ID A0A0V1LNC5_9BILA Unreviewed; 2112 AA.
AC A0A0V1LNC5;
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};
GN Name=Ca-alpha1D {ECO:0000313|EMBL:KRZ60860.1};
GN ORFNames=T02_6857 {ECO:0000313|EMBL:KRZ60860.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ60860.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ60860.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ60860.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-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:KRZ60860.1}.
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DR EMBL; JYDW01000024; KRZ60860.1; -; Genomic_DNA.
DR Proteomes; UP000054721; 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; 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:UP000054721};
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 108..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 177..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 351..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 384..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 515..531
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 551..576
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 583..601
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 638..658
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 679..696
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 708..731
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 876..894
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 914..935
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 947..973
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1008..1027
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1118..1145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1199..1217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1229..1249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1269..1286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1298..1316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1362..1382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1448..1472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1628..1662
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 54..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1762..1792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1980..2004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..827
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1769..1783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 698
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1091
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:KRZ60860.1"
SQ SEQUENCE 2112 AA; 241160 MW; 350CFBB7D200AD35 CRC64;
LYTDHARSEA NFNDDVNIGK ELSGNEAAAL LHGDEARASR ADLWQQTLQA AVAAQTESST
TTKKRQQQRK MQRNVQQERP ERSLLCLGLK NPIRKLFISI VEWKPFEWLI LCMICANCIA
LAVYQPFPAH DSDRKNAVLQ NRKHKLNPQP GQRTATVAAV GHTGWGVGLF SEEQVEYIFI
VVFTIECVMK VIAYGFLFHP GAYLRNGWNL LDFLIVVIGL ISTALSTLNI HGFDVKALRA
FRVLRPLRLV SGVPSLQVVL NSILRAMVPL FHIALLVLFV IIIYAIIGLE LFCGKLHKTC
VDQWTGEHVP DPGPCGESHT SFHCDRSKNL VCTENHTWPG PNDGITNFDN FGLAMLTVFQ
CISLEGWTDV MYWVNDSVGR EWPWIYFITL VILGSFFVLN LVLGVLSGEF SKEREKARAR
GLFQKFREKQ QLEDDLKGYL DWITQAEDID LVNEEDEEQE AMDREEFGAD GEGGEEGGSK
EEFQRQSWFS MKIKRLKKLN RRCRRSCRRI VKSQAFYWLV IVLVFLNTMV LTSEHYGQPE
WLDHFQEIAN LFFVVLFTLE MFLKMYSLGF VNYFVALFNR FDCFVVIGSI LEFALTFAGL
MKPLGVSVLR SARLLRIFKV TKYWNSLRNL VASLLNSLRS IASLLLLLFL FIVIFALLGM
QVFGGKFNTI DPNMNKPRAN FDTFVQALLT VFQILTGEDW NAVMYNGIAA FGGVHSIGVI
VCIYFIVLFI CGNYILLNVF LAIAVDNLAD AESLTAAEKE EENKRANEAD PEDDMVVKAT
ADEDAVSVGQ FHESGEVKLP FNEPTDAEDE HLASGDDDQE REMENQSQFK PTARPHRQSE
LNLPKKTKPI PDASSLFLFS STNKVRIFCN KVINHSYFTN SVLVCILVSS AMLAAEDPLQ
ASSFRNEVLN YFDYFFTTVF TIEISLKVLV YGLILHKGSF CRNAFNLLDM LVVGVSLTSF
GLKSGAISVV KILRVLRVLR PLRAINRAKG LKHVVQCVIV AVKTIGNIML VTFMLEFMFA
IIGVQIFKGS FFRCTDRARL TAEECKGTFI EFEGGDVTRP HVRNREWTNY DFNFDNVQNA
MVALFVVSTF EGWPDLLHVA MDSSDEGIGP QYNARVSVAI FFITFIVVIA FFMMNIFVGF
VIVTFQSEGE REYENCELDK NQRKCIEFAL TAKPQRRYIP KNRFQYKIWW FVTSQPFEYA
IFIIIILNTL ILGMKHYKSS AAFDEALDVL NLFFTTVFAL EFICKLFALT FKHHKMTRTF
DDVLDTMNLI FTGIFAMEFI LKVMAFRCKN YFGDAWNVFD FIIVLGSFID IIYGKVSPGS
NIISINFFRL FRVMRLVKLL SRGEGIRTLL WTFMKSFQAL PYVALLIVLL FFIYAVIGMQ
IFGKIALNSN TEIHRNNNFQ TFPSAVLVLF RSATGEAWQL IMLSCANTPA AMCDPESDDR
GQPCGNDFAY PFFISFFMLC SFLIINLFVA VIMDNFDYLT RDWSILGPHH LDEFVRLWSE
YDPDAKGRIK HLDVVTLLRK ISPPLGFGKL CPHRLACKRL VSMNMPLNSD GTVCFNSTLF
ALVRTNLKIY TEERPFLFLK KSEKVESQSL VSSNIEEANE QLRAVIKRIW KRTPQRLLDE
IVPPSGRDDE ITVGKFYATY LIQDYFRRFK KRKEVEQKET NMQGNITMSL QFGEEFPSDL
EAFDVLIVFL HVLLLQAGLR TLHEIGPEIK RAISGNLETD WSKEFEEPQH RRDHSLFGTL
VHALQAHYKP FIEGNLTNPA YSNVNGDLKS QEGDDEAEQQ HQQHQQEQQE QQQQLMFNKM
NDLKSPPVKS DRDKISEFES DESVCNKPER RCNSFFSNIR RRMDSIVSPS IVLFDSDHDS
SEHEMQERVR FVPRGSKPTG LSFEGSRWLP RKLSFRRTPI GGAAAVSNLQ QGNNKRLQFS
NAIILDDSDP DSVLHSENVV DLTESGDDSK LSVSPPLELR DDAYYLDGID YNTWRPAPMG
QGVRLRGRGN GRRKSRSMPL PHHEHQRNYA DVLVEKVLAD QGLGRYADPN LIRTTQLEIA
EAYNMTEAQM HSAARSLMQR SPKYFEHMGG QRPADIKDFN QYSKTALLKP REINSSEEVD
ISDDMNMFMS VV
//
