ID A0A1S3A9J7_ERIEU Unreviewed; 1916 AA.
AC A0A1S3A9J7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1D {ECO:0000313|RefSeq:XP_007531464.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007531464.1};
RN [1] {ECO:0000313|RefSeq:XP_007531464.1}
RP IDENTIFICATION.
RG RefSeq;
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. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_007531464.1; XM_007531402.2.
DR CTD; 776; -.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; A0A1S3A9J7; -.
DR OrthoDB; 1110761at2759; -.
DR Proteomes; UP000079721; Unplaced.
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; 3.
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; 3.
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:UP000079721};
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 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 406..425
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 478..505
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 640..658
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 678..698
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 710..736
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 756..786
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 883..908
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 962..980
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 992..1012
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1102..1120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1194..1217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1351..1385
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 182..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1414..1552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1648..1673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..591
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1414..1435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1450..1464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1490..1519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1537..1552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 458
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 854
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 1916 AA; 217853 MW; 789CE2C57F6C69C4 CRC64;
MVPLLHIALL VLFVIIIYAI IGLELFIGKM HKTCFFADSD IVAEEDPAPC AFSGNGRQCA
VNGTECRSGW VGPNGGITNF DNFAFAMLTV FQCITMEGWT DVLYWVNDAI GWEWPWVYFV
SLIILGSFFV LNLVLGVLSG EFSKEREKAK ARGDFQKLRE KQQLEEDLKG YLDWITQAED
IDPENEEEGG EENKRNTSMP TSETESVNTE NVSGEGEHRG CCVNLWCWWK RRGSAQTGPS
GCRRWGQAIS KSKLSRRWRR WNRFNRRRCR AAVKSVTFYW LVIVLVFLNT LTISSEHYNQ
PDWLTQIQDI ANKVLLALFT CEMLVKMYSL GLQAYFVSLF NRFDCFVVCG GITETILVEL
EIMSPLGISV FRCVRLLRIF KVTRHWTSLS NLVASLLNSM KSIASLLLLL FLFIIIFSLL
GMQLFGGKFN FDETQTKRST FDNFPQALLT VFQILTGEDW NAVMYDGIMA YGGPSSSGMI
VCIYFIILFI CGNYILLNVF LAIAVDNLAD AESLNTAQKE EAEEKERKKI ARKESLENKK
NNKPEVNQIA NSDNKVTIDD YREEDEDKDP YPPCDVPVGE EEEEEEEDEP EVPAGPRPRR
ISELNMKEKI APIPEGSAFF ILSKTNPIRV GCHKLINHHI FTNLILVFIM LSSAALAAED
PIRSHSFRNT ILGYFDYAFT AIFTVEILLK MTTFGAFLHK GAFCRSYFNL LDMLVVGVSL
VSFGIQSSAI SVVKILRVLR VLRPLRAINR AKGLKHVVQC VFVAIRTIGN IMIVTTLLQF
MFACIGVQLF KGKFYRCTDE AKSNPEECRG LFILYKDGDV DSPVVRERVW QNSDFNFDNV
LSAMMALFTV STFEGWPELL YKAIDSNGEN VGPIYNYRVE ISIFFIIYII IVAFFMMNIF
VGFVIVTFQE QGEKEYKNCE LDKNQRQCVE YALKARPLRR YIPKNPYQYK FWYVVNSSPF
EYMMFVLIML NTLCLAMQHY EQSKMFNDAM DILNMVFTGV FTVEMVLKVI AFKPKGYFSD
AWNTFDSLIV IGSIIDVALS EADPTESENV PVPTAPPGNS EESNRISITF FRLFRVMRLV
KLLSRGEGIR TLLWTFIKSF QALPYVALLI AMLFFIYAVI GMQMFGKVAM RDNNQINRNN
NFQTFPQAVL LLFRCATGEA WQEIMLACLP GKLCDPESDY NPGEEYTCGS NFAIVYFISF
YMLCAFLIIN LFVAVIMDNF DYLTRDWSIL GPHHLDEFKR IWSEYDPEAK GRIKHLDVVT
LLRRIQPPLG FGKLCPHRVA CKRLVAMNMP LNSDGTVMFN ATLFALVRTA LKIKTEGNLE
QANEELRAVI KKIWKKTSMK LLDQVVPPAG DDEVTVGKFY ATFLIQDYFR KFKKRKEQGL
VGKYPTKNTT IALQAGLRTL HDIGPEIRRA ISCDLQDDES EDRKREEEED VFKRNGALLG
NHVNHVNSDR RDSLQQTNTT HRPLHVQRPA MPPASDTEQP LFPPAGNSVC HNHHNRNSIG
KQAPSSTNAN LNNANMSKAA PGKRPSIGTL EQVSGNGHHS SHKHDCEPQR RASIKRTRYY
ETYIRSDSGD EQFPTICRED PEIQGCFRDA YCLVEQEYFS SEECYDEDSS PTGSRHNYGY
YNRYLGNSTD FERPRGYHHP QGFWEDEDTP VCYDSQRSPR RRLLPPTPTS HRRSSFNFEC
LRRQSSQEEA PPSPAFPQRT ALPLHLMQQQ IMAVAGLDSS KAQKYSPSHS TRSWATPPAT
PPYRDWTPCY TPLIQVERSE APDQVNGSLP SLHRSSWYTD EPGISYRTFT PASLTVPSSF
CNKNSDKQRS ADSLVEAVLI SEGLGRYARD PKFVSATKYE IADACDLTID EMESAASSLL
NGTMHGRAPG GLGSGIGCHC LDYELQDFGP GYSDEEPEPG REEEDLADEM ICITTL
//
