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Database: UniProt
Entry: F1LMS1_RAT
LinkDB: F1LMS1_RAT
Original site: F1LMS1_RAT 
ID   F1LMS1_RAT              Unreviewed;      2296 AA.
AC   F1LMS1;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 3.
DT   25-OCT-2017, entry version 56.
DE   RecName: Full=Voltage-dependent R-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=Cacna1e {ECO:0000313|Ensembl:ENSRNOP00000003928,
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:ENSRNOP00000003928, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000003928, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000003928,
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:0000313|Ensembl:ENSRNOP00000003928}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000003928};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [3] {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).
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:ENSRNOP00000003928}.
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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   PaxDb; F1LMS1; -.
DR   Ensembl; ENSRNOT00000003928; ENSRNOP00000003928; ENSRNOG00000002863.
DR   RGD; 2246; Cacna1e.
DR   eggNOG; ENOG410INF5; Eukaryota.
DR   eggNOG; ENOG410YD06; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   OMA; RRRHHMS; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   TreeFam; TF312805; -.
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; F1LMS1; 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:Ensembl.
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:SF57; PTHR10037:SF57; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
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     94    111       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    131    151       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    163    181       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    222    244       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    296    317       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    329    351       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    478    498       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    504    522       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    604    626       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    681    704       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1135   1154       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1207   1226       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1272   1294       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1384   1409       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1465   1483       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1495   1518       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1524   1542       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1589   1607       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1682   1706       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1722   1757       EF-hand. {ECO:0000259|PROSITE:PS50222}.
FT   COILED      700    727       {ECO:0000256|SAM:Coils}.
FT   COILED     1082   1104       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2296 AA;  259406 MW;  67E6F1BE5FB81DF5 CRC64;
     MARFGEAVVV GRPGSGDGDS DQSRNRQGTP VPASGPAAAY KQSKAQRART MALYNPIPVR
     QNCFTVNRSL FIFGEDNIVR KYAKKLIDWP PFEYMILATI IANCIVLALE QHLPEDDKTP
     MSRRLEKTEP YFIGIFCFEA GIKIVALGFI FHKGSYLRNG WNVMDFIVVL SGILATAGTH
     FNTHVDLRTL RAVRVLRPLK LVSGIPSLQI VLKSIMKAMV PLLQIGLLLF FAILMFAIIG
     LEFYSGKLHR ACFMNNSGIL EGFDPPHPCG VQGCPAGYEC KDWIGPNDGI TQFDNILFAV
     LTVFQCITME GWTTVLYNTN DALGATWNWL YFIPLIIIGS FFVLNLVLGV LSGEFAKERE
     RVENRRAFMK LRRQQQIERE LNGYRAWIDK AEEVMLAEEN KNSGTSALEV LRRATIKRSR
     TEAMTRDSSD EHCVDISSVG TPLARASIKS TKVDGASYFR HKERLLRISI RHMVKSQVFY
     WIVLSVVALN TACVAIVHHN QPQWLTHLLY YAEFLFLGLF LLEMSLKMYG MGPRLYFHSS
     FNCFDFGVTV GSIFEVVWAI FRPGTSFGIS VLRALRLLRI FKITKYWASL RNLVVSLMSS
     MKSIISLLFL LFLFIVVFAL LGMQLFGGRF NFNDGTPSAN FDTFPAAIMT VFQILTGEDW
     NEVMYNGIRS QGGVSSGMWS AIYFIVLTLF GNYTLLNVFL AIAVDNLANA QELTKDEQEE
     EEAFNQKHAL QKAKEVSPMS APNMPSIERE RRRRHHMSVW EQRTSQLRRH MQMSSQEALN
     KEEAPPMNPL NPLNPLSPLN PLNAHPSLYR RPRPIEGLAL GLGLEKCEEE RISRGGSLKG
     DIGGLTSVLD NQRSPLSLGK REPPWLPRSC HGNCDPTQQE TGGGETVVTF EDRARHRQSQ
     RRSRHRRVRT EGKESASASR SRSASQERSL DEGVSIDGEK EHEPQSSHRS KEPTIHEEER
     TQDLRRTNSL MVPRGSGLVG ALDEAETPLV QPQPELEVGK DAALTEQEAE GSSEQALLAD
     VQLDVGRGIS QSEPDLSCMT TNMDKATTES TSVTVAIPDM DPLVDSTVVN ISNKTDGEAS
     PLKEAETKEE EEEVEKKKQK KEKRETGKAM VPHSSMFIFS TTNPIRKACH YIVNLRYFEM
     CILLVIAASS IALAAEDPVL TNSERNKVLR YFDYVFTGVF TFEMVIKMID QGLILQDGSY
     FRDLWNILDF VVVVGALVAF ALANALGTNK GRDIKTIKSL RVLRVLRPLK TIKRLPKLKA
     VFDCVVTSLK NVFNILIVYK LFMFIFAVIA VQLFKGKFFY CTDSSKDTEK ECIGNYVDHE
     KNKMEVKGRE WKRHEFHYDN IIWALLTLFT VSTGEGWPQV LQHSVDVTEE DRGPSRSNRM
     EMSIFYVVYF VVFPFFFVNI FVALIIITFQ EQGDKMMEEC SLEKNERACI DFAISAKPLT
     RYMPQNRHTF QYRVWHFVVS PSFEYTIMAM IALNTVVLMM KYYSAPWTYE LALKYLNIAF
     TMVFSLECVL KVIAFGFLNY FRDTWNIFDF ITVIGSITEI ILTDSKLVNT SGFNMSFLKL
     FRAARLIKLL RQGYTIRILL WTFVQSFKAL PYVCLLIAML FFIYAIIGMQ VFGNIKLDEE
     SHINRHNNFR SFFGSLMLLF RSATGEAWQE IMLSCLGEKG CEPDTTAPSG QNESERCGTD
     LAYVYFVSFI FFCSFLMLNL FVAVIMDNFE YLTRDSSILG PHHLDEFVRV WAEYDRAACG
     RIHYTEMYEM LTLMSPPLGL GKRCPSKVAY KRLVLMNMPV AEDMTVHFTS TLMALIRTAL
     DIKIAKGGAD RQQLDSELQK ETLAIWPHLS QKMLDLLVPM PKASDLTVGK IYAAMMIMDY
     YKQSKVKKQR QQLEEQKNAP MFQRMEPSSL PQEIISNAKA LPYLQQDPVS GLSGRSGYPS
     MSPLSPQEIF QLACMDPADD GQFQEQQSLE PEVSELKSVQ SSNHGIYLPP DTQEHAGSGR
     ASSMPRLTMD PQVVTDPSSM RRSFSTIRDK RSNSSWLEEF SMERSSENTY KSRRRSYHSS
     LRLSAHRLNS DSGHKSDTHR SGGRERGRSK ERKHLLSPDV SRCNSEERGT QADWESPERR
     QSRSPSEGRS QTPNRQGTGS LSESSIPSIS DTSTPRRSRR QLPPVPPKPR PLLSYSSLMR
     HTGGISPPPD GSEGGSPLAS QALESNSACL TESSNSLHPQ QGQHPSPQHY ISEPYLALHE
     DSHASDCGEE ETLTFEAAVA TSLGRSNTIG SAPPLRHSWQ MPNGHYRRRR RGGPGPGMMC
     GAVSDLLSDT EEDDKC
//
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