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Database: UniProt
Entry: A0A183IKL3_9BILA
LinkDB: A0A183IKL3_9BILA
Original site: A0A183IKL3_9BILA 
ID   A0A183IKL3_9BILA        Unreviewed;       969 AA.
AC   A0A183IKL3;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   28-MAR-2018, entry version 10.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
OS   Soboliphyme baturini.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Dioctophymatida; Dioctophymatoidea; Soboliphymatidae; Soboliphyme.
OX   NCBI_TaxID=241478 {ECO:0000313|Proteomes:UP000050793, ECO:0000313|WBParaSite:SBAD_0000434001-mRNA-1};
RN   [1] {ECO:0000313|Proteomes:UP000050793, ECO:0000313|WBParaSite:SBAD_0000434001-mRNA-1}
RP   NUCLEOTIDE SEQUENCE.
RG   Helminth Genomes Consortium;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:SBAD_0000434001-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the
CC       entry of calcium ions into excitable cells and are also involved
CC       in a variety of calcium-dependent processes, including muscle
CC       contraction, hormone or neurotransmitter release, gene expression,
CC       cell motility, cell division and cell death. The isoform alpha-1C
CC       gives rise to L-type calcium currents. Long-lasting (L-type)
CC       calcium channels belong to the 'high-voltage activated' (HVA)
CC       group. They are blocked by dihydropyridines (DHP),
CC       phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA
CC       (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-
CC       GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA).
CC       Calcium channels containing the alpha-1C subunit play an important
CC       role in excitation-contraction coupling in the heart. Binding of
CC       calmodulin or CABP1 at the same regulatory sites results in
CC       opposite effects on the channel function.
CC       {ECO:0000256|RuleBase:RU003808}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003808};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU003808}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family. {ECO:0000256|RuleBase:RU003808}.
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DR   WBParaSite; SBAD_0000434001-mRNA-1; SBAD_0000434001-mRNA-1; SBAD_0000434001.
DR   Proteomes; UP000050793; Genome assembly.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.350; -; 2.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   Pfam; PF00520; Ion_trans; 3.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|RuleBase:RU003808};
KW   Calcium channel {ECO:0000256|RuleBase:RU003808};
KW   Calcium transport {ECO:0000256|RuleBase:RU003808};
KW   Complete proteome {ECO:0000313|Proteomes:UP000050793};
KW   Ion channel {ECO:0000256|RuleBase:RU003808};
KW   Ion transport {ECO:0000256|RuleBase:RU003808};
KW   Membrane {ECO:0000256|SAAS:SAAS00085096, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050793};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00084820,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00084701,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU003808};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003808}.
FT   TRANSMEM     70     89       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    151    172       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    184    206       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    330    346       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    366    391       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    456    478       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    499    520       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    636    654       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    674    695       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    753    783       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    878    903       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    948    967       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN        1    216       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      329    546       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      635    912       Ion_trans. {ECO:0000259|Pfam:PF00520}.
SQ   SEQUENCE   969 AA;  110519 MW;  8B497E770B86D80C CRC64;
     MKVIANGFLL HSGAYLRNGW NILDFLIYCT FNSQYSWVRR ESFASFSCAA TASTGLQVVL
     NSILRAMVPL FHIALLVLFV IIIYAIIGLE LFCGKLHKTC VNANSGEIVG EPGPCGESRT
     SYHCDHGHDI ICTDNHTWPG PNNGITNFDN FGLAMLTVFQ CISLEGWTDV MYWVNDAVGC
     EWPWIYFITL VILGSFFVLN LVLGVLSGEF SKEREKARAR GLFQKFREKQ QLEDDLKGYL
     DWITQAEDIE PVNEEEETES TTREGANAAF RKLALFTLLS LLEPVEGEAT DEGSKEEFRT
     QSWWLKRIRR IKKLNRRCRR FCRKLVKSQA FYWLVIVLVF LNTMVLTSEH YGQPDWLDKF
     QEIANLFFVI LFTLEMFLKI YSLGFVNYFV ALFNRFDCFV VISSILEFAL TFAGLMKPLG
     VSVLRSARLL RIFKVTKYWN SLRNLVASLL NSLRSIASLL LLLFLFIVIF ALLGMQLFGG
     KFNTIDVTMV KPRANFDSFV QSLLTVFQSA GIIVCIYFIV LFICGNYILL NVFLAIAVDN
     LADAESLTAA EKDDENKPED SNLQEVIYAD GNDTNQADQY SGYIEHAECQ LTARPHRISE
     INIPKKVKAI PNASSLFIFS ATNPLRVYCN RFINHSYFTN AVLICILVSS AMLAAEDPLQ
     ASSFRNEVLN YFDYFFTTVF TIEISLKVLV YGLVLHKGSF CRNAFNLLDM LVVGVSLTSF
     GLKSGAISVV KILRVLRVLR PLRAINRAKG LKHVVQCVIV AVKTIGNIML VTFMLQFMFA
     IIGVQLFKGT FFRCNDPSKM TMKECRGSYI NYEGGDINNP QVRNREWQNN DFNFDNVQHA
     MVALFVVSTF EGWPDLLYVA VDSREEDYGP EYNARITVAV FFIAFIVVIA FFMMNIFVGF
     VIVTFQNEGE REKCIEFALT AKPQRRYIPK NRFQYRIWWF VTSQPFEYGI FVIIMLNTLI
     LGMKVSASD
//
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