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Database: UniProt
Entry: F7CIX9_CALJA
LinkDB: F7CIX9_CALJA
Original site: F7CIX9_CALJA 
ID   F7CIX9_CALJA            Unreviewed;      1739 AA.
AC   F7CIX9;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   25-OCT-2017, entry version 38.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1D {ECO:0000313|Ensembl:ENSCJAP00000051012};
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:ENSCJAP00000051012, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000051012, 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:ENSCJAP00000051012}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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:ENSCJAP00000051012}.
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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   Ensembl; ENSCJAT00000059560; ENSCJAP00000051012; ENSCJAG00000007392.
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:SF139; PTHR10037:SF139; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16885; CAC1F_C; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 3.
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    120    138       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    158    181       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    250    269       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    322    349       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    485    503       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    523    543       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    555    581       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    601    631       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    728    753       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    807    825       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    837    857       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    933    951       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1027   1050       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1184   1218       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      352    383       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1739 AA;  198187 MW;  0DAF99C1DB439EC8 CRC64;
     VLSTEFSKER EKAKARGDFQ KLREKQQLEE DLKGYLDWIT QAEDIDPENE EEGGEEGKRN
     TSMPTSETES VNTENVSGEA ETRGCCRSLC QAISKSKLSR RWRRWNRFNR RRCRAAVKSV
     TFYWLVIVLV FLNTLTISSE HYNQPDWLTQ IQDIANKVLL ALFTCEMLVK MYSLGLQAYF
     VSLFNRFDCF VVCGGITETI LVELEIMSPL GISVFRCVRL LRIFKVTRHW TSLSNLVASL
     LNSMKSIASL LLLLFLFIII FSLLGMQLFG GKFNFDETQT KRSTFDNFPQ ALLTVFQILT
     GEDWNAVMYD GIMAYGGPSS SGMIVCIYFI ILFICGNYIL LNVFLAIAVD NLADAESLNT
     AQKEEAEEKE RKKIARKESL ENKKNNKPEV NQVANSDNKV TIDDYREEDE DKDPYPPCDV
     PGDGEEQEGF ASYEPEVPAG PRPRRISELN MKEKIAPIPE GSAFFILSKT NPIRVGCHKL
     INHHIFTNLI LVFIMLSSAA LAAEDPIRSH SFRNTILGYF DYAFTAIFTV EILLKMTTFG
     AFLHKGAFCR NYFNLLDMLV VGVSLVSFGI QSSAISVVKI LRVLRVLRPL RAINRAKGLK
     HVVQCVFVAI RTIGNIMIVT TLLQFMFACI GVQLFKGKFY RCTDEAKSNP EECRGLFILY
     KDGDVDSPVV RERIWQNSDF NFDNVLSAMM ALFTVSTFEG WPALLYKAID SNGENVGPVY
     NHRVEISIFF IIYIIIVAFF MMNIFVGFVI VTFQEQGEKE YKNCELDKNQ RQCVEYALKA
     RPLRRYIPKN PYQYKFWYVV NSSPFEYMMF VLIMLNTLCL AMQHYEQSKM FNDAMDILNM
     VFTGVFTVEM VLKVIAFKPK GYFSDAWNTF DSLIVIGSII DVALSEADGD VSSSRVSVTF
     SLRGFRMMRL VKLLSRGEGI RTLLWTFIKS FQALPYVALL IAMLFFIYAV IGMQMFGKVA
     MKDNNQINRN NNFQTFPQAV LLLFRKRCAT GEAWQEIMLA CLPGKLCDPE SDYNPGEEYT
     CGSNFAIVYF ISFYMLCAFL IINLFVAVIM DNFDYLTRDW SILGPHHLDE FKRIWSEYDP
     EAKGRIKHLD VVTLLRRIQP PLGFGKLCPH RVACKRLVAM NMPLNSDGTV MFNATLFALV
     RTALKIKTEG NLEQANEELR AVIKKIWKKT SMKLLDQVVP PAGDDEVTVG KFYATFLIQD
     YFRKFKKRKE QGLVGKYPAK NTTIALQAGL RTLHDIGPEI RRAISCDLQD DEPEEAKREE
     EDDVFKRNGA LLGNHVNHVN SDRRDSLQQT NTTHRPLHVQ RPSIPPASDT EKPLFPPAGN
     SVCHNHHNHN SIGKQVPTST NANLNNANMS KAAHGKRPSI GNLEHVSENG HHSSHKHDRE
     PQRRSSVKRS DSGDEQLPTI CREDPEVHGY FRDPRCLGEQ EYFSSEECYE DDSSPTWSRQ
     NYGYYSRYPG RNMDFERPRG YHQPQGFLED DDSPICYDSR RSPRRRLLPP TPASHRRSSF
     NFECLRRQSS QEEIPSSPTF FPHRTALPLH LMQQQIMAVA GLDSSKAQKY SPSHSTRSWA
     TPPATPPYRD WTPCYTPLIQ VEQSEALDQV NGSLPSLHRS SWYTDEPDIS YRTFTPASLT
     IPSSFRNKNS DKQRSADSLV EAVLISEGLG RYARDPKFVS ATKYEIADAC DLTIDEMESA
     ASTLLNGNVR PRANGDVGPL SHQQDYELQD FGPGYSDEEP DLGRDEEDLA DEMICITTL
//
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