ID A0A452I6S4_9SAUR Unreviewed; 1972 AA.
AC A0A452I6S4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000023301.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000023301.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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. {ECO:0000256|RuleBase:RU003808}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1D subfamily. {ECO:0000256|ARBA:ARBA00010354}.
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DR Ensembl; ENSGAGT00000026542.1; ENSGAGP00000023301.1; ENSGAGG00000013700.1.
DR Proteomes; UP000291020; 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; IPR031688; CAC1F_C.
DR InterPro; IPR031649; GPHH_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR005452; LVDCC_a1dsu.
DR InterPro; IPR014873; VDCC_a1su_IQ.
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:SF11; VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1D; 1.
DR Pfam; PF08763; Ca_chan_IQ; 1.
DR Pfam; PF16885; CAC1F_C; 1.
DR Pfam; PF16905; GPHH; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR PRINTS; PR01630; LVDCCALPHA1.
DR PRINTS; PR01636; LVDCCALPHA1D.
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};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000291020};
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 111..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 358..380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 490..508
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 528..551
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 620..639
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 697..719
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 801..819
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 839..859
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 871..897
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 917..947
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1042..1069
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1121..1141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1153..1171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1254..1272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1325..1349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1483..1517
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1655..1685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1779..1807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1657..1685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 339
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 672
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1015
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 1972 AA; 222683 MW; D1A9972CD92CA387 CRC64;
SKGFGSTGSS SGEAAAAGGG GAAPPPSKQT VLSWQAAIDA ARQAKAAQTM STTTAQPVGS
LSQRKRQQYA KSKKQGNTSN SRPPRALFCL SLNNPIRRAC ISLVEWKPFD IFILLAIFAN
CVALAVYIPF PEDDSNSTNH NLEKVEYAFL IIFTIETFLK IIAYGLLLHP NAYVRNGWNL
LDFVIVVVGL FSVILEQLTK ETEGGSHSGG KPGGFDVKAL RAFRVLRPLR LVSGVPSLQV
VLNSIIKAMV PLLHIALLVL FVIIIYAIIG LELFIGKMHK SYILVEDDPA PCAFSGNGRQ
CAINGTECRG GWVGPNGGIT NFDNFAFAML TVFQCITMEG WTDVLYWMND AMGFELPWVY
FVSLVIFGSF FVLNLVLGVL SGEFSKEREK AKARGDFQKL REKQQLEEDL KGYLDWITQA
EDIDPENEEE GDEEGKRNTS MPTSETESVN TENVSGEGES PASPIKMSNR RWRRWNRFSR
RKCRAAVKSV SFYWLVIVLV FLNTLTISSE HYNQPDWLTQ IQDIANKVLL ALFTCEMLIK
MYSLGLQAYF VSLFNRFDCF VVCGGIVETI LVELEIMSPL GISVFRCVRL LRIFKVTRHW
TSLSNLVASL LNSMKSIASL LLLLFLFIII FSLLGMQLFG GKFNFDETQT KRSTFDNFPQ
ALLTVFQILT GEDWNAVMYD GIMAYGGPSS SGMVVCIYFI ILFICGNYIL LNVFLAIAVD
NLADAESLNT AQKEEAEEKQ RKKNEGEEDE PEVPVGPRPR RISELNMKEK ITPIPEGSAF
FIFSSTNPIR VGCHRLINHH IFTNLILVFI MLSSVSLAAE DPIRSHSFRN NILGYFDYAF
TAIFTVEILL KMTAFGAFLH KGSFCRNYFN LLDLLVVGVS LVSFGIQSSA ISVVKILRVL
RVLRPLRAIN RAKGLKHVVQ CVFVAIRTIG NIMIVTTLLQ FMFACIGVQL FKGKFYRCTD
EAKQNPEDCR GIFIVYKDGD VDNPMVRERV WQNSDFNFDN VLSAMMALFT VSTFEGWPAL
LYKAIDSNAE NIGPVYNYRV EISIFFIIYI IIIAFFMMNI FVGFVIVTFQ EQGEQEYKNC
ELDKNQRQCV EYALKARPLR RYIPKNPYQY KFWYMVNSTG FEYIMFVLIM LNTLCLAMQH
YGQSKLFNDA MDILNMVFTG VFTVEMVLKL IAFKPKGYFS DAWNAFDSLI VIGSIVDVVL
SEADVINVSN NCSYSARISI TFFRLFRVMR LVKLLSRGEG IRTLLWTFIK SFQALPYVAL
LIAMLFFIYA VIGMQVIMTH YETIIFDGSC LVLFEIMLAC LPGKHCDPES DYSPEEEFTC
GSNFSIIYFI SFYMLCAFLI INLFVAVIMD NFDYLTRDWS ILGPHHLDEF KRIWSEYDPE
AKGRIKHLDV VTLLRRIQPP LGFGKLCPHR VACKRLVAMN MPLNSDGTVM FNATLFALVR
TALKIKTEGN LEQANEELRA VIKKIWKKTS MKLLDQVVPP AGDDEVTVGK FYATFLIQDY
FRKFKKRKEQ GLVGKYPAKN TTIALQAGLR TLHDIGPEIR RAISCDLQDD EPEENNHEEE
EDIYKRNGAL FGNHINHVSS DRRDSFQQIN TTHRPLHVQR PSIPSASDTE KNMYHQASNS
VFHNHHNHNS IGKHVPNSTN ANLNNANMSK VANGRHPNIG NHEHRSENGY HSYSRADHER
HRRANSKRNP CLVMNYTQIC TYKTKGRLFP PSIQKATLIT PKLLSGKIPM AQPIPPPCKS
LLSLGFNLQG QDCLRYANSC LIFTSLYQVM AVAGLDSSKA HKHSPSRSTR SWATPPATPP
NRDRTPYYTP LIQVDRAEST EQMNGSLPSL NRSSWYTDDP DISYRTFTPA NLTVPNDFRH
KHSDKQRSAD SLVEAVLISE GLGRYAKDPK FVSATKHEIA DACDMTIDEM ESAASNLLNG
NISNGTNGDM FPILSRQDYE LQDFGPGYSD EEPDTSRYEE DLADEMICIT TL
//
