ID H3D164_TETNG Unreviewed; 1848 AA.
AC H3D164;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Voltage-dependent P/Q-type calcium channel subunit alpha-1A {ECO:0000256|ARBA:ARBA00039688};
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.1 {ECO:0000256|ARBA:ARBA00041622};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000014250.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000014250.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 Ensembl; ENSTNIT00000014448.1; ENSTNIP00000014250.1; ENSTNIG00000011310.1.
DR GeneTree; ENSGT00940000156518; -.
DR HOGENOM; CLU_000540_1_0_1; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
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; 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 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:UP000007303};
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 221..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 496..515
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 622..644
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 697..723
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1109..1127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1147..1167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1179..1197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1239..1261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1351..1376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1430..1447
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1459..1482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1542..1571
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1643..1667
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1821..1848
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 719..755
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 920..979
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1005
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 315
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 676
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1322
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 1848 AA; 210659 MW; 0CA2F55DE5C8FD2E CRC64;
MARFGDELPN RYGGGGGGGS GGAGGQGGPG RGGSRQGGAP GAQRMYKQSM AQRARTMALY
NPIPVRQNCL TVNRSLFLFS EDNVVRKYAK KITEWPYPFM SIRTAWWFGF CLVWSSHLHL
SAAQLTPLSE RLEETEHYFI AIFCFESGIK ILALGFALHK GSYLRNGWNV MDFVVVLTGI
LSSVKSQFDL RTLRAVRVLR PLKLVSGIPS LQVVLKSIMK AMIPLLQIGL LLFVAILMFA
IIGLEFYMGK FHKTCYHEVT HEIVDNLPCG KALPSRLCPN GTVCLSGWLG PNFGITQFDN
ILFAVLTVFQ CITMEGWTEM LYYSNDVEGS TWNWMYYIPL IIIGSFFMLN LVLGVLSGEF
AKERERVENR SEFLKLRRQQ QIERELNGYL EWICRAEEVI LAEDDGTGNF DGDSPALLFH
FSRSGSRRTM RSKNNKTELL NPEEGEDNMG DAIDVEVMMG KGFARSSIKS GKEGSNYSKK
ERRLRFFIRK IVKTQAFYWT VLCLVGLNTI CVAAVHYDQP DLLSDFLFYA EFIFLGLFMS
EMLIKMYGLG IQPYFHSSFN CFDCVVILGS IFEVVWATIK PGTSFGISVL RALRLLRIFK
VTKYWAPLRN LVVSLLNSMK SIISLLFLLF LFIVVFALLG MQLFGGQFNF EGGTPPTNFD
TFAAAIMTVF QILTGEDWNM VMYNGIESQG GVNDKGMIFS IFFIVLTLFG NYTLLNVFLA
IAVDNLANAQ ELTKDEEEQE EAANQKTALQ KAKEVAEVSP LSAANLSIAA RNADKRTHQD
DVHKIPAAPQ EQQKNHIKGN KSVWEQRTSE IRRQNLMTSR EALYNELEQD DWKVSYPRKG
RGNMKTHLDR PLVVNPQDNR NNNTNRTQPE RERGADNEGA GPQAETRIEH ELSCTSLGNV
EGQQVPERHG HRSHCHRHRT RESREAGSTS PHHSDGAEGS EPRRPRQHHR AAKEGEEGRR
RRSKRAEERA RKPPREREGG AEGIAMATRG GDRGHRSRKE HHGACPNLST TRPIQQYNED
LDNLRNNSKL ASAQEHPYTL APDHPDHVNN LLNCCDTDTH TLLHSMDSLI LTSMAKNGPK
PMPPYSSCFI LSTTNPFRKC CHYILTLKYF EFSILSVIAM SSIALAAEDP VSPDSPRNHV
LRYFDYIFTG VFTFEMLIKM VVLGLFLHQG SYFRDLWNIL DFIVVSGALV AFAFTITSGK
QRHDLGSDRD FSPTRPQRTK XLPKLKAVFD CVVNSLKNVL NILIVYVLFM FIFAVVAVQL
FKGRFFFCTD ESKEFERDCR GEFLVYNGDE VKAQKREWRK YDFHYNNVAW ALLTLFTVST
GEGWPDVLKH SVDSTYENQG PSPGYRMEMS IFYVVYFVVF PFFFVNIFVA LIIITFQEQG
DKMMEDYSLE KNERACIDFV INTRPLTRHM PKNKLSFQYR MWQFVVSPPF EYSIMALIAL
NTIVLMMKFD GASKEYDDVL KYLNIVFTTF FFMESILKII AFGPLNYFRD AWNIFDFVSV
LGSITDILVT ELGNNFINLS FLRLFRAARL LKLLRQGETI RILLWTFVQS FKALPYVCLL
IAMLFFIYAI IGMQLFGNLA LDEDREHAIN EHNNFRTFFM ALMLLFRSAT GEAWHEIMLA
CLGGKECDPE SGNTGNECGS TVAYTYFVSF IFLCSFLMLN LFVAVIMDNF EYLTRDSSIL
GPHHLDEYVR IWAEYDPAAC HPSGRITYTD MYQMLRHMCP PLGLGKRCPA RVAYKRLLRM
DLPVADDNTV HFNSTLMALI RTALDIKIAK GGADKHQMDA ELRKEMMAIW PNLSQKSLDQ
LVTPHKGKKL NHMFSPHPKM STDLTVGKIY AAMMIMEYYR QSKMKKLQ
//
