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Database: UniProt
Entry: A0A091PPN2_LEPDC
LinkDB: A0A091PPN2_LEPDC
Original site: A0A091PPN2_LEPDC 
ID   A0A091PPN2_LEPDC        Unreviewed;      1235 AA.
AC   A0A091PPN2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   28-MAR-2018, entry version 19.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
DE   Flags: Fragment;
GN   ORFNames=N330_02524 {ECO:0000313|EMBL:KFQ09263.1};
OS   Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae;
OC   Leptosomus.
OX   NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ09263.1, ECO:0000313|Proteomes:UP000053001};
RN   [1] {ECO:0000313|EMBL:KFQ09263.1, ECO:0000313|Proteomes:UP000053001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ09263.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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
CC       opposite 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; KK676465; KFQ09263.1; -; Genomic_DNA.
DR   Proteomes; UP000053001; 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   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.350; -; 4.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR005450; VDCC_L_a1ssu.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR10037:SF190; PTHR10037:SF190; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
DR   PRINTS; PR01634; LVDCCALPHA1S.
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:UP000053001};
KW   Ion channel {ECO:0000256|RuleBase:RU003808};
KW   Ion transport {ECO:0000256|RuleBase:RU003808};
KW   Membrane {ECO:0000256|SAAS:SAAS00085096, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053001};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00084820,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00084701,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU003808};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003808}.
FT   TRANSMEM     58     75       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     95    115       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    192    213       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    311    333       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    434    451       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    471    489       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    563    582       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    635    662       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    796    818       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    838    859       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    917    947       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1042   1069       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1123   1144       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1165   1183       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       54    343       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      433    670       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      800   1075       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN     1119   1214       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   NON_TER    1235   1235       {ECO:0000313|EMBL:KFQ09263.1}.
SQ   SEQUENCE   1235 AA;  140607 MW;  1AAADFEEF9BB2996 CRC64;
     MEPASPQDDV KKRQQKEKSK KPVPPAAPRP ARALFCLTLQ NPLRKACISI VEWKPFEIII
     LLTIFANCVA LAIYLPMPED DTNVANSSLE KIEYAFLIFF AIEAMLKIIA YGFLFHTDAY
     LRNGWNVLDF SIVSLGLITM TLEQVNAKQG GTSGGKGGFD VKALRAFRVL RPLRLVSGVP
     SLQVVLNSII KAMVPLLHIA LLVLFMIIIY AIVGQELFKG KMHKTCYYFG TDVIATVASE
     KPAPCTSSGH GRHCTINGTE CRSGWPGPNN GITHFDNFGF AMLTVYQCIT MEGWTEVLYW
     VNDAIGNEWP WIYFVSLILL GSFFVLNLVL GVLSGEFTKE REKAKSRGTF QKLREKQQLE
     EDLKGYMDWI THAEVMDSDR ARGEGMMPSD EGGSETESLY EIEGMNKWIL YFRQWRRWNR
     MFRRKCRDVV KSKFFYWLVI LLVALNTLSI ASEHHFQPEW LTQVQDNANR VLLALFVAEM
     LLKMYALGLR QYFMSLFNRF DCFVVCAGIL ETILVELGTL SPLGISVLRC IRLLRIFKIT
     RYWTSLSNLV ASLLNSVRSI ASLLLLLFLF IIVFALLGMQ LFGGKFDFED MEVRRSTFDN
     FPQALISVFQ ILTGEDWNSI MYDGIMAYGG PSFPGMLVCI YFIILFVCGN YILLNVFLAI
     AVDNLAEAES LTLAQKAKAE ERKRRKMSRA YPEKSEDEKQ MLAKKLEQKA KGEGIPTTAK
     LKVDEFESNV NEIKDPYPSA DFPGDDEEDE PEIPLSPRPR PLAELQLKEK AVPMPEASSF
     FIFSPTNKFR MLCHRIVNAT WFTNFILLFI LLSSISLAAE DPIRAESFRN QILKYFDIGF
     TSVFTVEIVL KMTAYGAFLH KGSFCRNSFN ILDLLVVAVS LTSMGIESST ISVVKILRVL
     RVLRPLRAIN RAKGLKHVVQ CVFVAIKTIG NIVVVTTLLQ FMFACIGVQL FKGKFYRCTD
     PSKMTEKECR GYFINYVDGD PTQIELQERV WLHSNFHFNN VFSAMMSLFT VSTFEGWPEL
     LYMAIDTNAE DRGPIYNYRV EIAMFFIIYI ILIAFFMMNI FVGFVIVTFQ EQGESEYKNC
     ELDKNQRQCV QYALKARPLR RYIPKNPYQY QIWYVVTSSY FEYLMFFLIL LSAGAPGTVL
     LKWLPPQPSP QHYNQSAEMN YVSDILNVAF TILFTLEMIL KLMAFKAKGY FGDPWNVFDF
     LIVIGSIIDV ILSEIDTVLA SSGGLYCLGG GCDSV
//
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