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Database: UniProt
Entry: G3RNE3_GORGO
LinkDB: G3RNE3_GORGO
Original site: G3RNE3_GORGO 
ID   G3RNE3_GORGO            Unreviewed;      2040 AA.
AC   G3RNE3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-SEP-2017, entry version 44.
DE   RecName: Full=Voltage-dependent P/Q-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1A {ECO:0000313|Ensembl:ENSGGOP00000017309};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000017309, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000017309, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000017309}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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-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}.
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:ENSGGOP00000017309}.
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DR   STRING; 9593.ENSGGOP00000017309; -.
DR   Ensembl; ENSGGOT00000027496; ENSGGOP00000017309; ENSGGOG00000008660.
DR   GeneTree; ENSGT00830000128247; -.
DR   InParanoid; G3RNE3; -.
DR   OMA; EKDCRGK; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   TreeFam; TF312805; -.
DR   Proteomes; UP000001519; Chromosome 19.
DR   Bgee; ENSGGOG00000008660; -.
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:0016049; P:cell growth; 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: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   InterPro; IPR005448; CACNA1A.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF249; PTHR10037:SF249; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01632; PQVDCCALPHA1.
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:UP000001519};
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:UP000001519};
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     42     65       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    157    179       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    308    327       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    339    359       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    434    456       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    510    534       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1028   1047       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1067   1088       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1100   1117       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1162   1184       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1274   1299       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1355   1373       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1385   1408       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1476   1494       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1571   1595       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1732   1766       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      530    566       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2040 AA;  233092 MW;  700257CF0BCDA468 CRC64;
     ILATVGTEFD LRTLRAVRVL RPLKLVSGIP SLQVVLKSIM KAMIPLLQIG LLLFFAILIF
     AIIGLEFYMG KFHTTCFEEG TDDIQGESPA PCGTEEPART CPNGTKCQPY WEGPNNGITQ
     FDNILFAVLT VFQCITMEGW TDLLYNSNDA SGNTWNWLYF IPLIIIGSFF MLNLVLGVLS
     GEFAKERERV ENRRAFLKLR RQQQIERELN GYMEWISKAE EVILAEDETD GEQRHPFDGA
     LRRTTIKKSK TDLLNPEEAE DQLADIASVG SPFARASIKS AKLENSTFFH KKERRMRFYI
     RRMVKTQAFY WTVLSLVALN TLCVAIVHYN QPEWLSDFLY YAEFIFLGLF MSEMFIKMYG
     LGTRPYFHSS FNCFDCGVII GSIFEVIWAV IKPGTSFGIS VLRALRLLRI FKVTKYWASL
     RNLVVSLLNS MKSIISLLFL LFLFIVVFAL LGMQLFGGQF NFDEGTPPTN FDTFPAAIMT
     VFQILTGEDW NEVMYDGIKS QGGVQGGMVF SIYFIVLTLF GNYTLLNVFL AIAVDNLANA
     QELTKDEQEE EEAANQKLAL QKAKEVAEVS PLSAANMSIA VKEQQKNQKP AKSVWEQRTS
     EMRKQNLLAS REALYNEMDP DERWKAAYTR HLRPDMKTHL DRPLVVDPQE NRNNNTNKSR
     AAEPTVDQRL GQQRAEDFLR KQARYHDRAR DPSGSAGLDA RRPWAGSQEA ELSREGPYGR
     ESDHHAREGS LEQPGFWEGE AERGKAGDPH RRHVHRQGGS RESRSGSPRT GADGEHRRHR
     AHRRRRHRHG APATYEGDAR REDKERRHRR RKGAIAHFRD EQDLMSKKKK ERQSHSCPIT
     SPHLIRSQGL IQMMRKYSQP GFHDTQLLKK HHNLASGKPS GESQDRFMGN QGCVVQGARH
     GGSIYPALFL VTGSHSAASR WTPNNPGNPS NPGPPKTPEN SLIVTNPSGT QTNSAKTARK
     PDHTTVDIPP ACPPPLNHTV VQVNKNANPD PLPKRGEDGP KPMPPYSSMF ILSTTNPLRR
     LCHYILNLRY FEMCILMVIA MSSIALAAED PVQPNAPRNN VLRYFDYVFT GVFTFEMVIK
     MIDLGLVLHQ GAYFRDLWNI LDFIVVSGAL VAFAFTGNSK GKDINTIKSL RVLRVLRPLK
     TIKRLPKLKA VFDCVVNSLK NVFNILIVYM LFMFIFAVVA VQLFKGKFFH CTDESKEFEK
     DCRGKYLLYE KNEVKARDRE WKKYEFHYDN VLWALLTLFT VSTGEGWPQV LKHSVDATFE
     NQGPSPGYRM EMSIFYVVYF VVFPFFFVNI FVALIIITFQ EQGDKMMEEY SLEKNERACI
     DFAISAKPLT RHMPQNKQSF QYRMWQFVVS PPFEYTIMAM IALNTIVLMM KFYGASVAYE
     NALRVFNIVF TSLFSLECVL KVMAFGILNY FRDAWNIFDF VTVLGSITDI LVTEFGNNFI
     NLSFLRLFRA ARLIKLLRQG YTIRILLWTF VQSFKALPYV CLLIAMLFFI YAIIGMQVFG
     NIGIDVEDED SDEDEFQITE HNNFTFFQAL MLLFRSATGE AWHNIMLSCL SGKPCDKNSG
     ILTRECGNEF AYFYFVSFIF LCSFLMLNLF VAVIMDNFEY LTRDSSILGP HHLDEYVRVW
     AEYDPAACGR IHYKDMYSLL RVISPPLGLG KKCPHRVACK VLTRNTRPTL FFHSAHFLST
     LSFLSSRLRG CKFLKRGADK QQMDAELRKE MMAIWPNLSQ KTLDLLVTPH KSTDLTVGKI
     YAAMMIMEYY RQSKAKKLQA MREEQDRTPL MFQRMEPPSP TQEGGPGQNA LPSTQLDPGG
     ALMAHESGLK ESPSWVTQRA QEMFQKTGTW SPEQGPPTDM PNSQPNSQSV EMREMGRDGY
     SDSEHYLPME GQGRAASMPR LPAENQRRRG RPRGNNLSVC TAHQPHDVFT LRAGPKSRRL
     YDYSWNLSPP DEILLHHQRR SVRRHWVYEG SLARTPRPGP GLGTDLSMTT QSGDLPSKER
     DQERGRPKDR KHRPPPPDKD RYAQERPDHG RARARDQRWS RSPSEGREHM AHRQVGAAAS
//
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