ID F4WE86_ACREC Unreviewed; 1003 AA.
AC F4WE86;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN ORFNames=G5I_03917 {ECO:0000313|EMBL:EGI67524.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI67524.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) 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}.
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DR EMBL; GL888102; EGI67524.1; -; Genomic_DNA.
DR AlphaFoldDB; F4WE86; -.
DR STRING; 103372.F4WE86; -.
DR EnsemblMetazoa; XM_011052894.1; XP_011051196.1; LOC105144165.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; F4WE86; -.
DR Proteomes; UP000007755; 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; -; 3.
DR Gene3D; 6.10.250.2500; -; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 3.
DR InterPro; IPR005821; Ion_trans_dom.
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; PF00520; Ion_trans; 3.
DR PRINTS; PR00167; CACHANNEL.
DR PRINTS; PR01630; LVDCCALPHA1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 3.
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|PIRSR:PIRSR602077-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007755};
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 61..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 435..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 468..486
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 558..578
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 621..649
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 828..846
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 858..881
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 945..978
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 60..337
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 434..672
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 826..979
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..777
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..794
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 617
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 1003 AA; 113455 MW; 130F4DE8D211316B CRC64;
MQPPPSQMGP GAAGAVSKSA QKKPVRRGAK PPPDRPVRAL FCLALTNPVR KLCIKVVEWK
AFEYLILMTI FANCVALAVY TPYPCSDSNL TNQYLEKIEY VFLVIFTVEC VMKIIAYGFV
AHPGAYLRNG WNLLDFTIVV IGMISTVLML LMKEGFDVKA LRAFRVLRPL RLVSGVPSLQ
VVLNSILRAM VPLLHIALLV LFVIIIYAII GLELFSGKMH KTCRHNITDE IMEDPIPCGS
GGFQCYQIGS YYCSKQFWEG PNYGITNFDN FGLSMLTVFQ CITLEGWTDV LYNIEDAMGN
SWQWIYFISM VILGAFFVMN LILGVLSGEF SKEREKAKAR GDFHKLREKQ QIEDDLRGYL
DWITQAEDIE PETDEPKMLQ DGKTKQQNEI ESTDQLEGDE EGIQQESVYK KKKRDLERVN
RRMRRACRKA VKSQVFYWLI IVLVFLNTGV LATEHYDQPE WLDHFQEITN MFFIVLFSME
MILKMYSLGF QGYFVSLFNR FDCFVVIGSI TEMILTNTRV MPPLGVSVLR CVRLLRVFKV
TKYWRSLSNL VASLLNSIQS IASLLLLLFL FIVIFALLGM QVFGGKFNFS DNEEKTRHNF
DSFWQSLLTV FQILTGEDWN AVMYIGILAY GGVAGIGVLA CVYFIILFIC GNYILLNVFL
AIAVDNLADA ESLTAIEKEA EEEEKNKSRS GSPARDEVSG EVGDDGGEGT GGEDEGAGTD
LEHDPNETME DYEAALDTET SEKSEDMNTH KVRLNVESDE EMEEEEEEED EPEEMQGEEQ
EVTARPRRMS EYNTTTKKEP IPAGSAFFIF SSTNRFRVFC HWFCNHSYFS NVILICIMIS
SAMLAAEDPL RTSSERNLIL NYFDYFFTAV FTIEICLKMI SYGFIIHEGA FCRSAFNLLD
LLVVCASLVS MTVKAGAFSF IKVLRVLRVL RPLRAINRAK GLKHVVQCVI VAVKTIGNIV
LVTSLLQFVF AVIGVQLFKV GLSGPDTDMA PRKLSSEPLT VIH
//
