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Database: UniProt
Entry: L7N2Z6_XENTR
LinkDB: L7N2Z6_XENTR
Original site: L7N2Z6_XENTR 
ID   L7N2Z6_XENTR            Unreviewed;      1959 AA.
AC   L7N2Z6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   25-OCT-2017, entry version 33.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=cacna1f {ECO:0000313|Ensembl:ENSXETP00000015655};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Silurana.
OX   NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000015655, ECO:0000313|Proteomes:UP000008143};
RN   [1] {ECO:0000313|Ensembl:ENSXETP00000015655}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000015655};
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L.,
RA   Blitz I.L., Blumberg B., Dichmann D.S., Dubchak I., Amaya E.,
RA   Detter J.C., Fletcher R., Gerhard D.S., Goodstein D., Graves T.,
RA   Grigoriev I.V., Grimwood J., Kawashima T., Lindquist E., Lucas S.M.,
RA   Mead P.E., Mitros T., Ogino H., Ohta Y., Poliakov A.V., Pollet N.,
RA   Robert J., Salamov A., Sater A.K., Schmutz J., Terry A., Vize P.D.,
RA   Warren W.C., Wells D., Wills A., Wilson R.K., Zimmerman L.B.,
RA   Zorn A.M., Grainger R., Grammer T., Khokha M.K., Richardson P.M.,
RA   Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
RN   [2] {ECO:0000313|Ensembl:ENSXETP00000015655}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2013) 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:ENSXETP00000015655}.
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DR   EMBL; AAMC01109254; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01109255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01109256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 8364.ENSXETP00000015655; -.
DR   PaxDb; L7N2Z6; -.
DR   Ensembl; ENSXETT00000015655; ENSXETP00000015655; ENSXETG00000007195.
DR   Xenbase; XB-GENE-1013840; cacna1f.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   InParanoid; L7N2Z6; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   Reactome; R-XTR-5576892; Phase 0 - rapid depolarisation.
DR   Reactome; R-XTR-5576893; Phase 2 - plateau phase.
DR   Proteomes; UP000008143; Unassembled WGS sequence.
DR   Bgee; ENSXETG00000007195; -.
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   GO; GO:0050856; P:regulation of T cell receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0043029; P:T cell homeostasis; IEA:InterPro.
DR   GO; GO:0007601; P:visual perception; IEA:InterPro.
DR   InterPro; IPR031688; CAC1F_C.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR030157; VDCC_L_a1F.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF184; PTHR10037:SF184; 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   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   Complete proteome {ECO:0000313|Proteomes:UP000008143};
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:UP000008143};
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     56     73       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     93    113       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    125    143       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    197    220       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    280    301       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    313    335       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    447    465       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    485    507       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    574    595       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    646    668       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    807    826       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    838    860       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    924    957       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    972    992       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    999   1020       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1026   1046       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1273   1291       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1365   1388       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1522   1556       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   1959 AA;  221754 MW;  B68F629415A55036 CRC64;
     STASSQAQKK RQYHSKHKNQ GTGGVHRSPR ALFCLYLSNP IRRACISIVE WKPFDILILM
     TIFANCVALG VYIPFPEDDS NIANHNLEQV EYIFLIIFTV ESFLKIIAYG LVLHPSAYIR
     NGWNLLDFVI VVIGLFSVIL EQFSHKQGDA HHMSGKPGGF DVKALRAFRV LRPLRLVSGV
     PSLHIVLNSI MKAMVPLLHI ALLVLFVIII YAIIGLELFI GRMHKTCFYI GSVLMLDLVS
     EEEPAPCAFS GHGRECLLNN TECRGKWEGP NGGITNFDNF FFAMLTVFQC ITMEGWTDVL
     YWMQDAMGYE LPWVYFVSLV IFGSFFVLNL VLGVLSGEFS KEREKAKARG DFQKLREKQQ
     MEEDLKGYLD WITQAEDLEP DQEIRDERHP SLPASETTSV NTENIDEEHA NCCARCLSKL
     SQTGCCRKIR RWNRAFRRKC RLAVKSVTFY WMVLLLVFLN TLTIASEHYQ QPDWLTEIQA
     YANKVLLSLF TLEMLLKMYS LGLHAYFVSF FNRFDCFVVC GGILETVLVE FDIMSPLGIS
     VLRCVRLLRI FKVTRHWASL SNLVASLLNS MKSIASLLLL LFLFIIIFSL LGMQLFGGKF
     NFDETQTKRS TFDTFPQALL TVFQILTGED WNAVMYDGIM AYGGPFFPGM LVCVYFIILF
     ICGNYILLNV FLAIAVDNLA DGDNINSKDK NRVNNKSEKK DENSVKVPCE EENENQEEEG
     SEACKCKRQF VTLIQVVSDI VPNHTLSLLA EEEEDDEGSL PESHLDKIAD FAPKEKVLPI
     PEGSAFFILS NTNLLRVGCH KLIHHHIFTN LILVFIILSS ISLAAEDPIR AHSFRNHILG
     YFDYAFTSIF TVEILLKMTA YGAFLHKGSF CRNWFNLLDL LVVSVSLISF GIHSSAISVV
     KILRVLRVLR PLRAINRAKG LKHVVQCVFV AIRTIGNIMI VTTLLQFMFA CIGVQLFKHV
     NLINCVIFSY DPLLFCTAVF YTCICLYGYA YILSSSFSCA CLCLFVLLPV PIALFAGLHF
     VGVMQPWPSC LLYTFLFHIL VSVLMLRTHK SILIMIYIHT PVYKFKTIVL QFGVAVIRIR
     RVGTHDFQRL NLPGCSPHVF KQKSFESRPL HTGLMVNKKI YLSKSFVGKH YFDCLYDVLF
     VISHDPFNFQ RSSNQLFYSI SVFRMDGMLV SLFIITMEHV RFKSENGSLN HGTPFGTTEL
     VACLLCVSPD FSLYQLFYPV FFPDTISPQS SEDSSRISIT FFRLFRVMRL VKLLSKGEGI
     RTLLWTFIKS FQALPYVALL IAMIFFIYAV IGMQTFGKIA MQDASQINRN NNFQTFPQAV
     LLLFRCATGE AWQDIMLASL PGKRCDSESD FGPGEEFTCG SNFAIVYFIS FFMLCAFLII
     NLFVAVIMDN FDYLTRDWSI LGPHHLDEFK RIWSEYDPEA KGRIKHLDVV TLLRRIQPPL
     GFGKLCPHRV ACKRLVAMNM PLNADGTVTF NATLFALVRT SLKIKTEGNL ETANEELRAV
     IKKIWKRTKQ KILDEVIPPP EEEEVTVGKF YATFLIQDYF RKFRRRKEKG LLGTENLPCN
     STTLQAGLRS LQDLGSEIRR VISTELEEEE DISGFRALGL QATENKISGS VVSLTNSIGG
     GREEQLPMSR RSSLINRSVG GSKDSLLVPP TPPPNVSSSM KRRQMTTRRI HLSIKLKTDI
     IFALNRRSSE GSGITPTVHE EEEESAAEHE LRSRPPSPGY DQSNEIQRWV FFDLCVVVII
     LKQAEHCACS MPRLLGICQS SLEESQQRSA SPQERVKVLP PPAAPPSSFR ANGTLEGTKS
     AFSIQCLKRQ GSCDDIPIPG TYHQNAPVYG STDSWQRNSY STNGTHSWAN PPKRGRLLYA
     PLILVEEDSA LPTIPCTRWY QEEDSKAPYC HYTQLRVPGQ RLAEKRGSAD SLVEAVLISE
     GLGLYARDPK FVAFAKREIA DACQMTIDEM ESAASDLLS
//
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