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Database: UniProt
Entry: F6SQ28_MACMU
LinkDB: F6SQ28_MACMU
Original site: F6SQ28_MACMU 
ID   F6SQ28_MACMU            Unreviewed;      2027 AA.
AC   F6SQ28;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 2.
DT   25-OCT-2017, entry version 46.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1D {ECO:0000313|Ensembl:ENSMMUP00000025309};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000025309, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Ensembl:ENSMMUP00000025309, ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000025309,
RC   ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C.,
RA   Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W.,
RA   Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E.,
RA   Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y.,
RA   Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T.,
RA   Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J.,
RA   Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A.,
RA   Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M.,
RA   Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D.,
RA   Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J.,
RA   Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E.,
RA   Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S.,
RA   Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X.,
RA   Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E.,
RA   Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M.,
RA   Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M.,
RA   Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y.,
RA   Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J.,
RA   Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A.,
RA   Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B.,
RA   Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S.,
RA   Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V.,
RA   Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A.,
RA   Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C.,
RA   Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P.,
RA   Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E.,
RA   Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque
RT   genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMMUP00000025309}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000025309};
RG   Ensembl;
RL   Submitted (JUL-2011) 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-1C
CC       gives rise to L-type calcium currents. Long-lasting (L-type)
CC       calcium channels belong to the 'high-voltage activated' (HVA)
CC       group. They are blocked by dihydropyridines (DHP),
CC       phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA
CC       (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-
CC       GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA).
CC       Calcium channels containing the alpha-1C subunit play an important
CC       role in excitation-contraction coupling in the heart. Binding of
CC       calmodulin or CABP1 at the same regulatory sites results in an
CC       opposit effects on the channel function.
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: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSMMUP00000025309}.
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DR   EMBL; JSUE03023610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; JSUE03023611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; JSUE03023612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 9544.ENSMMUP00000025309; -.
DR   Ensembl; ENSMMUT00000027053; ENSMMUP00000025309; ENSMMUG00000019262.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   InParanoid; F6SQ28; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   TreeFam; TF312805; -.
DR   Proteomes; UP000006718; Chromosome 2.
DR   Bgee; ENSMMUG00000019262; -.
DR   ExpressionAtlas; F6SQ28; baseline.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
DR   GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR   InterPro; IPR031688; CAC1F_C.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR005452; LVDCC_a1dsu.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF139; PTHR10037:SF139; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16885; CAC1F_C; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
DR   PRINTS; PR01636; LVDCCALPHA1D.
DR   SMART; SM01062; Ca_chan_IQ; 1.
PE   3: Inferred from homology;
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:UP000006718};
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:UP000006718};
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     47     66       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     78     95       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    152    175       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    231    252       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    264    286       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    424    442       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    462    485       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    554    573       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    626    653       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    788    806       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    826    846       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    858    884       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    904    934       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1031   1056       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1110   1128       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1140   1160       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1235   1253       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1327   1350       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1473   1507       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      656    687       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2027 AA;  230274 MW;  DD54463FA4CE956B CRC64;
     ISSVQSHHWN LCCALVRRAC CVLQMCANNK HACYVLSRLI THEKVEYAFL IIFTVETFLK
     IIAYGLLLHP NAYVRNGWNL LDFVIVIVGL FSVILEQLTK ETEGGNHSSG KSGGFDVKAL
     RAFRVLRPLR LVSGVPSLQV VLNSIIKAMV PLLHIALLVL FVIIIYAIIG LELFIGKMHK
     TCFFADSDIV AEEDPAPCAF SGNGRQCTAN GTECRSGWVG PNGGITNFDN FAFAMLTVFQ
     CITMEGWTDV LYWMNDAMGF ELPWVYFVSL VIFGSFFVLN LVLGVLSGEF SKEREKAKAR
     GDFQKLREKQ QLEEDLKGYL DWITQAEDID PENEEEGGEE GKRNTSMPTS ETESVNTENV
     SGEGETRGCC GSLWCWWRRR GAAKAGPSGC RRWGQAISKS KLSRRWRRWN RFNRRRCRAA
     VKSVTFYWLV IVLVFLNTLT ISSEHYNQPD WLTQIQDIAN KVLLALFTCE MLVKMYSLGL
     QAYFVSLFNR FDCFVVCGGI TETILVELEI MSPLGISVFR CVRLLRIFKV TRHWTSLSNL
     VASLLNSMKS IASLLLLLFL FIIIFSLLGM QLFGGKFNFD ETQTKRSTFD NFPQALLTVF
     QILTGEDWNA VMYDGIMAYG GPSSSGMIVC IYFIILFICG NYILLNVFLA IAVDNLADAE
     SLNTAQKEEA EEKERKKIAR KESLENKKNN KPEVNQVANS DNKVTIDDYR EEDEDKDPYP
     PCDVPVGEEE EEEEEDEPEV PAGPRPRRIS ELNMKEKIAP IPEGSAFFIL SKTNPIRVGC
     HKLINHHVFT NLILVFIMLS SAALAAEDPI RSHSFRNTML GYADYVFTGT FAFEIILKMT
     TFGAFLHKGA FCRNYFNLLD MLVVGVSLVS FGIQSSAISV VKILRVLRVL RPLRAINRAK
     GLKHVVQCVF VAIRTIGNIM IVTTLLQFMF ACIGVQLFKG KFYRCTDEAK SNPEECRGLF
     ILYKDGDVDS PVVRERIWQN SDFNFDNVLS AMMALFTVST FEGWPALLYK AIDSNGENIG
     PIYNHRVEIS IFFIIYIIIV AFFMMNIFVG FVIVTFQEQG EKEYKNCELD KNQRQCVEYA
     LKARPLRRYI PKNPYQYKFW YVVNSSPFEY MMFVLIMLNT LCLAMQHYEQ SKMFNDAMDI
     LNMVFTGVFT VEMVLKVIAF KPKGYFSDAW NTFDSLIVIG SIIDVALSEA DNSEESNRIS
     ITFFRLFRVM RLVKLLSRGE GIRTLLWTFI KSFQALPYVA LLIAMLFFIY AVIGMQMFGK
     VAMRDNNQIN RNNNFQTFPQ AVLLLFRCAT GEAWQEIMLA CLPGKLCDPE SDYNPGEEYT
     CGSNFAIVYF ISFYMLCAFL IINLFVAVIM DNFDYLTRDW SILGPHHLDE FKRIWSEYDP
     EAKGRIKHLD VVTLLRRIQP PLGFGKLCPH RVACKVSVLC LTPLGSPGSQ NFTQIPPPGN
     LEQANEELRA VIKKIWKKTS MKLLDQVVPP AGDDEVTVGK FYATFLIQDY FRKFKKRKEQ
     GLVGKYPAKN TTIALQAGLR TLHDIGPEIR RAISCDLQDD EPEETKREEE DDVFKRNGAL
     LGNHVNHVNS DRRDSLQQTN TTHRPLHVQR PSIPPASDTE KPLFPPAGNS VCHNHHNHNS
     IGKQVPTSTN ANLNNANMSK AAHGKRPSIG NLEHVSENGH HSSHKHDREP QRRSSVKRSD
     SGDEQLPTIC REDPEIHGYF RDPRCFGEQE YFSSEECYED DSSPTWSRQN YGYYSRYPGR
     NVDFERPRGY HHPQGFLEDD DSPICYDSRR SPRRRLLPPT PASHRRSSFN FECLRRQSSQ
     EEVPSSPTFP HRTALPLHLM QQQIMAVAGL DSSKAQKYSP SHSTRSWATP PATPPYRDWT
     PCYTPLIQVE QSEALDQMNG SLPSLHRSSW YTDEPDISYR TFTPASLTVP SSFRNKNSDK
     QRSADSLVEA VLISEGLGRY ARDPKFVSAT KHEIADACDL TIDEMESAAS TLLNGNVCPR
     ANGDVGPLSH RQDYELQDFG PGYSDEEPDP GRDEEDLADE MICITTL
//
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