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Database: UniProt
Entry: A0A0Q3URY0_AMAAE
LinkDB: A0A0Q3URY0_AMAAE
Original site: A0A0Q3URY0_AMAAE 
ID   A0A0Q3URY0_AMAAE        Unreviewed;      2157 AA.
AC   A0A0Q3URY0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   25-OCT-2017, entry version 12.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   ORFNames=AAES_102344 {ECO:0000313|EMBL:KQK79546.1};
OS   Amazona aestiva (Blue-fronted Amazon parrot).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX   NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK79546.1, ECO:0000313|Proteomes:UP000051836};
RN   [1] {ECO:0000313|EMBL:KQK79546.1, ECO:0000313|Proteomes:UP000051836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FVVF132 {ECO:0000313|EMBL:KQK79546.1};
RA   Millard Andrew;
RL   Submitted (OCT-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:KQK79546.1}.
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DR   EMBL; LMAW01002581; KQK79546.1; -; Genomic_DNA.
DR   Proteomes; UP000051836; 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; IPR005451; VDCC_L_a1csu.
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   PRINTS; PR01635; LVDCCALPHA1C.
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:UP000051836};
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:UP000051836};
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     12     32       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     44     61       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    117    139       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    232    254       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    366    384       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    404    429       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    479    501       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    544    566       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    729    747       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    791    809       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    816    838       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    850    876       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    897    930       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    980   1001       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1022   1048       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1099   1120       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1132   1150       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1381   1404       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1474   1498       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1632   1666       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
SQ   SEQUENCE   2157 AA;  243771 MW;  1F28C7166F15E97B CRC64;
     MHVRCTQVER VEYLFLIIFT VEAFLKVIAY GLLFHPNAYL RNGWNLLDFI IVVVGLFSAI
     LEQATKADGV NSIGGKGAGF DVKALRAFRV LRPLRLVSGV PSLQVVLNSI IKAMVPLLHI
     ALLVLFVIII YAIIGLELFM GKMHKTCYHV QGGLIDTPAE DDPSPCAPQS AHGRQCQNGT
     ECKAGWEGPK HGITNFDNFA FAMLTVFQCI TMEGWTDVLY WMQDAMGYEL PWVYFVSLVI
     FGSFFVLNLV LGVLSGEFSK EREKAKARGD FQKLREKQQL EEDLKGYLDW ITQAEDIDPE
     NEDEGMDEEK PRNMSMPTSE TESVNTDNVP GADIEGENXG ARLARYWRRW NRFCRRKCRA
     AVKSNVFYWL VIFLVFLNTL TIASEHYNQP DWLTEVQEML LKMYSLGLQA YFVSLFNRFD
     CFIVCGGILE TILVETKIMS PLGISVLRCV RLLRIFKITR YWNSLSNLVA SLLNSVRSIA
     SLLLLLFLFI IIFSLLGMQL FGGKFNFDEM QTRRSTFDNF PQSLLTVFQI LTGEDWNSVM
     YDGIMAYGGP SFPGMLVCIY FIILFICGNC HLEGISCADL FGSSYVLVSR FPCLLECNEG
     QNFVGNLVTA SPEKKQEIEK TAVEEETKEE KIELKSITAD GESPPATKIN VDDYQPNENE
     EKSPYPTTEA PAEEDEEEPE MPVGPRPRPM SELHLKEKAV PMPDASAFFI FSPNNRFRVH
     CHRIVNDNIF TNLILFFILL SSISLAAEDP VRHLSFRNQG LILILFTLVK IRSNTLEFDV
     VTLEENGAIK ILFYFDIVFT VIFTIEIALK ILGNADYVFT SIFTLEIILK MTAYGAFLHK
     GSFCRNYFNI LDLLVVSVSL ISFGIQSSAI NVVKILRVLR VLRPLRAINR AKGLKHVVQC
     VFVAIRTIGN IVIVTTLLQF MFACIGVQLF KGKLYSCTDS SKQTEAECRG YYITYKDGEV
     NQPMIQPRSW ENSKFDFDNV LTAMMALFTV STFEGWPELL YRSIDSHMED VGPIYNHRVE
     ISIFFIIYII IIAFFMMNIF VGFVIVTFQE QGEQEYKNCE LDKNQRQCVE YALKARPLRR
     YIPKNQYQYK VWYVVNSTYF EYLMFVLILL NTICLAMQHY GQSCMFKEAM NILNMLFTGL
     FTVEMVLKLI AFKPKGYFSD PWNVFDFLIV IGSIIDVILS ETNHYFCDAW NTFDALIVVG
     SIVDIAITEV NTMKSKKNKT VRINVRENIN LPKEMEEKKT ALSSTVTITP LVLVFKSHIN
     FIVGKPVRHT GLLRDSNEES IGMDELLSVL DMAPDLIKEH QVEYLQQLDS SRHDQGSAQL
     SLASRETSIG SLELCYENAE ENSRISITFF RLFRVMRLVK LLSRGEGIRT LLWTFIKSFQ
     ALPYVALLIV MLFFIYAVIG MQVFGKIALX DTTEINRNNN FQTFPQAVLL LFRCATGEAW
     QEIMLACLPD KKCDPESEPA NSTEADHSCG SSFAVFYFIS FYMLCAFLII NLFVAVIMDN
     FDYLTRDWSI LGPHHLDEFK RIWAEYDPEA KGRIKHLDVV TLLRRIQPPL GFGKLCPHRV
     ACKRLVSMNM PLNSDGTVMF NATLFALVRT ALRIKTEGNL EQANEELRAI IKKIWKRTSM
     KLLDQVVPPA GDDEVTVGKF YATFLIQEYF RKFKKRKEQG LVGKPSQRNA LSLQAGLRTL
     HDIGPEIRRA ISGDLTAEEE LDKAMKEAVS AASEDDIFRR AGGLFGNHVS YYQSDGRSAF
     PQTFTTQRPL HINKSGNNQG DTESPSHEKL VDSTFTPSSY SSSGSNANIN NANNTALCRF
     PSPPSYPSTV STVEGHGTPL SPTIRVQEAP WKLPSKSSSS RDSQLAIVCQ EEVSQDETYD
     ENLNEDIEYC SEPSLLSTEM LAYQDDENRQ LTPPENNKGE DSRHSPKKGF LCSSALGRRA
     SFHLECLKRQ KNQGVDVSQK TVLPLHLVHH QALAVAGLSP LLQRSHSPTM FSRLCATPPA
     TPCNRGWPQQ TIPTLRLDGA ESSEKLNSSF PSVHCSSQYP DNTSCSSPRR ARPVSLTVPS
     QTGGSSRQFH GSAGSLVEAV LISEGLMQFA QDPKFIEVTT QELADACDMT IEEMENAADN
     ILNGNSKQSP NGNLLPFVNC RDPGQDSAGE EEEEVQNPDC RISQEELKDS RIYISSL
//
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