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Database: UniProt
Entry: A0A0D9R2C5_CHLSB
LinkDB: A0A0D9R2C5_CHLSB
Original site: A0A0D9R2C5_CHLSB 
ID   A0A0D9R2C5_CHLSB        Unreviewed;      1363 AA.
AC   A0A0D9R2C5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   25-APR-2018, entry version 25.
DE   RecName: Full=Voltage-dependent P/Q-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1A {ECO:0000313|Ensembl:ENSCSAP00000002764};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000002764, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000002764, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000002764}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (APR-2015) 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-1A
CC       gives rise to P and/or Q-type calcium currents. P/Q-type calcium
CC       channels belong to the 'high-voltage activated' (HVA) group and
CC       are blocked by the funnel toxin (Ftx) and by the omega-agatoxin-
CC       IVA (omega-Aga-IVA). They are however insensitive to
CC       dihydropyridines (DHP), and omega-conotoxin-GVIA (omega-CTx-GVIA).
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}.
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DR   EMBL; AQIB01141095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01141096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01141097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01141098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01141099; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01141100; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01141101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01141102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01141103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01141104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSCSAT00000004515; ENSCSAP00000002764; ENSCSAG00000006482.
DR   GeneTree; ENSGT00830000128247; -.
DR   OMA; NITTHEP; -.
DR   Proteomes; UP000029965; Chromosome 6.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:Ensembl.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IEA:Ensembl.
DR   GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
DR   GO; GO:0048266; P:behavioral response to pain; IEA:Ensembl.
DR   GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IEA:Ensembl.
DR   GO; GO:0030644; P:cellular chloride ion homeostasis; IEA:Ensembl.
DR   GO; GO:0021679; P:cerebellar molecular layer development; IEA:Ensembl.
DR   GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IEA:Ensembl.
DR   GO; GO:0021590; P:cerebellum maturation; IEA:Ensembl.
DR   GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
DR   GO; GO:0014051; P:gamma-aminobutyric acid secretion; IEA:Ensembl.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IEA:Ensembl.
DR   GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR   GO; GO:0051899; P:membrane depolarization; IEA:Ensembl.
DR   GO; GO:0050883; P:musculoskeletal movement, spinal reflex action; IEA:Ensembl.
DR   GO; GO:0032353; P:negative regulation of hormone biosynthetic process; IEA:Ensembl.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IEA:Ensembl.
DR   GO; GO:0007270; P:neuron-neuron synaptic transmission; IEA:Ensembl.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR   GO; GO:0043113; P:receptor clustering; IEA:Ensembl.
DR   GO; GO:0014056; P:regulation of acetylcholine secretion, neurotransmission; IEA:Ensembl.
DR   GO; GO:0050770; P:regulation of axonogenesis; IEA:Ensembl.
DR   GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IEA:Ensembl.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   GO; GO:0031335; P:regulation of sulfur amino acid metabolic process; IEA:Ensembl.
DR   GO; GO:0060024; P:rhythmic synaptic transmission; IEA:Ensembl.
DR   GO; GO:0021522; P:spinal cord motor neuron differentiation; IEA:Ensembl.
DR   GO; GO:0007416; P:synapse assembly; IEA:Ensembl.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:Ensembl.
DR   GO; GO:0019226; P:transmission of nerve impulse; IEA:Ensembl.
DR   GO; GO:0021750; P:vestibular nucleus development; IEA:Ensembl.
DR   Gene3D; 1.20.120.350; -; 3.
DR   InterPro; IPR005448; CACNA1A.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   Pfam; PF00520; Ion_trans; 3.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01632; PQVDCCALPHA1.
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:UP000029965};
KW   Ion channel {ECO:0000256|RuleBase:RU003808};
KW   Ion transport {ECO:0000256|RuleBase:RU003808};
KW   Membrane {ECO:0000256|SAAS:SAAS00085096, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00084820,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00084701,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU003808};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003808}.
FT   TRANSMEM    102    119       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    139    159       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    222    245       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    337    359       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    487    506       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    518    538       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    613    635       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    689    713       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1242   1261       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1281   1302       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1314   1331       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       98    370       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      486    722       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN     1243   1363       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   COILED      367    387       {ECO:0000256|SAM:Coils}.
FT   COILED      709    745       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1363 AA;  152841 MW;  5A8236D104EAA6D6 CRC64;
     MARFGDEMPA RYGGGGSGAA AGVVVGAGGG RGAGGSRQGG QPGAQRMYKQ SMAQRARTMA
     LYNPIPVRQN CLTVNRSLFL FSEDNVVRKY AKKITEWPPF EYMILATIIA NCIVLALEQH
     LPDDDKTPMS ERLDDTEPYF IGIFCFEAGI KIIALGFAFH KGSYLRNGWN VMDFVVVLTG
     ILATVGTEFD LRTLRAVRVL RPLKLVSGIP SLQVVLKSIM KAMIPLLQIG LLLFFAILIF
     AIIGLEFYMG KFHTTCFEEG TDDIQGESPA PCGTEEPART CPNGTKCQPY WEGPNNGITQ
     FDNILFAVLT VFQCITMEGW TDLLYNSNDA SGNTWNWLYF IPLIIIGSFF MLNLVLGVLS
     GEFAKERERV ENRRAFLKLR RQQQIERELN GYMEWISKAE EVILAEDETD GEQRHPFDAL
     RRTTIKKSKT DLLNPEEAED QLADIASVGS PFARASIKSA KLENSTFFHK KERRMRFYIR
     RMVKTQAFYW TVLSLVALNT LCVAIVHYNQ PEWLSDFLYY AEFIFLGLFM SEMFIKMYGL
     GTRPYFHSSF NCFDCGVIIG SIFEVIWAVI KPGTSFGISV LRALRLLRIF KVTKYWASLR
     NLVVSLLNSM KSIISLLFLL FLFIVVFALL GMQLFGGQFN FDEGTPPTNF DTFPAAIMTV
     FQILTGEDWN EVMYDGIKSQ GGVQGGMVFS IYFIVLTLFG NYTLLNVFLA IAVDNLANAQ
     ELTKDEQEEE EAANQKLALQ KAKEVAEVSP LSAANMSIAV KEQQKNQKPA KSVWEQRTSE
     MRKQNLLASR EALYNEMDPD ERWKAAYTRH LRPDMKTHLD RPLVVDPQEN RNNNTNKSRA
     AEPTVDQRLG QQRAEDFLRK QARYHDRARD PSGSAGLDAR RPWAGSQEAE LSREGPYGRE
     SDHHAREGSL EQPGFWEGEA ERGKAGDPHR RHVHRQGGSR ESRSGSPRTG ADGEPRRHRA
     HRRPGEEGPE DKAERRARHR EGSRPARGGE GEGEGPDGGE RRRRHRHGAP ATYEGDARRE
     DKERRHRRRK ENQGSGVPVS GPNLSTTRPI QQDLGRQDPP LAEDIDNMKN NKLATAESAG
     PHDSLGHAGL PQSPAKMGNS TDPGPTPAIP AMATNPQNAA SRRMPNNPGN PSNPGPPKTP
     ENSLIVTNPS GTQTNSAKTA RKPDHTTVDI PPACPPPLNH TIVQVNKNAN PDPLPKKEDE
     KKEEEEDDRG EDGPKPMPPY SSMFILSTTN PLRRLCHYIL NLRYFEMCIL MVIAMSSIAL
     AAEDPVQPNA PRNNVLRYFD YVFTGVFTFE MVIKMIDLGL VLHQGAYFRD LWNILDFIVV
     SGALVAFAFT GNSKGKDINT IKSLRVLRVL RPLKTIKRLP KLK
//
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