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Database: UniProt
Entry: A0A016VHS1_9BILA
LinkDB: A0A016VHS1_9BILA
Original site: A0A016VHS1_9BILA 
ID   A0A016VHS1_9BILA        Unreviewed;      1085 AA.
AC   A0A016VHS1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-SEP-2017, entry version 17.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=Acey_s0010.g1096 {ECO:0000313|EMBL:EYC26333.1};
GN   ORFNames=Y032_0010g1096 {ECO:0000313|EMBL:EYC26333.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Strongylida; Ancylostomatoidea; Ancylostomatidae; Ancylostomatinae;
OC   Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC26333.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
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 an
CC       opposit 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EYC26333.1}.
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DR   EMBL; JARK01001346; EYC26333.1; -; Genomic_DNA.
DR   Proteomes; UP000024635; Unassembled WGS sequence.
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   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
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:UP000024635};
KW   Ion channel {ECO:0000256|RuleBase:RU003808};
KW   Ion transport {ECO:0000256|RuleBase:RU003808};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU003808};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003808}.
FT   TRANSMEM     91    107       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    127    152       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    158    176       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    220    239       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    309    330       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    342    364       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    469    487       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    499    517       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    592    612       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    669    690       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    796    814       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    834    855       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    867    893       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    913    942       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1038   1065       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       87    374       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      468    705       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      795   1072       Ion_trans. {ECO:0000259|Pfam:PF00520}.
SQ   SEQUENCE   1085 AA;  123186 MW;  601A3A85F91B5958 CRC64;
     MTTLQSMMSS ADEEEPPPPD HERVDLWQQT LQAAVAASSG QDPAKKRPQQ RKPLRQTNVV
     ERSERSLLCL SLNNPIRKIC IAVVEWRPFE YLILLMICAN CIALAVYQPY PAQDSDSKNT
     ILEQIEYLFI VVFTIECILK VVALGFICHP GAYLRNAWNI LDFIIVVIGL VSTVLSRMNI
     QGFDVKALRA FRVLRPLRLV SGVPSLQVVL NAILRAMIPL LHIALLVLFV ILIYAIIGLE
     LFCGKLHSTC VDPATGQLAQ KDPTPCGTVG SAFKCEPSDA LTGMGVKWEC SSNTSWPGPN
     NGITNFDNFG LAMLTVFQCV SLEGWTDVMY WVNDAVGREW PWIYFVTLVI LGSFFVLNLV
     LGVLSGEFSK EREKARARGL FQKFREKQQL EEDLKGYLDW ITQAEDIDPV NDEQEEEPQA
     TATGEEVDEE GEERAEEARP SKWRSRMKRF EKTNRRCRRA CRRLVKSQTF YWLVILLVLL
     NTLVLTSEHY GQSEWLDDFQ TMANLFFVIL FSLEMLLKMY SLGFTTYTTS QFNRFDCFVV
     ISSIIEFVLL YLRLMKPLGV SVLRSARLLR IFKVTKYWTS LRNLVSSLLN SLRSIMSLLL
     LLFLFIVIFA LLGMQVFGGK FNFNPQQPKP RANFDTFIQS LLTVFQILTG EDWNTVMYNG
     IESFGGVGTL GVIVSIYYIV LFICGNYILL NVFLAIAVDN LADADSLTNA EKEEEQQELE
     GEEEYDEEGE GFGEGDDRMD MEEQEPGEDM VTARPRRMSE LPPTTPHKPI PKASSLFILS
     HTNPFRVFCN KIVNHSYFTN SVLVCILVSS AMLAAEDPLE ANSSRNTVLN YFDYFFTTVF
     TIEITLKVVV FGLVFHKGSF CRNAFNLLDI LVVAVSLVSF VLKSDAISVV KILRVLRVLR
     PLRAINRAKG LKHVVQCVIV AVKTIGNIML VTFMLQFMFA IIGVQLFKGT FFSCNDLSKM
     TEAECRGEYI HYEDGDPTKP VSKKRVWSNN DFNFDNVGDA MVSLFVVSTF EGWPDLLYVA
     INSNEEDRGP VHNSRQAVAL FFIAFIIVIA FFMMNIFVGF VIVTFQNEGE REYENCELDK
     NQKYE
//
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