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Database: UniProt
Entry: F7I2L9_CALJA
LinkDB: F7I2L9_CALJA
Original site: F7I2L9_CALJA 
ID   F7I2L9_CALJA            Unreviewed;      2138 AA.
AC   F7I2L9;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-SEP-2017, entry version 41.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1D {ECO:0000313|Ensembl:ENSCJAP00000014011};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000014011, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000014011, ECO:0000313|Proteomes:UP000008225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000014011}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUN-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:ENSCJAP00000014011}.
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DR   EMBL; ACFV01039409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01039410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01039411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01039412; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01039413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01039414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01039415; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01039416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01039417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ACFV01039418; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_002758480.1; XM_002758434.3.
DR   Ensembl; ENSCJAT00000014758; ENSCJAP00000014011; ENSCJAG00000007392.
DR   GeneID; 100397940; -.
DR   CTD; 776; -.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   Proteomes; UP000008225; Chromosome 15.
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; 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:SF239; PTHR10037:SF239; 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:UP000008225};
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:UP000008225};
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    130    147       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    167    187       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    199    218       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    271    294       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    350    371       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    383    405       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    523    541       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    561    584       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    653    672       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    725    752       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    887    905       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    925    945       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    957    983       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1003   1033       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1130   1155       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1209   1227       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1239   1259       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1334   1352       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1426   1449       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1583   1617       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      755    786       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2138 AA;  242683 MW;  52CD934F3EC71892 CRC64;
     MMMMMMMKKM QHQRQQQADH ANEANYARGT RLPLSGEGPT SQPNSSKQTV LSWQAAIDAA
     RQAKAAQTMS TSAPPPVGSL SQRKRQQYAK SKKQGNSSNS RPARALFCLS LNNPIRRACI
     SIVEWKPFDI FILLAIFANC VALAIYIPFP EDDSNSTNHN LEKVEYAFLI IFTVETFLKI
     IAYGLLLHPN AYVRNGWNLL DFVIVIVGLF SVILEQLTKE TEGGNHSSGK SGGFDVKALR
     AFRVLRPLRL VSGVPSLQVV LNSIIKAMVP LLHIALLVLF VIIIYAIIGL ELFIGKMHKT
     CFFADSDIVA EEDPAPCAFS GNGRQCTANG TECRSGWVGP NGGITNFDNF AFAMLTVFQC
     ITMEGWTDVL YWMNDAMGFE LPWVYFVSLV IFGSFFVLNL VLGVLSGEFS KEREKAKARG
     DFQKLREKQQ LEEDLKGYLD WITQAEDIDP ENEEEGGEEG KRNTSMPTSE TESVNTENVS
     GEAETRGCCR SLCQAISKSK LSRRWRRWNR FNRRRCRAAV KSVTFYWLVI VLVFLNTLTI
     SSEHYNQPDW LTQIQDIANK VLLALFTCEM LVKMYSLGLQ AYFVSLFNRF DCFVVCGGIT
     ETILVELEIM SPLGISVFRC VRLLRIFKVT RHWTSLSNLV ASLLNSMKSI ASLLLLLFLF
     IIIFSLLGMQ LFGGKFNFDE TQTKRSTFDN FPQALLTVFQ ILTGEDWNAV MYDGIMAYGG
     PSSSGMIVCI YFIILFICGN YILLNVFLAI AVDNLADAES LNTAQKEEAE EKERKKIARK
     ESLENKKNNK PEVNQVANSD NKVTIDDYRE EDEDKDPYPP CDVPVGEEEE EEEEDEPEVP
     AGPRPRRISE LNMKEKIAPI PEGSAFFILS KTNPIRVGCH KLINHHIFTN LILVFIMLSS
     AALAAEDPIR SHSFRNTILG YFDYAFTAIF TVEILLKMTT FGAFLHKGAF CRNYFNLLDM
     LVVGVSLVSF GIQSSAISVV KILRVLRVLR PLRAINRAKG LKHVVQCVFV AIRTIGNIMI
     VTTLLQFMFA CIGVQLFKGK FYRCTDEAKS NPEECRGLFI LYKDGDVDSP VVRERIWQNS
     DFNFDNVLSA MMALFTVSTF EGWPALLYKA IDSNGENVGP VYNHRVEISI FFIIYIIIVA
     FFMMNIFVGF VIVTFQEQGE KEYKNCELDK NQRQCVEYAL KARPLRRYIP KNPYQYKFWY
     VVNSSPFEYM MFVLIMLNTL CLAMQHYEQS KMFNDAMDIL NMVFTGVFTV EMVLKVIAFK
     PKGYFSDAWN TFDSLIVIGS IIDVALSEAD NSEESNRISI TFFRLFRVMR LVKLLSRGEG
     IRTLLWTFIK SFQALPYVAL LIAMLFFIYA VIGMQMFGKV AMKDNNQINR NNNFQTFPQA
     VLLLFRCATG EAWQEIMLAC LPGKLCDPES DYNPGEEYTC GSNFAIVYFI SFYMLCAFLI
     INLFVAVIMD NFDYLTRDWS ILGPHHLDEF KRIWSEYDPE AKGRIKHLDV VTLLRRIQPP
     LGFGKLCPHR VACKRLVAMN MPLNSDGTVM FNATLFALVR TALKIKTEGN LEQANEELRA
     VIKKIWKKTS MKLLDQVVPP AGDDEVTVGK FYATFLIQDY FRKFKKRKEQ GLVGKYPAKN
     TTIALQAGLR TLHDIGPEIR RAISCDLQDD EPEEAKREEE DDVFKRNGAL LGNHVNHVNS
     DRRDSLQQTN TTHRPLHVQR PSIPPASDTE KPLFPPAGNS VCHNHHNHNS IGKQVPTSTN
     ANLNNANMSK AAHGKRPSIG NLEHVSENGH HSSHKHDREP QRRSSVKRSD SGDEQLPTIC
     REDPEVHGYF RDPRCLGEQE YFSSEECYED DSSPTWSRQN YGYYSRYPGR NMDFERPRGY
     HQPQGFLEDD DSPICYDSRR SPRRRLLPPT PASHRRSSFN FECLRRQSSQ EEIPSSPTFF
     PHRTALPLHL MQQQIMAVAG LDSSKAQKYS PSHSTRSWAT PPATPPYRDW TPCYTPLIQV
     EQSEALDQVN GSLPSLHRSS WYTDEPDISY RTFTPASLTI PSSFRNKNSD KQRSADSLVE
     AVLISEGLGR YARDPKFVSA TKYEIADACD LTIDEMESAA STLLNGNVRP RANGDVGPLS
     HQQDYELQDF GPGYSDEEPD LGRDEEDLAD EMICITTL
//
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