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Database: UniProt
Entry: G3HNB3_CRIGR
LinkDB: G3HNB3_CRIGR
Original site: G3HNB3_CRIGR 
ID   G3HNB3_CRIGR            Unreviewed;      1387 AA.
AC   G3HNB3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   ORFNames=I79_012250 {ECO:0000313|EMBL:EGW06085.1};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW06085.1, ECO:0000313|Proteomes:UP000001075};
RN   [1] {ECO:0000313|Proteomes:UP000001075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX   PubMed=21804562; DOI=10.1038/nbt.1932;
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA   Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA   Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA   Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL   Nat. Biotechnol. 29:735-741(2011).
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. {ECO:0000256|RuleBase:RU003808}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003808}; Multi-
CC       pass membrane protein {ECO:0000256|RuleBase:RU003808}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC       1.A.1.11) family. {ECO:0000256|RuleBase:RU003808}.
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DR   EMBL; JH000543; EGW06085.1; -; Genomic_DNA.
DR   STRING; 10029.G3HNB3; -.
DR   PaxDb; 10029-XP_003505128-1; -.
DR   eggNOG; KOG2301; Eukaryota.
DR   InParanoid; G3HNB3; -.
DR   Proteomes; UP000001075; 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; 6.10.250.2500; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 4.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR005446; VDCC_L_a1su.
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:SF2; VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1F; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
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};
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|PIRSR:PIRSR602077-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001075};
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        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        59..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        90..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        163..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        242..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        275..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        447..465
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        480..498
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        576..595
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        645..667
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        788..807
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        827..847
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        905..934
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1030..1057
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1098..1125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1137..1156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1236..1254
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1327..1351
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          18..308
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   DOMAIN          448..680
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   DOMAIN          787..1063
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   DOMAIN          1108..1361
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   REGION          383..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          725..746
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        725..743
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         256
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         628
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         1003
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ   SEQUENCE   1387 AA;  157130 MW;  BF5B087B1F20B799 CRC64;
     MWGFQHYSSW VLNCVHLRPF DILILLTIFA NCVALGVYIP FPEDDSNTAN HNLEQVEYVF
     LVIFTVETVL KIVAYGLVLH PSAYIRNGWN LLDFIIVVVG LFSVLLEQGP GRPGDVPHTG
     GKPGGFDVKA LRAFRVLRPL RLVSGVPSLH IVLNSIMKAL VPLLHIALLV LFVIIIYAII
     GLELFLGRMH KTCYFLGSDM EAEEDPSPCA SSGSGRSCTL NQTECRGRWP GPNGGITNFD
     NFFFAMLTVF QCITMEGWTD VLYWMQDAMG YELPWVYFVS LVIFGSFFVL NLVLGVLSGE
     FSKEREKAKA RGDFQKLREK QQMEEDLRGY LDWITQAEEL DLHDPSIDGN LASLAEEGRA
     SHRPQLSELT NRRRGRLRWF SHSTRSTHST SSHASLPASD TGSMADTPGD EDEEEGSLAS
     CTRCLRHFRR ANRGLRARCR RAVKSNACYW AVLLLVFLNT LTIASEHHGQ PVWLTQTQEY
     ANKVLLCLFT VEMLLKLYGL GPSVYVASFF NRFDCFVVCG GILETTLVEV GAMQPLGISV
     LRCVRLLRIF KVTRHWASLS NLVASLLNSM KSIASLLLLL FLFIIIFSLL GMQLFGGKFN
     FDQTHTKRST FDTFPQALLT VFQILTGEDW NVVMYDGIMA YGGPFFPGML VCIYFIILFI
     CGNYILLNVF LAIAVDNLAS GDAGTAKDKG RKWEEFILCQ AQFQELSIDF FQPISPFALF
     PAPGIEEEEE EEEEEEEEEE EGGAGHVELL QEVVPKEKVV PIPEGSAFFC LSQTNPLRKA
     CHTLIHHHIF TSLILVFIIL SSVSLAAEDP IRAHSFRNHI LGYFDYAFTS IFTVEILLKM
     TVFGAFLHRG SFCRSWFNML DLLVVSVSLI SFGIHSSAIS VVKILRVLRV LRPLRAINRA
     KGLKHVVQCV FVAIRTIGNI MIVTTLLQFM FACIGVQLFK GKFYSCTDEA KHNLKECKGS
     FLIYPDGDVS RPLVRERLWV NSDFNFDNVL SAMMALFTVS TFEGWPALLY KAIDAHAEDE
     GPIYNYHVEI SVFFIVYIII IAFFMMNIFV GFVIITFRAQ GEQEYQNCEL DKNQRQCVEY
     ALKAQPLRRY IPKNPHQYRV WAAVNSAAFE YLMFLLILLN TVALAMQHYE QTAPFNYAMD
     ILNMVFTGLF TIEMVLKIIA FKPKHYFADA WNTFDALIVV GSVVDIAVTE VNSSEDSSRI
     SITFFRLFRV MRLVKLLSKG EGIRTLLWTF IKSFQALPYV ALLIAMIFFI YAVIGMQMFG
     KVALQDGTQI NRNNNFQTFP QAVLLLFRCA TGEAWQEIML ASLPGNRCDP ESDFGPGEEF
     TCGSNFAIAY FISFFMLCAF LIINLFVAVI MDNFDYLTRD WSILGPHHLD EFKRIWSEYD
     PGAKYTR
//
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