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Database: UniProt
Entry: H3ATD9_LATCH
LinkDB: H3ATD9_LATCH
Original site: H3ATD9_LATCH 
ID   H3ATD9_LATCH            Unreviewed;      2025 AA.
AC   H3ATD9;
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=CACNA1D {ECO:0000313|Ensembl:ENSLACP00000012910};
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:ENSLACP00000012910, ECO:0000313|Proteomes:UP000008672};
RN   [1] {ECO:0000313|Ensembl:ENSLACP00000012910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wild caught {ECO:0000313|Ensembl:ENSLACP00000012910};
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:ENSLACP00000012910}
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:ENSLACP00000012910}.
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DR   EMBL; AFYH01044127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01044128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01044129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01044130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01044131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01044132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01044133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01044134; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01044135; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AFYH01044136; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 7897.ENSLACP00000012910; -.
DR   Ensembl; ENSLACT00000013004; ENSLACP00000012910; ENSLACG00000011368.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   InParanoid; H3ATD9; -.
DR   OMA; LIQVERP; -.
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: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; 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: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      6     25       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     37     53       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    111    134       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    189    210       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    222    244       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    384    402       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    422    445       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    514    533       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    586    613       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    748    766       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    786    806       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    818    844       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    864    894       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    989   1014       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1068   1088       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1100   1119       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1210   1233       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1301   1325       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1459   1493       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      616    642       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2025 AA;  230934 MW;  864D1BD8D116E2E6 CRC64;
     ETVEYAFLII FTIETFLKII AYGLLMHPNA YVRNGWNLLD FIIVVVGLFS VVLEQVTTKE
     ADGGNHSSGK PGGFDVKALR AFRVLRPLRL VSGVPSLQVV LNSIIKAMVP LLHIALLVLF
     VIIIYAIIGL ELFIGKMHKT CFFTDTDIIA EEEPAPCEFS GNGRQCPNET NCKSGWAGPN
     GGITNFDNFA FAMLTVFQCI TMEGWTDVLY WVNDAIGCEW PWIYFVSLII LGSFFVLNLV
     LGVLSGEFSK EREKAKARGD FQKLREKQQL EEDLKGYLDW ITQAEDIDPE NEEDGDEEGK
     RNTSMPTSET ESVNTENVGG EGENAICCGS LCLLLWWKVV QSSRIGTRFR NIWNNRISKS
     KFSRRWRRWI RLSRRNCRAA VKSVTFYWLV IVLVFLNTLT ISSEHYNQPI WLTQTQDIAN
     KVLLAMFTCE MLVKMYSLGL QAYFVSLFNR FDCFVVCGGI IETILVEFEI MSPLGISVFR
     CVRLLRIFKV TRHWASLSNL VASLLNSMKS IASLLLLLFL FIIIFSLLGM QLFGGKFNFD
     ETHTKRSTFD NFPQSLLTVF QILTGEDWNA VMYDGIMAYG GPSSSGMIVC IYFIILFVCG
     NYILLNVFLA IAVDNLADAE SLNTAQKEAE EEKERKKSAR LHSIKNQYNE KPKHFKIFIF
     ENKVPVEELE DEEEDKDPYP PSDVPGFRRT DEDDEEEPEV PAGPRPQRLS ELIKKEKVTP
     IPEGSAFFIL SNTNPIRVGC HRLINHHIFT NLILVFIMLS SVSLAAEDPI RSHSFRNIIL
     GYFDYAFTAI FTVEILLKMT VAGAFLHKGS FCRNYFNLLD LLVVGVSLVS FGIQSSAISV
     VKILRVLRVL RPLRAINRAK GLKHVVQCVF VAIRTIGNIM IVTTLLQFMF ACIGVQLFKG
     KFYRCTDEAK QTPEECKGSY IVYKDGDVNQ PMIRERIWAN SDFNFDNVLS AMMALFTVST
     FEGWPALLYK AIDSNGENVG PIYNNRVEIS IFFIIYIIII AFFMMNIFVG FVIVTFQEQG
     EKEYENCELD KNQRQCVEYA LKARPLRRYI PKNPYQYKFW YVVNSTGFEY IMFVLIMLNT
     LCLAMQHYGQ SDLFNYAMDI LNMVFTGVFT VEMVLKLIAF KPRGYFSDAW NTFDSLIVIG
     SIVDVVLGEI DPTYGKTITP PTTTLKSSED SSRISITFFR LFRVMRLVKL LSRGEGIRTL
     LWTFIKSFQA LPYVALLIAM LFFIYAVIGM QVFGKVAMQD NTQINRNNNF QTFFQAVLLL
     FRCATGEAWQ EIMLACLPGK RCDPESDYNP GEEFTCGSNF AIVYFITFYM LCAFLIINLF
     VAVIMDNFDY LTRDWSILGP HHLDEFKRIW SEYDPEAKGR IKHLDVVTLL RRIQPPLGFG
     KLCPHRVACK RLVAMNMPLN SDGTVMFNAT LFALVRTALK IKTEGNLEQA NEELRAVIKK
     IWKRTSMKLL DQVVPPAGDD EVTVGKFYAT FLIQDYFRKF KKRKEQGLVG KHPTKNTTVA
     LQAGLRTLHD IGPEIRRAIS CDLQDEVPEE NNPEEEEDTY RRNGSVFGNH VNHVNSESRN
     SVQQTNATHR PLHVQRPSTP SAADAEKSTL FIKMGNSVPH NHQNHNCVGK PSPNSTNANL
     NNANISKIAN GKHPGPGHHE PASVNGFHLC SKNESEKDRN PSVKRDRTRY YETYIRSDSG
     DGHLPTICRE DPEADDYYNT SHYSGDQEYY SGDEYYEEDY TFSGNRQLYE YQERFQGNDL
     DCERPKGYHH PHGYYDDDDS QLYYESRRSP RRRLLPPTPT TNRRPSFNFE CLRRQSSQDD
     IPLSPSFHQR TALPLHLMQQ QVMAVAGLDS NRVQKHSPTR STRSWATPPA TPSNKDRSPY
     YTPLIRVDRA DSREHMNGSI PSMHRSSWYT DDLDTSYRTY TPANLTVPLD FRHKFTDKRG
     SADSLVEAVL ISEGLGRYAK DPKFVSATKH EIADACEMTI DEMESAASHL LNGNIKKGTN
     GDVFPVLSRQ DYELQDFGPG FSDEEPDSGR YEEDLADEMI CITTL
//
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