ID A0A1S3WN95_ERIEU Unreviewed; 2371 AA.
AC A0A1S3WN95;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Voltage-dependent P/Q-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1A {ECO:0000313|RefSeq:XP_016047757.1};
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_016047757.1};
RN [1] {ECO:0000313|RefSeq:XP_016047757.1}
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. 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 RefSeq; XP_016047757.1; XM_016192271.1.
DR GeneID; 103121909; -.
DR CTD; 773; -.
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; 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: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 51..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 253..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 436..455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 562..584
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 638..662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1169..1188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1208..1229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1241..1258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1303..1325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1415..1440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1496..1514
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1526..1549
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1617..1635
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1713..1737
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1874..1908
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 756..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1915..2001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2014..2371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 658..694
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 756..773
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..943
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1056
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1952..1996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2034..2050
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2061..2080
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2131..2147
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2148..2184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2185..2222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2290..2304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2312..2327
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 616
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 2371 AA; 267840 MW; 37773AFB4B52E217 CRC64;
MAQRARTMAL YNPIPVRQSC LTVNRSLFLF SEDNVVRKYA KKITEWPPFE YMILATIIAN
CIVLALEQHL PDNDKTPMSE RLDDTEPYFI GIFCFEAGIK IIALGFAFHK GSYLRNGWNV
MDFVVVLTGI LATIGAEFDL RTLRAVRVLR PLKLVSGIPS LQVVLKSIMK AMIPLLQIGL
LLFFAILIFA IIGLEFYMGK FHTTCFEEGT ADIPSESPAP CGTEEPARTC PNGTQCRPYW
EGPNNGITQF DNILFAVLTV FQCITMEGWT DLLYNSNDAS GNTWNWLYFI PLIIIGSFFM
LNLVLGVLSG EFAKERERVE NRRAFLKLRR QQQIERELNG YMEWISKAEE VILAEDDTDG
EQRLPFDALR RATMKKSKTD LLHPEEAEDQ LADIASVGSP FARASIKSAK LENSTFFHKK
ERRMRFYIRR MVKTQAFYWT VLSLVALNTL CVAIVHYNQP EWLSDFLYYA EFIFLGLFMS
EMFIKMYGLG TRPYFHSSFN CFDCGVIIGS IFEVIWAVIK PGTSFGISVL RALRLLRIFK
VTKYWASLRN LVVSLLNSMK SIISLLFLLF LFIVVFALLG MQLFGGQFNF DEGTPPTNFD
TFPAAIMTVF QILTGEDWNE VMYDGIKSQG GVQGGMVFSI YFIVLTLFGN YTLLNVFLAI
AVDNLANAQE LTKDEQEEEE VANQKLALQK AKEVAEVSPL SAANLSIAVK EQQKNQKPVR
SVWEQRTSEM RKQNLMASRE ALYPERDPEE RWATTYRHLR PDTKSHLDRP LVVDPQDNRN
NNTNKTRVAE PPGDPRVSPP RPCPAEDLGR KAARCPPDGR RAWAAPPDVQ LGREGPYGRE
CDPRPREPGP GTPGPPAPLG GWGPESGGIP GEARKAGDPQ RRPARRPVGG RDSRGGSPRA
GVDGEPPRRP RTHRRAPDDS GGGGGERRAR RRDPEDGGER RRRHRHGPPG SSAPEPDPRR
RRRRENQVSG VPMSGPNLST TRPIQQDLSR QDPLPLAEDI DNMRNNKLVT AEAAGPHDGM
GPPGLPPSPT KTGDCAEPGP HSNPQNTAGR RVPNNPGNPS NPGPPGTPEN SLIVTNPSST
QANSAKTARK PDHTAVDIPP ACPVPLNHTV VQVNKNANPD PLPKKEEEKK EEEDDPGEDG
PKPMPPYSSM FILSTTNPLR RLCHYILNLR YFEMCILMVI AMSSIALAAE DPVQPNAPRN
NVLRYFDYVF TGVFTFEMVI KMIDLGLVLH QGAYFRDLWN ILDFIVVSGA LVAFAFTGNS
KGKDINTIKS LRVLRVLRPL KTIKRLPKLK AVFDCVVNSL KNVFNILIVY MLFMFIFAVV
AVQLFKGKFF HCTDESKEFE KDCRGKYLLY EKNEVKARDR EWKKYEFHYD NVLWALLTLF
TVSTGEGWPQ VLKHSVDATF ENQGPSPGYR MEMSIFYVVY FVVFPFFFVN IFVALIIITF
QEQGDKMMEE YSLEKNERAC IDFAISAKPL TRHMPQNKQS FQYRMWQFVV SPPFEYTIMA
MIALNTIVLM MKFYGASVAY ENALRVFNIV FTSLFSLECV LKVMAFGILN YFRDAWNIFD
FVTVLGSITD ILVTEFGNNF INLSFLRLFR AARLIKLLRQ GYTIRILLWT FVQSFKALPY
VCLLIAMLFF IYAIIGMQVF GNIGIDVEDE DSDEDDFQIT EHNNFRTFFQ ALMLLFRSAT
GEAWHNIMLS CLSGKPCDKN SGILTPECGN EFAYFYFVSF IFLCSFLMLN LFVAVIMDNF
EYLTRDSSIL GPHHLDEYVR VWAEYDPAAW GRMPYRDMYQ MLTHMSPPLG LGKKCPSRVA
YKRLLRMDLP VAEDNTVHFN STLMALIRTA LDIKIAKGGA DKQQMDAELR KEMTAIWPNL
SQKTLDLLVT PHKSTDLTVG KIYAAMMIME YYRQSKAKKL QAMREEQNRT PLMFQRMEPP
SPTQEGGPGQ NALPSTQLDP GGGLMTHEQG LKDSPSWVTQ RAQEMFQKTG TWSPERGPPS
DMPNSQPNSQ SVEMREMSRD GYSDREHYLP MEGQVRAASM PRLPAENQRR RGRPRGNNLT
TISDNSPMKR SASVLGPKAR RLEDYSLERV PPEDDPRHHQ RRRDRGHRAS ERSLGRYTDV
DTGLGTDLSM TTQSGDLPPK ERDQERGRPK DRKHRQHHHH HHHHHPQPPD KERYPQERPD
HGRTRTRDQR WSRSPSEGRE HMTHRQGSSS VSGSPAPSTS GTSTPRRGRR QLPQTPSTPR
PHVSYSPVVR KAGGPSGGAR RYPPGPGSEP GAHGVGGRSP GLERRAPGRP ESPRACRHGA
RWPGGGGHGS EGPRHHHGGY YYDEADGEDP PLDGPPPRTP RAAGPPLCAS PPARHGRRLP
NGYYAAHGPA RPRAPRKGLQ DAYSETDDDW C
//
