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Database: UniProt
Entry: H2T0E9_TAKRU
LinkDB: H2T0E9_TAKRU
Original site: H2T0E9_TAKRU 
ID   H2T0E9_TAKRU            Unreviewed;      1691 AA.
AC   H2T0E9;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   25-OCT-2017, entry version 39.
DE   RecName: Full=Voltage-dependent T-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae;
OC   Takifugu.
OX   NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000018137, ECO:0000313|Proteomes:UP000005226};
RN   [1] {ECO:0000313|Ensembl:ENSTRUP00000018137}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21551351;
RA   Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A.,
RA   Hosoya S., Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT   "Integration of the genetic map and genome assembly of fugu
RT   facilitates insights into distinct features of genome evolution in
RT   teleosts and mammals.";
RL   Genome Biol. Evol. 3:424-442(2011).
RN   [2] {ECO:0000313|Ensembl:ENSTRUP00000018137}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-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. This channel gives
CC       rise to T-type calcium currents. T-type calcium channels belong to
CC       the "low-voltage activated (LVA)" group and are strongly blocked
CC       by nickel and mibefradil. A particularity of this type of channels
CC       is an opening at quite negative potentials, and a voltage-
CC       dependent inactivation. T-type channels serve pacemaking functions
CC       in both central neurons and cardiac nodal cells and support
CC       calcium signaling in secretory cells and vascular smooth muscle.
CC       They may also be involved in the modulation of firing patterns of
CC       neurons which is important for information processing as well as
CC       in cell growth processes. {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:ENSTRUP00000018137}.
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DR   Ensembl; ENSTRUT00000018213; ENSTRUP00000018137; ENSTRUG00000007344.
DR   GeneTree; ENSGT00830000128242; -.
DR   OMA; DSDANIC; -.
DR   Proteomes; UP000005226; Unplaced.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0008332; F:low voltage-gated calcium channel activity; IEA:InterPro.
DR   GO; GO:0070509; P:calcium ion import; IEA:InterPro.
DR   GO; GO:0030317; P:flagellated sperm motility; IEA:InterPro.
DR   GO; GO:0019228; P:neuronal action potential; IEA:InterPro.
DR   InterPro; IPR030162; CACNA1I.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR005445; VDCC_T_a1.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF209; PTHR10037:SF209; 2.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01629; TVDCCALPHA1.
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:UP000005226};
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:UP000005226};
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      7     27       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     47     68       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     80     99       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    135    159       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    281    303       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    309    334       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    578    596       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    608    634       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    699    721       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    777    799       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1105   1123       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1143   1164       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1176   1200       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1240   1262       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1302   1321       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1333   1352       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1549   1576       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1645   1666       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        6    345       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      577    804       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN     1103   1279       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN     1493   1677       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   COILED     1370   1394       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1691 AA;  191739 MW;  2A9A685B8159E8E8 CRC64;
     LRTVSTWFER ITIMVILLNC VTLGMYQPCE NIDCASDHCQ ILQAFDAFIY IFFALEMVVK
     MVALGIFGRR CYLGDTWNRL DFFIVMAGMV EYSLDLQNIN LSAIRTVRVL RPLKAINRVP
     SLRILVNLLL DTLPMLGNVL LLCFFVFFIF GIIGVQLWAG LLRNRCYLEE NFTLVKPGMT
     LPPPYYQPEE DDERPFICSL PSDNGIMSCS DVPARREGGR TCCLDKEDAF YRQALGLSPE
     PLANGSGEAT GLCINWNQYY TRCHTGSSNP HKGAISFDNI VYAWIVIFQV ITLEGWVEIM
     YYVMDAHSFY NFIYFILLII IGSFFMINLC LVVIATQFSE TKQREHQLMQ EQRAQCLSSS
     TLASMAEPGD CYEEIFQLVC HVLRKAKRRS AALYYTLRGK PLPAGWSRSN RHGGGNVNSE
     HQFRHPRCEY IIGFDSSKKK QGWLQTRRLF PAPRPNGSNT CLATRFITCL CVSVASHCPH
     QSRPDHSSQP SANPISLAVP QGPDDCPICA QTEGTRAQGD GFSGKDQEED AVKEMDKEES
     RQEENVGVKR RKRTCFRYLR DIWNGMRRKL WGIVESKYFS RGIMIAILIN TISMGIEHHN
     QPDELTNVLE ICNIVFTSMF TLEMILKLTA FGFFEYLRNP YNIFDGIIVI ISVCEIIGQA
     DGGLSVLRTF RLLRVIKLVR FMPALRRQLV VLMKTMDNVA TFCMLLMLFI FIFSILGMHI
     FGCKFSLKTE AGDTVPDRKN FDSLLWAIVT VFQILTQEDW NVVLYNGMVS TSPCASLYFV
     ALMTFGNYVL FNLLVAILVE GFQAEGDANR SYSDDDRSSC NFDEDVQGYH GNKSIKEATS
     FFLFFFSLRN KMSTSAIGSL RPIPEMRLRC YPKISTLTPN GHLDLPPALI HGETMTFALG
     SRKNSVISLG RANLEQKAVY PGYHNWGRPL PPHPQALWAR RSSWNSLGRC RPCSSSSPSD
     EEQSLLSPPA SHSLHPPCTM LPGHFVPRRD RRALSLELPH LLQVPPHLAP PSRHLSGGGL
     GSLSGLGDLH QDCNGKTPLS QVLQPRPRHS GEQAEALQSL CFRIQKMLEV YRPDWCETRE
     DWSVFLFSPQ NKFRQMCQSI IAHKLFDYVV LVFIFSNCIT VALERPKILQ GSLERVFLTV
     SNYIFTAIFV GEMTLKVVSM GLYMGEQAYL RSSWNVLDGF LVFVSLVDIV VSMAGGAKIL
     GVLRVLRLLR TLRPLRTRVI SRAPGLKLVV ETLITSLKPI GNIVLICCAF FIIFGILGVQ
     LFKGKFFYCL GPDVKNITNK SDCLQANYKW VHHKYKIEDA RLSLVCVFMG VGAVPLLTFS
     FQSLDLVLKY CNYFFTSTFV LESILKLIAF GFRRFFKDSC LEDFYKFLQA NQTRERERER
     ERERERERER ERREMIYGRG SSVDQRPKEE DKDTPAYPSH FAGRRNHLTG ILLHMMNLFR
     ALWGGALLHT HQKCILDSDA NICSLALVIL QPSRGSWRGA APSATPVCVC CRWNQLDLAI
     VLLSVMGITL EEIEISAALP INPTIIRIMR VLRIARVLKL LKMATGMRAL LDTVVQALPQ
     VGNLGLLFML LFFIYAALGV ELFGELVCNA DYPCEGMSRH ATFENFGMAF LTLFQVSTGD
     NWNGIMKDTL RECPPDHNTE FISPMYFVSF VLTAQFVLIN VVVAVLMKHL DDSNKEAQEE
     AEMDAEIELE L
//
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