GenomeNet

Database: UniProt
Entry: I3MW93_ICTTR
LinkDB: I3MW93_ICTTR
Original site: I3MW93_ICTTR 
ID   I3MW93_ICTTR            Unreviewed;      1981 AA.
AC   I3MW93;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-SEP-2017, entry version 36.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1F {ECO:0000313|Ensembl:ENSSTOP00000016388};
OS   Ictidomys tridecemlineatus (Thirteen-lined ground squirrel)
OS   (Spermophilus tridecemlineatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha;
OC   Sciuridae; Xerinae; Marmotini; Ictidomys.
OX   NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000016388, ECO:0000313|Proteomes:UP000005215};
RN   [1] {ECO:0000313|Ensembl:ENSSTOP00000016388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Spermophilus tridecemlineatus.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSTOP00000016388}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAY-2012) 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:ENSSTOP00000016388}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AGTP01099242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 43179.ENSSTOP00000016388; -.
DR   Ensembl; ENSSTOT00000028916; ENSSTOP00000016388; ENSSTOG00000023000.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   InParanoid; I3MW93; -.
DR   OMA; LNQTECR; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   TreeFam; TF312805; -.
DR   Proteomes; UP000005215; Unassembled WGS sequence.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:Ensembl.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IEA:InterPro.
DR   GO; GO:0050908; P:detection of light stimulus involved in visual perception; IEA:Ensembl.
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   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:SF234; PTHR10037:SF234; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005215};
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:UP000005215};
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     96    113       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    133    152       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    164    180       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    235    258       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    314    335       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    347    369       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    528    546       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    561    579       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    657    676       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    726    748       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    874    892       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    912    932       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    990   1019       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1074   1095       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1115   1142       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1183   1210       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1222   1241       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1328   1346       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1419   1443       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1577   1611       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      805    828       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1981 AA;  221269 MW;  4511FD3B057B6422 CRC64;
     MSESEVGKDT TPDPSPANGT GPGPDWGICP GPPVVEGDTG GASGLGTPRR KAQHNKHKTV
     AVASAQRSPR ALFCLTLANP LRRSCISIVE WKPFDILILL TIFANCVALG VYIPFPEDDS
     NTANHNLEQV EYVFLVIFTV ETVLKIVAYG LVLHPSAYIR NGWNLLDFII VVVGLFSVLL
     EQGSGRPGEA PHTKPGGFDV KALRAFRVLR PLRLVSGVPS LHIVLNSIMK ALVPLLHIAL
     LVLFVIIIYA IIGLELFLGR MHKTCYFLGS DVEAEEDPSP CASSGSGRAC TLNQTECRGR
     WPGPNGGITN FDNFFFAMLT VFQCITMEGW TDVLYWMQDA MGHELPWLYF VSLVIFGSFF
     VLNLVLGVLS GEFSKEREKA KARGDFQKLR EKQQMEEDLR GYLDWITQAE ELDLEDPSAD
     GNFGSMAEEG RAGNRPHLAE LTNRRRGRLR WFRHSTRSTH STSSHASLPA SDTGSMAETP
     ADEEEEEGAL ASCARCLNKI MKTSVCRRFR RANRGLRAHC RKAVKSNACY WAVLLLVFLN
     TLTIASEHHG QPVWLTRIQE YANKVLLCLF TVEMLLKLYG LGPSVYVASF FNRFDCFVVC
     GGILETTLVE VGAMQPLGIS VLRCVRLLRI FKVTRHWASL SNLVASLLNS MKSIASLLLL
     LFLFIIIFSL LGMQLFGGKF NFDQTQTKRS TFDTFPQALL TVFQILTGED WNVVMYDGIM
     AYGGPFFPGM LVCVYFIILF ICGNYILLNV FLAIAVDNLA SGDAGTATDK SREKSSEESV
     PKENGILVPG GENEEQEGTK TEEAVPGVEE EEEEDEEEEE EEEEEEAGAG HEELLQEVVP
     KEKVMPIPEG SAFFCLSQTN PLRKACHTLI HHHIFTNLIL VFIILSSVSL AAEDPIRAHS
     FRNHILGYFD YAFTSIFTVE ILLKMTVFGA FLHRGSFCRS WFNLLDLLVV SVSLISFGIH
     SSAISVVKIL RVLRVLRPLR AINRAKGLKH VVQCVFVAIR TIGNIMIVTT LLQFMFACIG
     VQLFKGKFYS CTDEAKHTPK ECKGTFLVYP DGDVSRPLVR ERLWVNSDFN FDNVLSAMMA
     LFTVSTFEGW PALLYKAIDA HAENRGPIYN YRVEISVFFI VYIIIIAFFM MNIFVGFVII
     TFRAQGEQEY QNCELDKNQR QCVEYALKAQ PLRRYIPKNP HQYRVWAAVN SAAFEYLMFL
     LILLNTVALA MQHYEQTAPF NYAMDILNMV FTGLFTIEMV LKIIAFKPKH YFTDAWNTFD
     ALIVVGSVVD IAVTEVNNGG HLGESSEDSS RISITFFRLF RVMRLVKLLS KGEGIRTLLW
     TFIKSFQALP YVALLIAMIF FIYAVIGMQM FGKVALQDGT QINRNNNFQT FPQAVLLLFR
     CATGEAWQEI MLASLPGSRC DPESDYGPGE EFTCGSNFAI AYFISFFMLC AFLIINLFVA
     VIMDNFDYLT RDWSILGPHH LDEFKRIWSE YDPGAKGRIK HLDVVALLRR IQPPLGFGKL
     CPHRVACKRL VAMNVPLNSD GTVTFNATLF ALVRTSLKIK TEGNLEQANQ ELRMVIKKIW
     KRIKQKLLDE IIPPPDEEEV TVGKFYATFL IQDYFRKFRR RKEKGLLGTE APSSTSSVLQ
     AGLRSLQDLG PEIRQALTCD TDEEGEEEEE GQEGEEEAEK SCDSPQAPME SQPPSRRNSR
     ISVSLPVGSK NPDSLSLGPS DDDGRASNSR QPSVNPAGSH NQRRSSGVFM FTIPEEGSSQ
     PKETKEQNKQ VEEEEIPDRL SYLDEQREAP PHPALLPPHQ PQRYVNGHNA PRRRLLPPTP
     AGRKPSFTIQ CLQRQGSCED LPIPGTYHRG RNTGPSRAQG SWATPPQRGR LLYAPLLLVE
     EGAAGEGYLG KSSGPLRTFT CLHVPGSRSD PSHGKRGSAD SLVEAVLISE GLGLFARDPR
     FVALAKKEIA DACRLTLDEM DSAASDLLAQ GTSSLYSDEE SILSRFDEED LGDEMACVHA
     L
//
DBGET integrated database retrieval system