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Database: UniProt
Entry: A0A0V1CUD9_TRIBR
LinkDB: A0A0V1CUD9_TRIBR
Original site: A0A0V1CUD9_TRIBR 
ID   A0A0V1CUD9_TRIBR        Unreviewed;      1880 AA.
AC   A0A0V1CUD9;
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=T03_15840 {ECO:0000313|EMBL:KRY52906.1};
OS   Trichinella britovi (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichocephalida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY52906.1, ECO:0000313|Proteomes:UP000054653};
RN   [1] {ECO:0000313|EMBL:KRY52906.1, ECO:0000313|Proteomes:UP000054653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS120 {ECO:0000313|EMBL:KRY52906.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-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:KRY52906.1}.
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DR   EMBL; JYDI01000096; KRY52906.1; -; Genomic_DNA.
DR   Proteomes; UP000054653; 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:UP000054653};
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:UP000054653};
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    512    530       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    570    594       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    615    636       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    642    665       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    815    833       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    853    874       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    886    912       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    932    962       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1057   1084       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1127   1153       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1165   1191       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1262   1284       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1360   1381       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1516   1550       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   1880 AA;  215257 MW;  B2CF6C1A9CFA732F CRC64;
     MSAENYTTPS DTTIVDSCLL SSTVAGTTPT ARSKRNNSSY 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 SFPQSLLTVF QVGHFLIIPY LFLLWIQSFG GASSIGIVVC VYFIVLFVCG
     NYILLNVFLA IAVDNLGDND QSEPETALPH VNEETLQEQD DEKMMIDNDN IEQEEEANFE
     IQLCNGETQR ENGQFEQLNN NNWSNSDGTK DETDDATVLN GNNRKRGASL LAKDDSFGEN
     CRKASLLHIP PYNSLFIFSP QNKLRIACAK LIRHAYFKNL VLLCILVSSA LLAAEDPLSR
     HSTLNDVLGF FDIFFTSVFT VEIVLKIITF GLVLHEESFC RNAFNLLDLL VVAVSLASFG
     LKSGAISVVK ILRVLRVLRP LRAINRAKGL KHVVQCVIVA VKTIGNILLV TFMLQFMFAI
     VGVQLFKGTF YRCTDSTKTN PQDCRGVFIH YDGGDRTKPV VEFREWVNND FNFDDIRNAL
     ISLFVVGTFE GWPDLLYVAI DSTEEDSGPV YNYRQAVAIF FIAYIVVIAF FMQNIFVGFV
     IITFQNEGER EYENCELDKN QRKCIDFTLN VKPQKRYVPS SQFRYKLWLF VTSSYFEYGI
     LFIIILNTFV LAMRHHHPNP ITEEVLDFLN FIFTSVFAAE VLLKLMAFTI VNYFADAWNV
     FDFIVVLGSV IDIVCSKVGP GESVISMNFF RLFRVMRLVK LLGRGEGMRT LVWTFLKSFQ
     SLPYVVLLIV LLFFIYAVIG MQVFGKIAFD DDTQIHRHNN FRTFYSALLV LFRCATGEAW
     QNIMLDCSDR PTVLCEKAFL HEDEEASGAT TCGTNFAYPY FISFFILSSC LIINLFVAII
     MDNFDYLTRD WSILGPHHLE EFVRLWSEFD PDARGRIKHL DVLILLRKIS PPLGFGDFCP
     HRIACKKLIS MNMSLFPDGT VGFHATLLAL VRTSLNIFCD NSIEMANIRL RRVIRKVWKK
     TSESFLDEIL PLTTGEDDVT VGKFYATYLI QDYFLRFKRR RMLEARRMNQ TPRHGIKVLM
     AGLREPIHDS AEPHRRYSGN LFADWMKDFE EPQHRRNHIL FNGLTNDHQK HQRVNNKNFS
     SAINYKEHFR KKKNVPSLQI NKTTHSTSTP NGHVPQSESD DPQPWRPYPH NACVRLFDLH
     SVKRTNCLTS GKLTAWQMAH QLLLSYMQCN SHPHTAVAPM GRPVANETPI APNNRLRTMD
     QEKTSARHCN SGCKLSTNPT ARWDFFPNST TRLATEITDA CDIPFPFRWY LKLFFIPSQR
     GFGFITNKLE GIEKGWTADV DQVKVDGGEC CKREESSKVG RLKAVRVLEH SGKRRERSPP
     LVERCLNGIR STRVACAPSD
//
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