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Database: UniProt
Entry: W5JR46_ANODA
LinkDB: W5JR46_ANODA
Original site: W5JR46_ANODA 
ID   W5JR46_ANODA            Unreviewed;      1625 AA.
AC   W5JR46;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-SEP-2017, entry version 27.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   ORFNames=AND_002447 {ECO:0000313|EMBL:ETN65778.1};
OS   Anopheles darlingi (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Nematocera; Culicoidea;
OC   Culicidae; Anophelinae; Anopheles.
OX   NCBI_TaxID=43151 {ECO:0000313|EMBL:ETN65778.1, ECO:0000313|Proteomes:UP000000673};
RN   [1] {ECO:0000313|EMBL:ETN65778.1, ECO:0000313|EnsemblMetazoa:ADAC002447-PA, ECO:0000313|Proteomes:UP000000673}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20920257; DOI=10.1186/1471-2164-11-529;
RA   Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.;
RT   "Combination of measures distinguishes pre-miRNAs from other stem-
RT   loops in the genome of the newly sequenced Anopheles darlingi.";
RL   BMC Genomics 11:529-529(2010).
RN   [2] {ECO:0000313|EMBL:ETN65778.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Almeida L.G., Nicolas M.F., Souza R.C., Vasconcelos A.T.R.;
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ETN65778.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23761445;
RA   Marinotti O., Cerqueira G.C., de Almeida L.G., Ferro M.I.,
RA   Loreto E.L., Zaha A., Teixeira S.M., Wespiser A.R.,
RA   Almeida E Silva A., Schlindwein A.D., Pacheco A.C., Silva A.L.,
RA   Graveley B.R., Walenz B.P., Lima Bde A., Ribeiro C.A.,
RA   Nunes-Silva C.G., de Carvalho C.R., Soares C.M., de Menezes C.B.,
RA   Matiolli C., Caffrey D., Araujo D.A., de Oliveira D.M., Golenbock D.,
RA   Grisard E.C., Fantinatti-Garboggini F., de Carvalho F.M.,
RA   Barcellos F.G., Prosdocimi F., May G., Azevedo Junior G.M.,
RA   Guimaraes G.M., Goldman G.H., Padilha I.Q., Batista Jda S.,
RA   Ferro J.A., Ribeiro J.M., Fietto J.L., Dabbas K.M., Cerdeira L.,
RA   Agnez-Lima L.F., Brocchi M., de Carvalho M.O., Teixeira Mde M.,
RA   Diniz Maia Mde M., Goldman M.H., Cruz Schneider M.P., Felipe M.S.,
RA   Hungria M., Nicolas M.F., Pereira M., Montes M.A., Cantao M.E.,
RA   Vincentz M., Rafael M.S., Silverman N., Stoco P.H., Souza R.C.,
RA   Vicentini R., Gazzinelli R.T., Neves Rde O., Silva R.,
RA   Astolfi-Filho S., Maciel T.E., Urmenyi T.P., Tadei W.P., Camargo E.P.,
RA   de Vasconcelos A.T.;
RT   "The genome of Anopheles darlingi, the main neotropical malaria
RT   vector.";
RL   Nucleic Acids Res. 41:7387-7400(2013).
RN   [4] {ECO:0000313|EnsemblMetazoa:ADAC002447-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) 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 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}.
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DR   EMBL; ADMH02000580; ETN65778.1; -; Genomic_DNA.
DR   EnsemblMetazoa; ADAC002447-RA; ADAC002447-PA; ADAC002447.
DR   VectorBase; ADAC002447-RA; ADAC002447-PA; ADAC002447.
DR   OMA; PTTKINM; -.
DR   Proteomes; UP000000673; 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; 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   Pfam; PF08763; Ca_chan_IQ; 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.
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:UP000000673};
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:UP000000673};
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     20     38       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     82    104       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    160    181       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    193    215       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    342    359       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    379    396       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    465    485       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    534    557       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    727    753       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    773    794       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    806    832       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    867    886       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    980   1004       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1056   1077       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1089   1107       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1119   1136       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1191   1211       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1280   1304       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1439   1473       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   1625 AA;  186172 MW;  CAFB66818A24949B CRC64;
     MKLVAYGFVM HPGAYLRSRW NMLDFTIVLI GMISTTLSSI MKDGFDVKAL RAFRVLRPLR
     LVSGVPSLQV VLNSILRAMV PLLHIALLVL FVIIIYAIVG LELFSGKMHK TCFHNITGDM
     MEDPTPCGEG GYQCNSIGSH YICRYYWEGP NAGITNFDNF GLSMLTVFQC ITLEGWTDML
     YYIEDAMGSN WQWIYFVSMV ILGAFFVMNL ILGVLSGEFS KERTKAKSRG DFQKLREKQR
     IEEDLKGYLD WITQAEDIDT YQDPPLIGMI QESKMKIVKA NVDNTNNSVG GIAMDSLNQI
     PETTADYIHQ QSESWYKRRL RAWDRFNRKM RRSCRKAVKS QAFYWLIIVL VFLNTGVLAT
     EHYHQPQWLD DFQEYTNMFF VALFSLEMFL KMYSLGLQGY YVSLFNRFDC FVVIGSVVEV
     LLTNTQIMPP LGISVLRCVR LLRVFKVTKY WQSLSNLVAS LLNSIQSIAS LLLLLFLFIV
     IFALLGMQVF GGRFIFNSMD NKPRSNFDSF VQSLLTVFQI LTGEDWNAVM YDGISAYGGV
     ASFGILASIY FIILFICGNY ILLNVFLAIA VDNLADAESL TAVEKDEDPD TELDDIADRP
     EHDGKDEDNE REEEDGETND NADENVSNGD DEQQRQSDRH TIIANASNDD SNIKNVSASL
     EKTQKIRISR VIIQDHCEAI EIPNDRASVH TTYAKRLSEA VVSSSPILMN SEQSLFLLKP
     TNRFRLFCHW LCNHTVFGNI ILLCIMLSSV MLAAEDPLNA NSERNQILNQ FDFFFTAVFA
     IELILKVIAY GFILHKGAFC RSAFNLLDLL VVSVSLISMF FSSGTISVVK ILRVLRVLRP
     LRAINRAKGL KHVVQCVIVA VKTIGNIVLV TFLLQFMFAV IGVQLFKGKF FSCSDRSKYE
     ESDCHGTYLV FEDGNVDKPV SKEREWSNNR FHFDDVQKAM LTLFTVSTFE GWPSLLYVSI
     DSHTENFGPI YNYRPLVATY YIIYIIVIAF FMVNIFVGFV IVTFQNEGEQ EYKNCDLDKN
     QRNCIEFALK AKPVRRYIPN DDRIQYKVWW FVTSQLFEYT IFILIMMNTI TLSMKFYRQP
     QPYTEWLDFF NLLFTAVFAL EFVFKLAAFR FQNYFGDAWN VFDFIIVLGS FIDIVYSEVT
     TTSGTKGAST IISINFFRLF RVMRLIKLLA RGEGIRTLLW TFIKSFQALP YVALLIVMLF
     FIYAVIGMQV FGRIALDDET AIHRNNNFQT FPQAILVLFR SATGEAWQDI MLDCSSREEV
     RCDENSEDKE SKEGCGSNFA FPYFISFYVL CSFLIINLFV AVIMDNFDYL TRDWSILGPH
     HLDEFVRLWS EYDPDAKGRI KHLDVVTLLR KISPPLGFGK LCPHRVACKR LVSMNMPLNS
     DGTVLFNATL FAVVRTSLKI KTEGNIDEAN IELRHIIKQI WKRTSNKLLD QVVPPPGIED
     EVTVGKFYAT YLIQDYFRRF KKRKNYERPN EGISRSEVTL TAGLRILQKK GPRIKRKISG
     TLHESASSIN PEPTHRRNHN LFGFTWSATS ALKHRCFKNG VLGPARQVSA TTKPQRKYAT
     LNKGFKDVNK ALLFGFRSSQ DFMNEHFAND SNTDKSPEKS LKPLCFGEVY SKQTGRVFNA
     KELDV
//
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