ID A0A0V1A6X9_9BILA Unreviewed; 2072 AA.
AC A0A0V1A6X9;
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=CACNA1F {ECO:0000313|EMBL:KRY20599.1};
GN ORFNames=T12_7833 {ECO:0000313|EMBL:KRY20599.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY20599.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY20599.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY20599.1};
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:KRY20599.1}.
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DR EMBL; JYDQ01000023; KRY20599.1; -; Genomic_DNA.
DR Proteomes; UP000054783; 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:UP000054783};
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 146..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 277..296
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 358..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 391..413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 522..538
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 558..583
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 590..608
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 645..665
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 686..703
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 715..738
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 883..901
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 921..942
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1015..1034
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1125..1152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1206..1224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1236..1258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1264..1283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1327..1345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1416..1441
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1596..1630
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 94..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1725..1783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1940..1964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1746..1760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1765..1783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 372
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 705
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1098
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 2072 AA; 236493 MW; 8DFD9687194AA6A3 CRC64;
MGGEGKKKYL CWHRESRPEQ VVPSPIAEPR VASIQTMIVR QVRHHARSEA NFNDDVNIGK
ELSGNEAAAL LHGDEARASR ADLWQQTLQA AVAAQTESST TTKKRQQQRK MQRNVQQERP
ERSLLCLGLK NPIRKLFISI VEWKPFEWLI LCMICANCIA LAVYQPFPAH DSDRKNAVLE
QVEYIFIVVF TIECVMKVIA YGFLFHPGAY LRNGWNLLDF LIVVIGLIST ALSTLNIHGF
DVKALRAFRV LRPLRLVSGV PSLQVVLNSI LRAMVPLFHI ALLVLFVIII YAIIGLELFC
GKLHKTCVDQ WTGEHVPDPG PCGESHTSFH CDRSKNLVCT ENHTWPGPND GITNFDNFGL
AMLTVFQCIS LEGWTDVMYW VNDSVGREWP WIYFITLVIL GSFFVLNLVL GVLSGEFSKE
REKARARGLF QKFREKQQLE DDLKGYLDWI TQAEDIDLVN EEDEEQEAMD REEFGADGEG
GEEGGSKEEF QRQSWFSMKI KRLKKLNRRC RRSCRRIVKS QAFYWLVIVL VFLNTMVLTS
EHYGQPEWLD HFQEIANLFF VVLFTLEMFL KMYSLGFVNY FVALFNRFDC FVVIGSILEF
ALTFAGLMKP LGVSVLRSAR LLRIFKVTKY WNSLRNLVAS LLNSLRSIAS LLLLLFLFIV
IFALLGMQVF GGKFNTIDPN MNKPRANFDT FVQALLTVFQ ILTGEDWNAV MYNGIAAFGG
VHSIGVIVCI YFIVLFICGN YILLNVFLAI AVDNLADAES LTAAEKEEEN KRANEADPED
DMVVKATADE DAVSVGQFHE SGEVKLPFNE PTDAEDEHLA SGDDDHEREM ENQSQFKPTA
RPHRQSELNL PKKTKPIPDA SSLFLFSSTN KVRIFCNKVI NHSYFTNSVL VCILVSSAML
AAEDPLQASS FRNEVLNYFD YFFTTVFTIE ISLKVLVYGL ILHKGSFCRN AFNLLDMLVV
GVSLTSFGLK SGAISVVKIL RVLRVLRPLR AINRAKGLKH VVQCVIVAVK TIGNIMLVTF
MLEFMFAIIG VQIFKGSFFR CTDRARLTAE ECKGTFIEFE GGDVTRPHVR NREWTNYDFN
FDNVQNAMVA LFVVSTFEGW PDLLHVAMDS SDEGIGPQYN ARVSVAIFFI TFIVVIAFFM
MNIFVGFVIV TFQSEGEREY ENCELDKNQR KCIEFALTAK PQRRYIPKNR FQYKIWWFVT
SQPFEYAIFI IIILNTLILG MKHYKSSAAF DEALDVLNLF FTTVFALEFI CKLFALTFKN
YFGDAWNVFD FIIVLGSFID IIYGKPGSNI ISINFFRLFR VMRLVKLLSR GEGIRTLLWT
FMKSFQALPY VALLIVLLFF IYAVIGMQIF GKIALNSNTE IHRNNNFQTF PSAVLVLFRS
ATGEAWQLIM LSCANTPAAM CDPESDDRGQ PCGNDFAYPF FISFFMLCSF LIINLFVAVI
MDNFDYLTRD WSILGPHHLD EFVRLWSEYD PDAKGRIKHL DVVTLLRKIS PPLGFGKLCP
HRLACKRLVS MNMPLNSDGT VCFNSTLFAL VRTNLKIYTE ERPFLFLKKS EKVESQSLVS
SNIEEANEQL RAVIKRIWKR TPQRLLDEIV PPSGRDDEIT VGKFYATYLI QDYFRRFKKR
KEVEQKETNM QGNITMSLQA GLRTLHEIGP EIKRAISGNL ETDWSKEFEE PQHRVGKKKT
SSNRIKFSAG IITLRDHSLF GTLVHALQAH YKPFIEGNLT NPAYSNVNGD LKSQEGDDEA
EQQHQQEQQE 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
//
