ID A0A0V0Y9E2_TRIPS Unreviewed; 2042 AA.
AC A0A0V0Y9E2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
DE Flags: Fragment;
GN Name=Ca-alpha1D {ECO:0000313|EMBL:KRX96791.1};
GN ORFNames=T4E_8154 {ECO:0000313|EMBL:KRX96791.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX96791.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX96791.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX96791.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX96791.1}.
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DR EMBL; JYDU01000039; KRX96791.1; -; Genomic_DNA.
DR STRING; 6337.A0A0V0Y9E2; -.
DR Proteomes; UP000054815; 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; 1.10.238.10; EF-hand; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 5.
DR InterPro; IPR031688; CAC1F_C.
DR InterPro; IPR031649; GPHH_dom.
DR InterPro; IPR005821; Ion_trans_dom.
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:SF1; VOLTAGE-DEPENDENT CALCIUM CHANNEL TYPE D SUBUNIT ALPHA-1; 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 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 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:UP000054815};
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 85..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 216..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 461..477
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 497..522
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 529..547
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 584..604
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 625..642
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 654..677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 821..839
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 859..880
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 892..918
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 953..972
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1063..1090
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1144..1162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1174..1194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1214..1231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1243..1261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1307..1327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1393..1417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1571..1605
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 33..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1681..1711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1826..1888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1912..1934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1687..1706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1826..1853
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 311
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 644
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1036
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX96791.1"
SQ SEQUENCE 2042 AA; 233470 MW; 96F5EADE4896ACCB CRC64;
LSGNEAAALL HGDEARASRA DLWQQTLQAA VAAQTESSTT TKKRQQQRKM QRNVQQERPE
RSLLCLGLKN PVRKLFISIV EWKPFEWLIL CMICANCIAL AVYQPFPAHD SDRKNAVLEQ
VEYIFIVVFT IECVMKVIAY GFLFHPGAYL RNGWNLLDFL IVVIGLISTA LSTLNIHGFD
VKALRAFRVL RPLRLVSGVP SLQVVLNSIL RAMVPLFHIA LLVLFVIIIY AIIGLELFCG
KLHKTCVDQW TGEHVPDPGP CGESHTSFHC DRSKNLVCTE NHTWPGPNDG ITNFDNFGLA
MLTVFQCISL EGWTDVMYWV NDSVGREWPW IYFITLVILG SFFVLNLVLG VLSGEFSKER
EKARARGLFQ KFREKQQLED DLKGYLDWIT QAEDIDLVNE EDEEQEAMDR EEFGADGEGG
EEGASKEEYQ RQSWFSMKIR RLKKLNRRCR RSCRRIVKSQ AFYWLVIVLV FLNTMVLTSE
HYGQPEWLDH FQEIANLFFV VLFTLEMFLK MYSLGFVNYF VALFNRFDCF VVIGSILEFA
LTFAGLMKPL GVSVLRSARL LRIFKVTKYW NSLRNLVASL LNSLRSIASL LLLLFLFIVI
FALLGMQVFG GKFNTIDPNM NKPRANFDTF VQALLTVFQI LTGEDWNAVM YNGIAAFGGV
HSIGVIVCIY FIVLFICGNY ILLNVFLAIA VDNLADAESL TAAEKEEEGK RANEADPDDT
VTKAPADEDA VSVEQFHESG EVKLPFNEPT DAEDEHLASG DEDQEREMEN QSQFKPTARP
HRQSELNLPK KTKPIPDASS LFLFSSTNKV RIFCNKVINH SYFTNSVLVC ILVSSAMLAA
EDPLQASSFR NEVLNYFDYF FTTVFTIEIS LKVLVYGLIL HKGSFCRNAF NLLDMLVVGV
SLTSFGLKSG AISVVKILRV LRVLRPLRAI NRAKGLKHVV QCVIVAVKTI GNIMLVTFML
EFMFAIIGVQ IFKGSFFRCT DRARLTAEEC KGTFIEFEGG DVTRPHVRNR EWTNYDFNFD
NVQNAMVALF VVSTFEGWPD LLHVAMDSSD EGIGPQYNAR VSVAIFFITF IVVIAFFMMN
IFVGFVIVTF QSEGEREYEN CELDKNQRKC IEFALTAKPQ RRYIPKNRFQ YKIWWFVTSQ
PFEYAIFIII ILNTLILGMK HYKSSAAFDE ALDVLNLFFT TVFALEFICK LFALTFKHHK
MTRTFDDVLD TMNLIFTGIF AMEFILKVMA FRCKNYFGDA WNVFDFIIVL GSFIDIIYGK
VSPGSNIISI NFFRLFRVMR LVKLLSRGEG IRTLLWTFMK SFQALPYVAL LIVLLFFIYA
VIGMQIFGKI ALNSNTEIHR NNNFQTFPSA VLVLFRSATG EAWQLIMLSC ANTPTAMCDP
ESDDRGQPCG NDFAYPFFIS FFMLCSFLII NLFVAVIMDN FDYLTRDWSI LGPHHLDEFV
RLWSEYDPDA KGRIKHLDVV TLLRKISPPL GFGKLCPHRL ACKRLVSMNM PLNSDGTVCF
NSTLFALSDS YQQFSERPFL FLKKSEKVES QSLVSSNIEE ANEQLRAVIK RIWKRTPQRL
LDEIVPPSGR DDEITVGKFY ATYLIQDYFR RFKKRKEVEQ KETNLQGNIT MSLQAGLRTL
HEIGPEIKRA ISGNLETDWS KEFEEPQHRR DHSLFGTLVH ALQAHYKPFI EGNLANPAYS
NVNGDLKSQE GDDEIEHHHY HQQQQEPEHQ QEPQQMMMFK MNDLKSPPVK SDRDKISEFE
SDDSVCNKPE RRCNSFFSNI RRRVDSIVSP SIVLFDSDHD SSEHEMQERM RFVPRGSKPT
TGLSFEGSRW LPRKLSFRRA PIGAAAVSNS QQGNSNNNNN NNNNNNKRLQ FSNAIILDDS
DPDSVMHPEN VVDLTESGDD SKSSVSPPLE LRDDAYYLDG IDYNTWRPAP MGQGVRLRRR
GNGRRKSRSM PLPHDQRNYA DVLVEKVLAD QGLGRYADPN LIRTTQLEIA EAYNMTEAQM
HSAARSLMQR SPKYFEHMGG QRPADIKDFN QYSKTALLKP RQMNSSEDVD ISDDMNMFMS
VV
//
