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Database: UniProt
Entry: A0A0V0TY85_9BILA
LinkDB: A0A0V0TY85_9BILA
Original site: A0A0V0TY85_9BILA 
ID   A0A0V0TY85_9BILA        Unreviewed;      1962 AA.
AC   A0A0V0TY85;
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   Name=CACNA1F {ECO:0000313|EMBL:KRX43957.1};
GN   ORFNames=T05_15844 {ECO:0000313|EMBL:KRX43957.1};
OS   Trichinella murrelli.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichocephalida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX43957.1, ECO:0000313|Proteomes:UP000055048};
RN   [1] {ECO:0000313|EMBL:KRX43957.1, ECO:0000313|Proteomes:UP000055048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS417 {ECO:0000313|EMBL:KRX43957.1};
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:KRX43957.1}.
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DR   EMBL; JYDJ01000107; KRX43957.1; -; Genomic_DNA.
DR   Proteomes; UP000055048; 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; IPR031688; CAC1F_C.
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; PF16885; CAC1F_C; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 5.
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:UP000055048};
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:UP000055048};
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    146    165       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    243    264       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    276    296       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    336    355       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    417    438       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    450    472       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    581    597       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    617    642       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    649    667       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    704    724       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    745    762       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    774    797       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    943    961       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    981   1005       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1078   1097       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1188   1215       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1269   1287       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1299   1319       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1387   1412       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1549   1583       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   1962 AA;  223272 MW;  E1D23DBBC0FA1F97 CRC64;
     MHAWKEYLCW HRESRPEQVV PSPIAEPRVA SIQTMIVRQV RHHARSEANF NDDVNIGKEL
     SGNEAAALLH GDEARASRAD LWQQTLQAAV AAQTESSTTT KKRQQQRKMQ RNVQQERPER
     SLLCLGLKNP IRKLFISIVE WKPFEWLILC MICANCIALA VYQPFPAHDS DRKNAVLLCA
     IGKTFFDFVP AELRPAIDRQ PGTAFQNRKH KLNPQPGQRT ATVAAVGHTG WGVGLFSEEQ
     VEYIFIVVFT IECVMKVIAY GFLFHPGAYL RNGWNLLDFL IVVIGLISTA LSTLNIHGFD
     VKALRAFRVL RPLRLVSGVP SLQVVLNSIL RAMVPLFHIA LLVLFVIIIY AIIGLELFCG
     KLHKTCVDQW TGEHVPDPGP CGESHTSFHC DRSKNLVCTE NHTWPGPNDG ITNFDNFGLA
     MLTVFQCISL EGWTDVMYWV NDSVGREWPW IYFITLVILG SFFVLNLVLG VLSGEFSKER
     EKARARGLFQ KFREKQQLED DLKGYLDWIT QAEDIDLVNE EDEEQEAMDR EEFGADGEGG
     EEGGSKEEFQ RQSWFSMKIK RLKKLNRRCR RSCRRIVKSQ AFYWLVIVLV FLNTMVLTSE
     HYGQPEWLDH FQEIANLFFV VLFTLEMFLK MYSLGFVNYF VALFNRFDCF VVIGSILEFA
     LTFAGLMKPL GVSVLRSARL LRIFKVTKYW NSLRNLVASL LNSLRSIASL LLLLFLFIVI
     FALLGMQVFG GKFNTIDPNM NKPRANFDTF VQALLTVFQI LTGEDWNAVM YNGIAAFGGV
     HSIGVIVCIY FIVLFICGNY ILLNVFLAIA VDNLADAESL TAAEKEEENK RANEADPEDD
     MVVKATADED AVSVGQFHES GEVKLPFNEP TDAEDEHLAS GDDDQEREME NQSQFKPTAR
     PHRQSELNLP KKTKPIPDAS SLFLFSSTNK VRIFCNKVIN HSYFTNSVLV CILVSSAMLA
     AEDPLQASSF RNEVPKFVLN YFDYFFTTVF TIEISLKVLV YGLILHKGSF CRNAFNLLDM
     LVVGVSLTSF GLKSGAISVV KILRVLRVLR PLRAINRAKG LKHVVQCVIV AVKTIGNIML
     VTFMLEFMFA IIGVQIFKGS FFRCTDRARL TAEECKGTFI EFEGGDVTRP HVRNREWTNY
     DFNFDNVQNA MVALFVVSTF EGWPDLLHVA MDSSDEGIGP QYNARVSVAI FFITFIVVIA
     FFMMNIFVGF VIVTFQSEGE REYENCELDK NQRKCIEFAL TAKPQRRYIP KNRFQYKIWW
     FVTSQPFEYA IFIIIILNTL ILGMKHYKSS AAFDEALDVL NLFFTTVFAL EFICKLFALT
     FKNYFGDAWN VFDFIIVLGS FIDIIYGKVS VPTGEAWQLI MLSCANTPAA MCDPESDDRG
     QPCGNDFAYP FFISFFMLCS FLIINLFVAV IMDNFDYLTR DWSILGPHHL DEFVRLWSEY
     DPDAKGRIKH LDVVTLLRKI SPPLGFGKLC PHRLACKRLV SMNMPLNSDG TVCFNSTLFA
     LVRTNLKIYT EVSSNIEEAN EQLRAVIKRI WKRTPQRLLD EIVPPSGRDD EITVGKFYAT
     YLIQDYFRRF KKRKEVEQKE TNMQGNITMS LQAGLRTLHE IGPEIKRAIS GNLETDWSKE
     FEEPQHRRDH SLFGTLVHAL QAHYKPFIEG NLTNPAYSNV NGDLKSQEGF LNSNPTNLYA
     TSRNGAVIHF SPTYVVEWTA LVLFDSDHDS SEHEMQERVR FVPRGSKPTG LSFEGSRWLP
     RKLSFRRTPI GGAAAVSNLQ QGNNKRLQFS NAIILDDSDP DSVLHSENVV DLTESGDDSK
     LSVSPPLELR DDAYYLDGID YNTWRPAPMG QGVRLRGRGN GRRKSRSMPL PHHEHQRNYA
     DVLVEKVLAD QGLGRYADPN LIRTTQLEIA EAYNMTEAQM HSAARSLMQR SPKYFEHMGG
     QRPADIKDFN QYSKTALLKP REINSSEEVD ISDDMNMFMS VV
//
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