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Database: UniProt
Entry: A0A0V1L9Y5_9BILA
LinkDB: A0A0V1L9Y5_9BILA
Original site: A0A0V1L9Y5_9BILA 
ID   A0A0V1L9Y5_9BILA        Unreviewed;      1665 AA.
AC   A0A0V1L9Y5;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-SEP-2017, entry version 10.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   ORFNames=T02_12006 {ECO:0000313|EMBL:KRZ56261.1};
OS   Trichinella nativa.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichocephalida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ56261.1, ECO:0000313|Proteomes:UP000054721};
RN   [1] {ECO:0000313|EMBL:KRZ56261.1, ECO:0000313|Proteomes:UP000054721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS10 {ECO:0000313|EMBL:KRZ56261.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KRZ56261.1}.
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DR   EMBL; JYDW01000097; KRZ56261.1; -; Genomic_DNA.
DR   Proteomes; UP000054721; 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:UP000054721};
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:UP000054721};
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     71     89       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    109    129       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    141    159       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    203    221       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    316    338       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    444    462       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    477    500       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    570    592       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    642    670       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    806    824       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    844    865       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    877    903       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    923    953       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1048   1075       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1118   1144       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1156   1182       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1253   1275       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1351   1372       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1500   1534       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   1665 AA;  190802 MW;  94C7F7EADA29767C CRC64;
     MSAENYTTPS DTTIVDSCLL SSTVAGTTPT TRSKRNNSSY TIERPKRSLF CLDQKNRFRL
     LCIHIVEWKP FEWLILTMIC ANCLALAIYQ PYSGLDSDFR NTILEMLEYV FIFVFTIECL
     LKIVAYGFVM HPGAYLRNAW NILDFVIIVV GNCSTALSWA NLPNVDVKAL RAFRVLRPLR
     LVSGVPSLQI VLNSVLQAMV PLFHVALLVL FVIIIYAIMG LELFCGKLSR TCVHPDTGLP
     LQGGSSSPCG FGHSARHCSI NANCSETKYW PGPNHGITNF DNIGFAMLTV FTCVSQEGWT
     DVMYWVNDAV GNEWPWIYFV SLVVLGSFFV LNLVLGVLSG EFSKEREKAR VRGIFKKRRE
     KIRFEEELRS YLDWILQAED IWDAVGDEAT FETVENNDAK YTSGSRLDWL LGRFSRLKCK
     KLQMLPFYSS KLRRKGRKLI KSQAFYWIVI VLVFLNTFVL TLEHHRQPLW LEEFQDYVNI
     CFVILFALEM LLKMFCLGFY NYFMSLFNRF DCFVVLCSIV EISLTQARVI KPLGLSVLRS
     ARLLRLFKVT RYWDSLRNLV ASLLNSLRSI VSLLLLLFLF IVIFALLGMQ IFGGKFKFDP
     FGSKPRSNFD SFPQSLLTIL TGEDWNSVMY AGIQSFGGAS SIGIVVCVYF IVLFVCGNYI
     LLNVFLAIAV DNLGDNDQSE PETALPHVNE ETLQEQDDEK MIIDNDNIEQ EEEEEANFEI
     QLCNGETQRE NGQFEQLNNN NWSNSDGTKD ETDDATVLNG NNRKRGASLL AKDDSFGENC
     RKASLLHIPP YNSLLRIACA KLIRHAYFKN LVLLCILVSS ALLAAEDPLS RHSTLNDVLG
     FFDIFFTSVF TVEIVLKIIT FGLVLHEESF CRNAFNLLDL LVVAVSLASF GLKSGAISVV
     KILRVLRVLR PLRAINRAKG LKHVVQCVIV AVKTIGNILL VTFMLQFMFA IVGVQLFKGT
     FYRCTDSTKT NPQDCRGVFI HYDGGDRTKP VVEFREWVNN DFNFDDIRNA LISLFVVGTF
     EGWPDLLYVA IDSTEEDSGP VYNYRQAVAI FFIAYIVVIA FFMQNIFVGF VIITFQNEGE
     REYENCELDK NQRKCIDFTL NVKPQKRYVP SSQFRYKLWL FVTSSYFEYG ILFIIILNTF
     VLAMRHHHPN PITEEVLDFL NFIFTSVFAA EVLLKLMAFT IVNYFADAWN VFDFIVVLGS
     VIDIVCSKVG PGESVISMNF FRLFRVMRLV KLLGRGEGMR TLVWTFLKSF QSLPYVVLLI
     VLLFFIYAVI GMQVFGKIAF DDDTQIHRHN NFRTFYSALL VLFRCATGEA WQNIMLDCSD
     RPTVLCEKAF LHEDEEASGA TTCGTNFAYP YFISFFILSS CLIINLFVAI IMDNFDYLTR
     DWSILGPHHL EEFVRLWSEF DPDARGRIKH LDVLILLRKI SPPLGFGDFC PHRIACKKLI
     SMNMSLFPDG TVGFHATLLA LVRTTSIEMA NIRLRRVIRK VWKKTSESFL DEILPLTTGE
     DDVTVGKFYA TYLIQDYFLR FKRRRMLEAR RMNQTPRHGI KVLMAGLREP IHDSAEPHRR
     YSGNLFADWM KDFEEPQHRR NHILFNGLTN DHQKQQRVNN KNFSSAINYK EHFRKKKNVP
     SLQINKTTHS TSTPNGHVPQ SESDDPQPWR PYPHNACVRL FDLDG
//
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