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Database: UniProt
Entry: A0A0V1L9Y5_9BILA
LinkDB: A0A0V1L9Y5_9BILA
Original site: A0A0V1L9Y5_9BILA 
ID   A0A0V1L9Y5_9BILA        Unreviewed;      1665 AA.
AC   A0A0V1L9Y5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   ORFNames=T02_12006 {ECO:0000313|EMBL:KRZ56261.1};
OS   Trichinella nativa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ56261.1, ECO:0000313|Proteomes:UP000054721};
RN   [1] {ECO:0000313|EMBL:KRZ56261.1, ECO:0000313|Proteomes:UP000054721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS10 {ECO:0000313|EMBL:KRZ56261.1};
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:KRZ56261.1}.
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DR   EMBL; JYDW01000097; KRZ56261.1; -; 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; 6.10.250.2500; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 4.
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; 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   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        71..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        141..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        203..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        316..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        444..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        477..500
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        570..592
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        642..670
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        806..824
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        844..865
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        877..903
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        923..953
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1048..1075
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1118..1144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1156..1182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1253..1275
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1351..1372
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1500..1534
FT                   /note="Voltage-dependent calcium channel alpha-1 subunit
FT                   IQ"
FT                   /evidence="ECO:0000259|SMART:SM01062"
FT   REGION          678..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1614..1651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1620..1642
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         297
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         623
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         1021
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ   SEQUENCE   1665 AA;  190802 MW;  94C7F7EADA29767C CRC64;
     MSAENYTTPS DTTIVDSCLL SSTVAGTTPT TRSKRNNSSY TIERPKRSLF CLDQKNRFRL
     LCIHIVEWKP FEWLILTMIC ANCLALAIYQ PYSGLDSDFR NTILEMLEYV FIFVFTIECL
     LKIVAYGFVM HPGAYLRNAW NILDFVIIVV GNCSTALSWA NLPNVDVKAL RAFRVLRPLR
     LVSGVPSLQI VLNSVLQAMV PLFHVALLVL FVIIIYAIMG LELFCGKLSR TCVHPDTGLP
     LQGGSSSPCG FGHSARHCSI NANCSETKYW PGPNHGITNF DNIGFAMLTV FTCVSQEGWT
     DVMYWVNDAV GNEWPWIYFV SLVVLGSFFV LNLVLGVLSG EFSKEREKAR VRGIFKKRRE
     KIRFEEELRS YLDWILQAED IWDAVGDEAT FETVENNDAK YTSGSRLDWL LGRFSRLKCK
     KLQMLPFYSS KLRRKGRKLI KSQAFYWIVI VLVFLNTFVL TLEHHRQPLW LEEFQDYVNI
     CFVILFALEM LLKMFCLGFY NYFMSLFNRF DCFVVLCSIV EISLTQARVI KPLGLSVLRS
     ARLLRLFKVT RYWDSLRNLV ASLLNSLRSI VSLLLLLFLF IVIFALLGMQ IFGGKFKFDP
     FGSKPRSNFD SFPQSLLTIL TGEDWNSVMY AGIQSFGGAS SIGIVVCVYF IVLFVCGNYI
     LLNVFLAIAV DNLGDNDQSE PETALPHVNE ETLQEQDDEK MIIDNDNIEQ EEEEEANFEI
     QLCNGETQRE NGQFEQLNNN NWSNSDGTKD ETDDATVLNG NNRKRGASLL AKDDSFGENC
     RKASLLHIPP YNSLLRIACA KLIRHAYFKN LVLLCILVSS ALLAAEDPLS RHSTLNDVLG
     FFDIFFTSVF TVEIVLKIIT FGLVLHEESF CRNAFNLLDL LVVAVSLASF GLKSGAISVV
     KILRVLRVLR PLRAINRAKG LKHVVQCVIV AVKTIGNILL VTFMLQFMFA IVGVQLFKGT
     FYRCTDSTKT NPQDCRGVFI HYDGGDRTKP VVEFREWVNN DFNFDDIRNA LISLFVVGTF
     EGWPDLLYVA IDSTEEDSGP VYNYRQAVAI FFIAYIVVIA FFMQNIFVGF VIITFQNEGE
     REYENCELDK NQRKCIDFTL NVKPQKRYVP SSQFRYKLWL FVTSSYFEYG ILFIIILNTF
     VLAMRHHHPN PITEEVLDFL NFIFTSVFAA EVLLKLMAFT IVNYFADAWN VFDFIVVLGS
     VIDIVCSKVG PGESVISMNF FRLFRVMRLV KLLGRGEGMR TLVWTFLKSF QSLPYVVLLI
     VLLFFIYAVI GMQVFGKIAF DDDTQIHRHN NFRTFYSALL VLFRCATGEA WQNIMLDCSD
     RPTVLCEKAF LHEDEEASGA TTCGTNFAYP YFISFFILSS CLIINLFVAI IMDNFDYLTR
     DWSILGPHHL EEFVRLWSEF DPDARGRIKH LDVLILLRKI SPPLGFGDFC PHRIACKKLI
     SMNMSLFPDG TVGFHATLLA LVRTTSIEMA NIRLRRVIRK VWKKTSESFL DEILPLTTGE
     DDVTVGKFYA TYLIQDYFLR FKRRRMLEAR RMNQTPRHGI KVLMAGLREP IHDSAEPHRR
     YSGNLFADWM KDFEEPQHRR NHILFNGLTN DHQKQQRVNN KNFSSAINYK EHFRKKKNVP
     SLQINKTTHS TSTPNGHVPQ SESDDPQPWR PYPHNACVRL FDLDG
//
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