ID A0A0V1P1M9_9BILA Unreviewed; 1983 AA.
AC A0A0V1P1M9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1F {ECO:0000313|EMBL:KRZ89966.1};
GN ORFNames=T08_7067 {ECO:0000313|EMBL:KRZ89966.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ89966.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ89966.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ89966.1};
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:KRZ89966.1}.
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DR EMBL; JYDM01000062; KRZ89966.1; -; Genomic_DNA.
DR Proteomes; UP000054924; 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; 5.
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:UP000054924};
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 110..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 322..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 486..502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 522..547
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 554..572
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 609..629
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 650..667
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 679..702
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 848..866
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 901..924
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1012..1039
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1093..1111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1123..1143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1163..1182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1189..1208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1254..1274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1340..1364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1520..1554
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 58..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1629..1659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1847..1871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1636..1650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 669
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 985
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 1983 AA; 226719 MW; EDC61893AD057A32 CRC64;
MIVRQVRHHA RSEANFNDDV NIGKELSGNE AAALLHGDEA RASRADLWQQ TLQAAVAAQT
ESSTTTKKRQ QQRKMQRNVQ QERPERSLLC LGLKNPIRKL FISIVEWKPF EWLILCMICA
NCIALAVYQP FPAHDSDRKN AVLEQVEYIF IVVFTIECVM KVIAYGFLFH PGAYLRNGWN
LLDFLIVVIG LISTALSTLN IHGFDVKALR AFRVLRPLRL VSGVPSLQVV LNSILRAMVP
LFHIALLVLF VIIIYAIIGL ELFCGKLHKT CVDQWTGEHV PDPGPCGESH TSFHCDRSKN
LVCTENHTWP GPNDGITNFD NFGLAMLTVF QCISLEGWTD VMYWVNDSVG REWPWIYFIT
LVILGSFFVL NLVLGVLSGE FSKEREKARA RGLFQKFREK QQLEDDLKGY LDWITQAEDI
DLVNEEDEEQ EAMDREEFGA DGEGGEEGGS KEEFQRQSWF SMKIKRLKKL NRRCRRSCRR
IVKSQAFYWL VIVLVFLNTM VLTSEHYGQP EWLDHFQEIA NLFFVVLFTL EMFLKMYSLG
FVNYFVALFN RFDCFVVIGS ILEFALTFAG LMKPLGVSVL RSARLLRIFK VTKYWNSLRN
LVASLLNSLR SIASLLLLLF LFIVIFALLG MQVFGGKFNT IDPNMNKPRA NFDTFVQALL
TVFQILTGED WNAVMYNGIA AFGGVHSIGV IVCIYFIVLF ICGNYILLNV FLAIAVDNLA
DAESLTAAEK EEENKRANEA DPEDDMVVKA TADEDAVSVG QFHESGEVKL PFNEPTDAED
EHLASGDDDQ EREMENQSQF KPTARPHRQS ELNLPKKTKP IPDASSLFLF SSTNKVRIFC
NKVINHSYFT NSVLVCILVS SAMLAAEDPL QASSFRNEVL VYGLILHKGS FCRNAFNLLD
MLVVGVSLTS FGLKSGAISV VKILRVLRVL RPLRAINRAK GTFIEFEGGD VTRPHVRNRE
WTNYDFNFDN VQNAMVALFV VSTFEGWPDL LHVAMDSSDE GIGPQYNARV SVAIFFITFI
VVIAFFMMNI FVGFVIVTFQ SEGEREYENC ELDKNQRKCI EFALTAKPQR RYIPKNRFQY
KIWWFVTSQP FEYAIFIIII LNTLILGMKH YKSSAAFDEA LDVLNLFFTT VFALEFICKL
FALTFKHHKM TRTFDDVLDT MNLIFTGIFA MEFILKVMAF RCKNYFGDAW NVFDFIIVLG
SFIDIIYGKP GSNIISINFF RLFRVMRLVK LLSRGEGIRT LLWTFMKSFQ ALPYVALLIV
LLFFIYAVIG MQIFGKIALN SNTEIHRNNN FQTFPSAVLV LFRSATGEAW QLIMLSCANT
PAAMCDPESD DRGQPCGNDF AYPFFISFFM LCSFLIINLF VAVIMDNFDY LTRDWSILGP
HHLDEFVRLW SEYDPDAKGR IKHLDVVTLL RKISPPLGFG KLCPHRLACK RLVSMNMPLN
SDGTVCFNST LFALVRTNLK IYTEERPFLF LKKSEKVESQ SLVSSNIEEA NEQLRAVIKR
IWKRTPQRLL DEIVPPSGRD DEITVGKFYA TYLIQDYFRR FKKRKEVEQK ETNMQGNITM
SLQAGLRTLH EIGPEIKRAI SGNLETDWSK EFEEPQHRRD HSLFGTLVHA LQAHYKPFIE
GNLTNPAYSN VNGDLKSQEG DDEAEQQHQQ HQQEQQEQQQ QLMFNKMNDL KSPPVKSDRD
KISEFESDES VCNKPERRCN SFFSNIRRRM DSIVSPSIVL FDSDHDSSEH EMQERVRFVP
RGSKPTGLSF EGSRWLPRKL SFRRTPIGGA AAVSNLQQGN NKRLQFSNAI ILDDSDPDSV
LHSENVVDLT ESGDDSKLSV SPPLELRDDA YYLDGIDYNT WRPAPMGQGV RLRGRGNGRR
KSRSMPLPHH EHQRNYADVL VEKVLADQGL GRYADPNLIR TTQLEIAEAY NMTEAQMHSA
ARSLMQRSPK YFEHMGGQRP ADIKDFNQYS KTALLKPREI NSSEEVDISD DMNMFMSVSH
IIN
//