ID A0A0V1CJK9_TRIBR Unreviewed; 1920 AA.
AC A0A0V1CJK9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Voltage-dependent calcium channel type A subunit alpha-1 {ECO:0000313|EMBL:KRY49214.1};
GN Name=CAC {ECO:0000313|EMBL:KRY49214.1};
GN ORFNames=T03_9250 {ECO:0000313|EMBL:KRY49214.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY49214.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY49214.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY49214.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, 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:KRY49214.1}.
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DR EMBL; JYDI01000182; KRY49214.1; -; Genomic_DNA.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; IPR002048; EF_hand_dom.
DR InterPro; IPR031649; GPHH_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014873; VDCC_a1su_IQ.
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:SF7; VOLTAGE-DEPENDENT CALCIUM CHANNEL TYPE A 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 SMART; SM01062; Ca_chan_IQ; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
DR PROSITE; PS50222; EF_HAND_2; 1.
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
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 70..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 255..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 288..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 433..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 463..484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 558..580
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 767..785
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 805..825
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 834..853
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 900..922
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1013..1037
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1095..1113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1125..1145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1205..1234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1304..1328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1344..1379
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 19..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1896..1920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 269
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 612
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 1920 AA; 219628 MW; DD817D60D0BD280B CRC64;
MNLRIDDIAR LASERTKLQL HSQSLDSSAD KSSQARRIPG KRGDGKGPTS LFIFTENNLV
RRYAQISLTV SFFTPFEYFI LMTIIANCIV LALDQHLPHN DKMPLSLKLE ATEPYFMGIF
TIECLLKIIA FGFVMHKGSY LRSGWNILDF IVVMSGVISM LPFTTSGVDL RTLRAVRVLR
PLKLVSGIPS LQVVLKSILC AMAPLLQIGI PVAIGNKPFP CTNKSTTGAY HCPEGTTCKE
QWIGPNYGIT SFDNIAFAML TVFQCITMEG WTNVMYYTND SQGDTFNWLY FIPLIILGSF
FMLNLVLGVL SGEFAKERER VENRREFLKL RRQQHIEREL NGYLEWICKA EEVILNEERT
TEEERKAIME ARHLAVSKQL KHLVQQSTET EDDLEEEDLD VEFRTKDLSQ TGKCWLVVRR
LRVFVRRFVK TQFFYWLVIT LVFLNTVCVS IEHYGQPQWL DEFLYYAEWT FLGIFLFEML
FKMFGLGIGT YFQSSFNIFD FVVITGSLFE VIWEELKGGS FGISVLRALR LLRIFKVTKY
WTSLRNLVVS LMNSMRSIIS LLFLLFLFIL IFALLGMQLF GGEFNFPEGR PSTHFDTFPV
ALITVFQILT GEDWNEVMYL AIESQNDTLL NVFLAIAVDN LANAQELTAA EEAHEQEVQS
TYSSADIKND ECEYEKGPKM IENLSQNGQA KLTDACDAVC DVKNTLNIQE NKTVTSAPLC
YVNSIDESDS NCAFGGHREI VPYSSLFIFS PKNRFRIFVH KIVCTKYFEM AIMVVICLSS
ISLAAEDPVD ESNPRNKYLN YLDYAFTAVF TIEMILKVID MGVIIHPGSY CRDLWNIMDA
TVVICALVGF AFVDSTKAGK NLSTIKSLRV LRVLRPLKTI KRIPKLKAVF DCVVNSLKNV
FNILIVFILF QFIFAVIAVQ LFKGKFFYCT DRTKRFEQDC QGYFFHYDKQ GSPPQVVQRE
WTSFALNYDN TIHAMLTLFT VTTGEGWPGI RQASIDATEE NQGPIPFNHI EVALFYVVYF
IVFPFFFVNI FVALIIITFQ EQGEAELAEG DLDKNQKQCI DFALNARPVC RYIPEDKDSI
KYHIWKMVVS TPFEYFIMAM ICLNTIILMM SYYQEPPAYR AVLRYLNSTL TAVFTVEAIL
KILAFGVRNY FKDGWNIFDF ITVIGSITDA LVTEFGGNFV SLGFLRLFRA ARLIKLLRQG
YTIRILLWTF VQSFKALPYV CLLIGMLFFI YAIVGMQVFG NIELNGDTEI NRHNNFQTFF
NSIILLFRCA TGEAWQEVTL ACIANRKCDP RTGKLNNECG TNFAYVYFTS FVFLSSFLML
NLFVAVIMDN FDYLTRDSSI LGPHHLDEFV RVWAEYDPEA TGRIHYTDMY EMLRNIPPPV
GFGRKCPYRL AYKHLIRMNM PVDEDGTVQF TTTLFALIRE SLSIKMRSAD EMDRADMELR
KTLKKLWPIH AKKNLTDLAV PPNSKLCNKK LTVGKIYAGL LLLENFRSKR CGRVPDRSTF
LFGRLVDAAL KEKEKIHSSE ADPSSCTEFF SDSEPPRSEI RYGFEHQRRM LPTAEQPRIF
DIPGKWQTHD EMNSQMQSIY VPQDEYNNER VQHRRKVLRR QQEDDRVDGF ASAQEWHNYA
RQRMQRCTDS KNKALSERAN LDHYYVTGLA DAKSHHESAS NVLFNQLSPV LGHSFSPAFV
EKIPSPACYF HQQLPMVWEN PVTNKFSEVS HLKAHPMFKS SPELQQCVGK RKRLAAKTAR
TFCTSTIRPH REVENYAEFL QLSDDESCNY SARSAKQTVF DSNLMSPLTV SPDPAFFSSS
SSSSDASFVN VSCPAQQNVN TSSYASYCQI SPDNSYIFAG NPTSSGEHPV RSSQSSGATY
KLSGYKTAGH CQPALKEPNQ QRLYCMRSNG PNADEHHCHS VVHSQPGHIP LSDSEQEDWC
//
