ID A0A0V1D2S4_TRIBR Unreviewed; 2202 AA.
AC A0A0V1D2S4;
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:KRY55670.1};
GN ORFNames=T03_3929 {ECO:0000313|EMBL:KRY55670.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY55670.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY55670.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY55670.1};
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:KRY55670.1}.
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DR EMBL; JYDI01000052; KRY55670.1; -; Genomic_DNA.
DR Proteomes; UP000054653; 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: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 263..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 437..458
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 470..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 601..617
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 637..662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 669..687
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 724..744
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 765..782
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 794..817
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 963..981
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1001..1025
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1037..1063
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1098..1117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1208..1235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1289..1307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1319..1339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1359..1376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1388..1406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1452..1472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1538..1562
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1718..1752
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 112..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1852..1882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2070..2094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1859..1873
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 451
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 784
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 2202 AA; 251517 MW; EED226074519CBF0 CRC64;
MLAGGETLLQ IEFSWLLWSR RRSRASYLCW HRESRPEQVV PSPIAEPRVA SIQTMIVRQV
RHHARSEANF NDDVNIGKEL SGNEAAALLH GDEARASRAD LWQQTLQAAV AAQTESSTTT
KKRQQQRKMQ RNVQQERPER SLLCLGLKNP IRKLFISIVE WKPFEWLILC MICANCIALA
VYQPFPAHDS DRKNAVLLCA IGKTFFDFVP AELRPAIDRQ PGTAFQNRKH KLNPQPGQRT
ATVAAVGHTG WGVGLFSEEQ VEYIFIVVFT IECVMKVIAY GFLFHPGAYL RNGWNLLDFL
IVVIGLISTA LSTLNIHGFD VKALRAFRVL RPLRLVSGVP SLQVVLNSIL RAMVPLFHIA
LLVLFVIIIY AIIGLELFCG KLHKTCVDQW TGEHVPDPGP CGESHTSFHC DRSKNLVCTE
NHTWPGPNDG ITNFDNFGLA MLTVFQCISL EGWTDVMYWV NDSVGREWPW IYFITLVILG
SFFVLNLVLG VLSGEFSKER EKARARGLFQ KFREKQQLED DLKGYLDWIT QAEDIDLVNE
EDEEQEAMDR EEFGADGEGG EEGGSKEEFQ RQSWFSMKIK RLKKLNRRCR RSCRRIVKSQ
AFYWLVIVLV FLNTMVLTSE HYGQPEWLDH FQEIANLFFV VLFTLEMFLK MYSLGFVNYF
VALFNRFDCF VVIGSILEFA LTFAGLMKPL GVSVLRSARL LRIFKVTKYW NSLRNLVASL
LNSLRSIASL LLLLFLFIVI FALLGMQVFG GKFNTIDPNM NKPRANFDTF VQALLTVFQI
LTGEDWNAVM YNGIAAFGGV HSIGVIVCIY FIVLFICGNY ILLNVFLAIA VDNLADAESL
TAAEKEEENK RANEADPEDD MVVKATADED AVSVGQFHES GEVKLPFNEP TDAEDEHLAS
GDDDQEREME NQSQFKPTAR PHRQSELNLP KKTKPIPDAS SLFLFSSTNK VRIFCNKVIN
HSYFTNSVLV CILVSSAMLA AEDPLQASSF RNEVPKFVLN 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 QFGEEFLSDL 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
//
