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Database: UniProt
Entry: H3BA90_LATCH
LinkDB: H3BA90_LATCH
Original site: H3BA90_LATCH 
ID   H3BA90_LATCH            Unreviewed;      2064 AA.
AC   H3BA90;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   25-OCT-2017, entry version 39.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1C {ECO:0000313|Ensembl:ENSLACP00000018811};
OS   Latimeria chalumnae (West Indian ocean coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000018811, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Ensembl:ENSLACP00000018811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Ensembl:ENSLACP00000018811};
RX   PubMed=9215903;
RA   Zardoya R., Meyer A.;
RT   "The complete DNA sequence of the mitochondrial genome of a 'living
RT   fossil,' the coelacanth (Latimeria chalumnae).";
RL   Genetics 146:995-1010(1997).
RN   [2] {ECO:0000313|Ensembl:ENSLACP00000018811}
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. 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:ENSLACP00000018811}.
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DR   EMBL; AFYH01019406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01019407; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01019408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01019409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01019410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01019411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01019412; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01019413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01019414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01019415; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 7897.ENSLACP00000018811; -.
DR   Ensembl; ENSLACT00000018944; ENSLACP00000018811; ENSLACG00000016558.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   InParanoid; H3BA90; -.
DR   OMA; PTTKINM; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   TreeFam; TF312805; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:Ensembl.
DR   GO; GO:0070509; P:calcium ion import; IEA:Ensembl.
DR   GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
DR   GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR   GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR   GO; GO:0003301; P:physiological cardiac muscle hypertrophy; IEA:Ensembl.
DR   GO; GO:0008016; P:regulation of heart contraction; IEA:Ensembl.
DR   InterPro; IPR031688; CAC1F_C.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16885; CAC1F_C; 2.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 5.
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:UP000008672};
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:UP000008672};
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      5     24       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     36     53       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    109    131       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    191    212       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    224    246       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    367    384       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    404    427       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    496    516       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    570    595       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    744    763       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    775    796       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    802    822       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    834    860       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    880    910       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1005   1032       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1083   1104       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1116   1136       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1148   1170       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1251   1269       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1346   1369       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1500   1534       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      598    624       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2064 AA;  233809 MW;  A2A86C6A2A6F26B2 CRC64;
     ERVEYLFLII FTVEAFLKVI GYGLLFHPNA YLRNGWNLLD FIIVVVGLFS AILEQATKAE
     GVNPIGGKAA GFDVKALRAF RVLRPLRLVS GVPSLQVVLN SIIKAMVPLL HIALLVLFVI
     IIYAIIGLEL FMGKMHKTCY FTRDSFPGIM AEEEPAPCAL DSSHGRQCRN GTVCKPGWVG
     PNDGITNFDN FAFAMLTVFQ CITMEGWTDV LYWVNDAIGS GWPWIYFVTL IIIGSFFVLN
     LVLGVLSGEF SKEREKAKAR GDFQKLREKQ QLEEDLKGYL DWITQAEDID PENEDEGLDE
     EKPRNMSMPA SETESVNIDN VGANDLEGEN CCTQLVHRIT KSKFSRYWRR WNRFCRRKCR
     AAVKSNVFYW LVIFLVFLNT LTISSEHYSQ PNWLTQVQDT ANKVLLALFT AEMLLKMYSL
     GLQAYFVSLF NRFDCFIVCG GILETILVET KIMSPLGISV LRCVRLLRIF KITRYWNSLS
     NLVASLLNSV RSIASLLLLL FLFIIIFSLL GMQLFGGKFN FDEMVTRRST FNNFPQALLT
     VFLILTGEDW NSVMYDGIMA YGGPSFPGML VCIYFIILFI CGNYILLNVF LAIAVDNLAD
     AESLTSAQKE EEEEKERKKM ARKMTDQTCL KFNEKPMEDE EKKEEKIELK SITVDGDAQP
     TTKIAVEDYQ LDGNEEKSSY PVNDFPGEEE EEEPEMPVGP RPRPLSELQL KEKAVPMPEA
     SAFFVFSSSN RFRIFCHRIV NDNIFTNLIL FFILLSSISL AAEDPVRHTS SRNQILFYFD
     IVFTIIFTIE ITLKILGYAD YVFTSIFTLE ITLKMTAYGA FLHKGSFCRN YFNILDLVVV
     SVSLISFGIQ SSAINVVKIL RVLRVLRPLR AINRAKGLKH VVQCVFVAIR TIGNIVIVTT
     LLQFMFACIG VQLFKGKFYR CSDGSKQTEA ECRGQFIVYK DGDVAHPQLE KREWNNSNFH
     FDDILHAMMA LFTVSTFEGW PTLLYQAIDS HTEDVGPIYN HRVEISIFFI IYIIIIAFFM
     MNIFVGFVIV TFQEQGEQEY KNCELDKNQR QCVEYALKAR PQRRYIPKNP YQYKVWYVVN
     SSYFEYLMFV LILLNTICLA MQHHGRSSSF NDAMDVLNMV FTGLFTVEMV LKLIAFKPRG
     YFSDPWNVFD FLIVIGSIID VILSEINHYF CDAWNTFDAL IVVGSIVDIA ITEVNPTEHA
     TSSPNAMDSE DNSRISITFF RLFRVMRLVK LLSRGEGIRT LLWTFIKSFQ ALPYVALLIV
     MLFFIYAVIG MQMFGKIALD DESQINRNNN FQTFPQAVLL LFRCATGEAW QEIMLACMPK
     RRCDPESESP NSSSDEDTSC GSSFAIFYFV SFYMLCAFLI INLFVAVIMD NFDYLTRDWS
     ILGPHHLDEF KRIWAEYDPE ANTHYEERSS CSAHRRGSPR LVVCPQTRLS QRLVSMNMPL
     NSDGTVMFNA TLFALVRTAL RIKTEGNLEQ ANEELRAIIK KIWKRTSMKL LDQVVPPAGD
     DEVTVGKFYA TFLIQEYFRK FKKRKEQGLV GKVPQKNALS LQAGLRTLHD IGPEIRRAIS
     GDLTAEEELD KAMKENASAA SEDDIFRRAG GLFGNHVNYY QSDGRGSFPQ TFTTQRPLHI
     NKTGTVPGDV ESPSHEKLVD STFTPSSYSS SGSNANINNA NNTALCHFPS PANFQSTVST
     VEGHTGTLPA TLLQHGSSWK LNAKSLTAQM LVYNFITKKG CGKSMKNTRV HHMVLCKTEP
     GRSNSGDSRL PIICREETSP EETYDENFNQ NTEYSSDQSI FSSEILSYQD NEHKQLTPSE
     DCEAEEEEKA RQSPKRGFLC AASLGRRRSS FHLECLKRQR TQGMDVNQRT ALPLHLLQHQ
     ALAVAGLSPL LRRSHSPTMF ARLCSTPPAT PCTQGRSRQQ QHHYQRVPTL RLEGVESCEK
     LNSSLPSVNC SSWYPEGGSS RKARPVSLTV PSHFSDVARQ CHGSASSLVE AVLISEGLGQ
     FAQDPKFIEA TTQELADACD MTIEEIENAA DNILNGNTKP SPNGNLLPFV NCRDLGPQDP
     GRDSTTEEEE EEEVEEVVVV VESL
//
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