ID A0A0V1ME06_9BILA Unreviewed; 2057 AA.
AC A0A0V1ME06;
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:KRZ69843.1};
GN ORFNames=T10_13548 {ECO:0000313|EMBL:KRZ69843.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ69843.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ69843.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ69843.1};
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:KRZ69843.1}.
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DR EMBL; JYDO01000127; KRZ69843.1; -; Genomic_DNA.
DR Proteomes; UP000054843; 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; 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:UP000054843};
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 139..157
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 875..893
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 913..934
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1007..1026
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1117..1144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1198..1216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1228..1250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1256..1275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1319..1337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1408..1433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1570..1604
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 87..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1679..1714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1850..1878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1902..1925
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 801..826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1686..1704
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 1090
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 2057 AA; 234754 MW; C03B9A5193CC3390 CRC64;
MGRSIFVGTV NPALSKSSVP LPIPEHLRAS LQLDHDHHAR SEANFNDDVN IGKELSGNEA
AALLHGDEAR ASRADLWQQT LQAAVAAQTE SSTTTKKRQQ QRKMQRNVQQ ERPERSLLCL
GLKNPIRKLF ISIVEWKPFE WLILCMICAN CIALAVYQPF PAHDSDRKNA VLEQVEYIFI
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
EEYQRQSWFS 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 EEGKRVNEAD PDDAMVKVPA
DEDAVSVEQF HESGEVKLPF NEPTDAEDEH LASGDEDQER EMENQSQFKP TARPHRQSEL
NLPKKTKPIP DASSLFLFSS TNKVRIICNK VINHSYFTNS VLVCILVSSA MLAAEDPLQA
SSFRNEVLNY FDYFFTTVFT IEISLKVLVY GLILHKGSFC RNAFNLLDML VVGVSLTSFG
LKSGAISVVK ILRVLRVLRP LRAINRAKGL KHVVQCVIVA VKTIGNIMLV TFMLEFMFAI
IGVQIFKGAF FRCTDRARLT AEECKGTFIE FEGGDVTRPH VRSREWTNYD FNFDNVQNAM
VALFVVSTFE GWPDLLHVAM DSSDEGIGPQ YNARVSVAIF FITFIVVIAF FMMNIFVGFV
IVTFQSEGER EYENCELDKN QRKCIEFALT AKPQRRYIPK NRFQYKIWWF VTSQPFEYAI
FIIIILNTLI LGMKHYKSSA AFDEALDVLN LFFTTVFALE FICKLFALTF KNYFGDAWNV
FDFIIVLGSF IDIIYGKPGS NIISINFFRL FRVMRLVKLL SRGEGIRTLL WTFMKSFQAL
PYVALLIVLL FFIYAVIGMQ IFGKIALNSN TEIHRNNNFQ TFPSAVLVLF RSATGEAWQL
IMLSCANTPT AMCDPESDDR GQPCGNDFAY PFFISFFMLC SFLIINLFVA VIMDNFDYLT
RDWSILGPHH LDEFVRLWSE YDPDAKGRIK HLDVVTLLRK ISPPLGFGKL CPHRLACKRL
VSMNMPLNSD GTVCFNSTLF ALVRTNLKIY TEVSSNIEEA NEQLRAVIKR IWKRTPQRLL
DEIVPPSGRD DEITVGKFYA TYLIQDYFRR FKKRKEVEQK ETNLQGNITM SLQAGLRTLH
EIGPEIKRAI SGNLETDWSK EFEEPQHRRD HSLFGTLVHA LQAHYKPFIE GNLANPAYSN
VNGDLKSQEG DDEVEQHQHQ EQEPQHQHQQ QPQPQQMMMM FKMNDLKSPP VKSDRDKISE
FESDESVCNK PERRCNSFFS NIRRRVDSIV SPSIMLFDSD HDSSEHEMQE RVRFVPRGSK
PTTGLSFEGS RWLPRKLSFR RAPIGAAVSN LQQGNNKRLQ FSNAIILDDS DPDSIMHPEN
VVDLTESGDD SKSSVSPPLE LRDDAYYLDG IDYNTWRPAP MGQGVRLRRR GNNGRRKSRS
MPLPHDQRNY ADVLVEKVLA DQGLGRYADP NLIRTTQLEI AEAYNMTEAQ MHSAARSLMQ
RSPKYFEHMG GQRPADIKDF NQYSKTALLK PREMNNSEDV DISDDMNMFM SVAESWIKTG
RVLMDSNVSL RSDRLSP
//
