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Database: UniProt
Entry: F2UMP7_SALR5
LinkDB: F2UMP7_SALR5
Original site: F2UMP7_SALR5 
ID   F2UMP7_SALR5            Unreviewed;      1446 AA.
AC   F2UMP7;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-SEP-2017, entry version 34.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   ORFNames=PTSG_09464 {ECO:0000313|EMBL:EGD78396.1};
OS   Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC   Eukaryota; Choanoflagellida; Craspedida; Salpingoecidae; Salpingoeca.
OX   NCBI_TaxID=946362 {ECO:0000313|EMBL:EGD78396.1, ECO:0000313|Proteomes:UP000007799};
RN   [1] {ECO:0000313|Proteomes:UP000007799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q.,
RA   Gargeya S., Alvarado L., Berlin A., Chapman S.B., Chen Z.,
RA   Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heilman E., Heiman D., Howarth C., Mehta T., Neiman D., Pearson M.,
RA   Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA   White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Salpingoeca rosetta.";
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; GL832982; EGD78396.1; -; Genomic_DNA.
DR   RefSeq; XP_004989719.1; XM_004989662.1.
DR   EnsemblProtists; EGD78396; EGD78396; PTSG_09464.
DR   GeneID; 16070270; -.
DR   KEGG; sre:PTSG_09464; -.
DR   InParanoid; F2UMP7; -.
DR   KO; K04851; -.
DR   Proteomes; UP000007799; Unassembled WGS sequence.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
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   Complete proteome {ECO:0000313|Proteomes:UP000007799};
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:UP000007799};
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     16     36       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     48     65       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    113    132       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    358    376       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    388    407       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    427    448       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    483    509       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    521    540       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    560    587       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    732    752       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    764    787       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    808    836       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    929    955       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1011   1031       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1037   1059       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1136   1158       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1221   1245       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       12    201       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      357    594       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      696    960       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN     1007   1256       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN     1258   1328       GPHH. {ECO:0000259|Pfam:PF16905}.
FT   DOMAIN     1329   1404       Ca_chan_IQ. {ECO:0000259|Pfam:PF08763}.
SQ   SEQUENCE   1446 AA;  162270 MW;  2B3CF37251B20F4C CRC64;
     MTNDDLSSRE TDSLEYVFLA IFTLEALLKI IATGFLFCGP PSYLRNKWNI LDFIIVAVGL
     IGVVVEQSGS SVADVKALRA LRVLRPLRLI TSVQSLQIVL NSILLSIPAL ADVAMLLGFL
     IVIYAIIGLE FYRGVLNHQC FLPSSDVGAN VTADRYINNT PYFLAPDTAP CDPAGRGRVC
     STDGLCLAGS SPNSNITAFD HAGSFLKFDA AESMAEHEQN FFNSSAGADG NDGDDDDDDI
     DDDATTVLVL GLSLPSGNRD FVEAEPTEPI SNIRTRIMQK FAEQGEDRDK LMSFVLAHPH
     DGHILDETRT LGEQGVQVKS LREYNEILTM SQHNQHELLK PATVQMLSKL GAVVKSRWFN
     LVVTFMVLVN TVLLAVQTDA GATDEAAFAF TIVEASFVGL FVLEMLVKLA GLRPHMYFES
     KFNRFDLTVV LLSLLELILV HTTGLRSIGI SALRSLRLLR IFREMKQYWE DINDFVVSLL
     NSIASIVSLL LLILIYMVIV ALLGMQIFGG RFDFEDPKPR INFDDFFSAL LTVFIVIVGD
     DWNSVMYNGI LAYNGVNKDG WVAIVFFCVV VILGMFVLLN VFLAIAVKSL DDARDLKAAR
     DEHKERWKAE AAVSDESEDD REDRRRHRQY ANPLVGAAEQ EKEEVELQNT VLCDVDNVPL
     RKHLTRAVAN NKSLFCLGPR NSFRKFCNNI AYDNRFESVI LLLILISSAL LAAEDPVNLD
     AQINKDLETA DIFFTSVFSL EMALKIVALG FIPYITDPWN DLDAVVVLAS VVSLAISSDD
     AAVVRVLRVF RVLRPLRAIK RAPGLRKVVS CMVVSIKTIG NVFIVTFLLT FIYAIIGVQS
     FKECFGRCND PDVMFKSQCN GTFLVEDDAG LFSNATRAWS TPYFNFDNVG KGMLTLFTVS
     TLEGWIDVMN NAIDCTAENR QPERNNNPVA ALFFVTYVIL VAFFMLNIFV GYVIITFSSE
     GESYEAVDGL DKNQRKCLAF CLNAQPIRVH RPLYRAQISI FRFVSSKHFE WFIMAAIIGN
     SIVLLMAYEG MPSDYEMGLQ LCNIVFTGIF TVEALLKLFA LNPTGYFHDS WNFFDFIIVV
     GSLVDVFLSA TQSSGDSGVN IGFLRLFRVA RLLKLVSRGK GMKRLLWTFA KSFQSLPYVA
     ALIMMLFFVY AVIGMQLFAR TGFREDGDIN EHNNFRDFFG ALLLLFRCAT GENWQNMMRD
     IHLGPPNCDP ATEPGVCGSV VAVPFFCTFL VLCSFLILNL FVAVIMDNFE YLTQDNSLLG
     EHDLPQFIDR WSEFDPACTH RISHHDLMEL LRSEEPPLGF GRKCPPKTVY SKMMRLNVPL
     HLDGTVDFHA CLLAIVRNQL HIKTSYLDGS WEQRNYDLRK LLEKLYDPPK EQLDRMLPPP
     SKRNVTIGVL YAVYLLQEIY RENKRNAARQ ARETAEVLDA GSNEEKPQPS ENEEVEDDLR
     LVEHAF
//
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