297   1315       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1390   1414       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1430   1465       EF-hand. {ECO:0000259|PROSITE:PS50222}.
FT   COILED      388    415       {ECO:0000256|SAM:Coils}.
FT   COILED      789    811       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1960 AA;  222715 MW;  15BE7A69B5E31AF3 CRC64;
     TIFLSQTNDA LGATWNWLYF IPLIIIGSFF VLNLVLGVLS GEFAKERERV ENRRAFMKLR
     RQQQIERELN GYRAWIDKAE EVMLAEENKN SGTSALEVLR RATIKRSRTE AMTRDSSDEH
     CVDISSVGTP LARASIKSTK VDGASYFRHK ERLLRISIRH MVKSQVFYWI VLSVVALNTA
     CVAIVHHNQP QWLTHLLYYA EFLFLGLFLL EMSLKMYGMG PRLYFHSSFN CFDFGVTVGS
     IFEVVWAIFR PGTSFGISVL RALRLLRIFK ITKYWASLRN LVVSLMSSMK SIISLLFLLF
     LFIVVFALLG MQLFGGRFNF NDGTPSANFD TFPAAIMTVF QILTGEDWNE VMYNGIRSQG
     GVSSGMWSAI YFIVLTLFGN YTLLNVFLAI AVDNLANAQE LTKDEQEEEE AFNQKHALQK
     AKEVSPMSAP NMPSIERDRR RRHHMSMWEP RSSHLRERRR RHHMSVWEQR TSQLRRHMQM
     SSQEALNKEE APPMNPLNPL NPLSPLNPLN AHPSLYRRPR PIEGLALGLG LEKCEEERIS
     RGGSLKGDIG GLTSVLDNQR SPLSLGKREP PWLPRSCHGN CDPTQQETGG GETVVTFEDR
     ARHRQSQRRS RHRRVRTEGK ESASASRSRS ASQERSLDEG VSIDGEKEHE PQSSHRSKEP
     TIHEEERTQD LRRTNSLMVP RGSGLVGALD EAETPLVQPQ PELEVGKDAA LTEQEAEGSS
     EQALLADVQL DVGRGISQSE PDLSCMTTNM DKATTESTSV TVAIPDMDPL VDSTVVNISN
     KTDGEASPLK EAETKEEEEE VEKKKQKKEK RETGKAMVPH SSMFIFSTTN PIRKACHYIV
     NLRYFEMCIL LVIAASSIAL AAEDPVLTNS ERNKVLRYFD YVFTGVFTFE MVIKMIDQGL
     ILQDGSYFRD LWNILDFVVV VGALVAFALA VDAFRTNKGR DIKTIKSLRV LRVLRPLKTI
     KRLPKLKAVF DCVVTSLKNV FNILIVYKLF MFIFAVIAVQ LFKGKFFYCT DSSKDTEKEC
     IGNYVDHEKN KMEVKGREWK RHEFHYDNII WALLTLFTVS TGEGWPQVLQ HSVDVTEEDR
     GPSRSNRMEM SIFYVVYFVV FPFFFVNIFV ALIIITFQEQ GDKMMEECSL EKNERACIDF
     AISAKPLTRY MPQNRHTFQY RVWHFVVSPS FEYTIMAMIA LNTVVLMMKY YSAPWTYELA
     LKYLNIAFTM VFSLECVLKV IAFGFLNYFR DTWNIFDFIT VIGSITEIIL TDSKLVNTSG
     FNMSFLKLFR AARLIKLLRQ GYTIRILLWT FVQSFKALPY VCLLIAMLFF IYAIIGMQVF
     GNIKLDEESH INRHNNFRSF FGSLMLLFRS ATGEAWQEIM LSCLGEKGCE PDTTAPSGQN
     ESERCGTDLA YVYFVSFIFF CSFLMLNLFV AVIMDNFEYL TRDSSILGPH HLDEFVRVWA
     EYDRAACGRI HYTEMYEMLT LMSPPLGLGK RCPSKVAYKR LVLMNMPVAE DMTVHFTSTL
     MALIRTALDI KIAKGGADRQ QLDSELQKET LAIWPHLSQK MLDLLVPMPK ASDLTVGKIY
     AAMMIMDYYK QSKVKKQRQQ LEEQKNAPMF QRMEPSSLPQ EIISNAKALP YLQQDPVSGL
     SGRSGYPSMS PLSPQEIFQL ACMDPADDGQ FQEQQSLVVT DPSSMRRSFS TIRDKRSNSS
     WLEEFSMERS SENTYKSRRR SYHSSLRLSA HRLNSDSGHK SDTHRSGGRE RGRSKERKHL
     LSPDVSRCNS EERGTQADWE SPERRQSRSP SEGRSQTPNR QGTGSLSESS IPSISDTSTP
     RRSRRQLPPV PPKPRPLLSY SSLMRHTGGI SPPPDGSEGG SPLASQALES NSACLTESSN
     SLHPQQGQHP SPQHYISEPY LALHEDSHAS DCGEEETLTF EAAVATSLGR SNTIGSAPPL
     RHSWQMPNGH YRRRRVGGLG LAMCGAVSDL LSDTEEDDKC
//
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