ID G3R006_GORGO Unreviewed; 2146 AA.
AC G3R006;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Voltage-dependent P/Q-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000008481.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000008481.3, 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:ENSGGOP00000008481.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000008481.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry
CC of calcium ions into excitable cells and are also involved in a variety
CC of calcium-dependent processes, including muscle contraction, hormone
CC or neurotransmitter release, gene expression, cell motility, cell
CC division and cell death. The isoform alpha-1A gives rise to P and/or Q-
CC type calcium currents. {ECO:0000256|RuleBase:RU003808}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU003808}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1A subfamily. {ECO:0000256|ARBA:ARBA00037936}.
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DR EMBL; CABD030111848; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030111849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030111850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030111851; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030111852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030111853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030111854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030111855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030111856; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030111857; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSGGOT00000008714.3; ENSGGOP00000008481.3; ENSGGOG00000008660.3.
DR GeneTree; ENSGT00940000156518; -.
DR HOGENOM; CLU_000540_1_0_1; -.
DR Proteomes; UP000001519; Chromosome 19.
DR Bgee; ENSGGOG00000008660; Expressed in cerebellum and 2 other cell types or tissues.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR Gene3D; 1.10.287.70; -; 4.
DR Gene3D; 6.10.250.2180; -; 1.
DR Gene3D; 6.10.250.2500; -; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 4.
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 InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR45628; VOLTAGE-DEPENDENT CALCIUM CHANNEL TYPE A SUBUNIT ALPHA-1; 1.
DR PANTHER; PTHR45628:SF3; VOLTAGE-DEPENDENT P_Q-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1A; 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.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR602077-1};
KW Calcium channel {ECO:0000256|ARBA:ARBA00022673,
KW ECO:0000256|RuleBase:RU003808};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU003808}; Coiled coil {ECO:0000256|SAM:Coils};
KW Glycoprotein {ECO:0000256|PIRSR:PIRSR602077-3};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602077-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW ECO:0000256|RuleBase:RU003808}.
FT TRANSMEM 38..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 385..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 511..533
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 587..611
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1141..1160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1180..1201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1213..1230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1275..1297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1387..1412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1468..1486
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1498..1521
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1589..1607
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1685..1709
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1846..1880
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 716..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1887..1930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1942..2146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 607..643
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 725..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1027
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1942..1965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1996..2010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2021..2040
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2091..2107
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2108..2146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 565
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1358
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 2146 AA; 244514 MW; B4D40B6EA737BB5D CRC64;
MILATIIANC IVLALEQHLP DDDKTPMSER LDDTEPYFIG IFCFEAGIKI IALGFAFHKG
SYLRNGWNVM DFVVVLTGIL ATVGTEFDLR TLRAVRVLRP LKLVSGIPSL QVVLKSIMKA
MIPLLQIGLL LFFAILIFAI IGLEFYMGKF HTTCFEEGTD DIQGESPAPC GTEEPARTCP
NGTKCQPYWE GPNNGITQFD NILFAVLTVF QCITMEGWTD LLYNSNDASG NTWNWLYFIP
LIIIGSFFML NLVLGVLSGE FAKERERVEN RRAFLKLRRQ QQIERELNGY MEWISKAEEV
ILAEDETDGE QRHPFDALRR TTIKKSKTDL LNPEEAEDQL ADIASVGSPF ARASIKSAKL
ENSTFFHKKE RRMRFYIRRM VKTQAFYWTV LSLVALNTLC VAIVHYNQPE WLSDFLYYAE
FIFLGLFMSE MFIKMYGLGT RPYFHSSFNC FDCGVIIGSI FEVIWAVIKP GTSFGISVLR
ALRLLRIFKV TKYWASLRNL VVSLLNSMKS IISLLFLLFL FIVVFALLGM QLFGGQFNFD
EGTPPTNFDT FPAAIMTVFQ ILTGEDWNEV MYDGIKSQGG VQGGMVFSIY FIVLTLFGNY
TLLNVFLAIA VDNLANAQEL TKDEQEEEEA ANQKLALQKA KEVAEVSPLS AANMSIAVKE
QQKNQKPAKS VWEQRTSEMR KQNLLASREA LYNEMDPDER WKAAYTRHLR PDMKTHLDRP
LVVDPQENRN NNTNKSRAAE PTVDQRLGQQ RAEDFLRKQA RYHDRARDPS GSAGLDARRP
WAGSQEAELS REGPYGRESD HHAREGSLEQ PGFWEGEAER GKAGDPHRRH VHRQGGSRES
RSGSPRTGAD GEHRRHRAHR RPGEEGPEDK AERRARHREG SRPARGGEGE GEGPDGGERR
RRHRHGAPAT YEGDARREDK ERRHRRRKEN QGSGVPVSGP NLSTTRPIQQ DLGRQDPPLA
EDIDNMKNNK LATAESAVPH GSLGHAGLPQ SPAKMGNSTD PGPTPAIPAM ATNPQNNAAS
RWTPNNPGNP SNPGPPKTPE NSLIVTNPSG TQTNSAKTAR KPDHTTVDIP PACPPPLNHT
VVQVNKNANP DPLPKKEEEK KEEEEDDRGE DGPKPMPPYS SMFILSTTNP LRRLCHYILN
LRYFEMCILM VIAMSSIALA AEDPVQPNAP RNNVLRYFDY VFTGVFTFEM VIKMIDLGLV
LHQGAYFRDL WNILDFIVVS GALVAFAFTG NSKGKDINTI KSLRVLRVLR PLKTIKRLPK
LKAVFDCVVN SLKNVFNILI VYMLFMFIFA VVAVQLFKGK FFHCTDESKE FEKDCRGKYL
LYEKNEVKAR DREWKKYEFH YDNVLWALLT LFTVSTGEGW PQVLKHSVDA TFENQGPSPG
YRMEMSIFYV VYFVVFPFFF VNIFVALIII TFQEQGDKMM EEYSLEKNER ACIDFAISAK
PLTRHMPQNK QSFQYRMWQF VVSPPFEYTI MAMIALNTIV LMMKFYGASV AYENALRVFN
IVFTSLFSLE CVLKVMAFGI LNYFRDAWNI FDFVTVLGSI TDILVTEFGN NFINLSFLRL
FRAARLIKLL RQGYTIRILL WTFVQSFKAL PYVCLLIAML FFIYAIIGMQ VFGNIGIDVE
DEDSDEDEFQ ITEHNNFRTF FQALMLLFRS ATGEAWHNIM LSCLSGKPCD KNSGILTREC
GNEFAYFYFV SFIFLCSFLM LNLFVAVIMD NFEYLTRDSS ILGPHHLDEY VRVWAEYDPA
AWGRMPYLDM YQMLRHMSPP LGLGKKCPAR VAYKRLLRMD LPVADDNTVH FNSTLMALIR
TALDIKIAKG GADKQQMDAE LRKEMMAIWP NLSQKTLDLL VTPHKSTDLT VGKIYAAMMI
MEYYRQSKAK KLQAMREEQD RTPLMFQRME PPSPTQEGGP GQNALPSTQL DPGGALMAHE
SGLKESPSWV TQRAQEMFQK TGTWSPEQGP PTDMPNSQPN SQSVEMREMG RDGYSDSEHY
LPMEGQGRAA SMPRLPAENQ TISDTSPMKR SASVLGPKAR RLDDYSLERV PPEENQRHHQ
RRRDRSHRAS ERSLGRYTDV DTGLGTDLSM TTQSGDLPSK ERDQERGRPK DRKHRQHHHH
HHHHHPPPPD KDRYAQERPD HGRARARDQR WSRSPSEGRE HMAHRQ
//
