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Database: UniProt
Entry: A0A151PH96_ALLMI
LinkDB: A0A151PH96_ALLMI
Original site: A0A151PH96_ALLMI 
ID   A0A151PH96_ALLMI        Unreviewed;      1194 AA.
AC   A0A151PH96;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   20-DEC-2017, entry version 10.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   ORFNames=Y1Q_0006642 {ECO:0000313|EMBL:KYO48399.1};
OS   Alligator mississippiensis (American alligator).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO48399.1};
RN   [1] {ECO:0000313|EMBL:KYO48399.1, ECO:0000313|Proteomes:UP000050525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO48399.1};
RX   PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA   St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y.,
RA   Gongora J., Dalzell P., Moran C., Bed'hom B., Abzhanov A.,
RA   Burgess S.C., Cooksey A.M., Castoe T.A., Crawford N.G., Densmore L.D.,
RA   Drew J.C., Edwards S.V., Faircloth B.C., Fujita M.K., Greenwold M.J.,
RA   Hoffmann F.G., Howard J.M., Iguchi T., Janes D.E., Khan S.Y.,
RA   Kohno S., de Koning A.J., Lance S.L., McCarthy F.M., McCormack J.E.,
RA   Merchant M.E., Peterson D.G., Pollock D.D., Pourmand N., Raney B.J.,
RA   Roessler K.A., Sanford J.R., Sawyer R.H., Schmidt C.J., Triplett E.W.,
RA   Tuberville T.D., Venegas-Anaya M., Howard J.T., Jarvis E.D.,
RA   Guillette L.J.Jr., Glenn T.C., Green R.E., Ray D.A.;
RT   "Sequencing three crocodilian genomes to illuminate the evolution of
RT   archosaurs and amniotes.";
RL   Genome Biol. 13:415-415(2012).
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:KYO48399.1}.
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DR   EMBL; AKHW03000199; KYO48399.1; -; Genomic_DNA.
DR   Proteomes; UP000050525; Unassembled WGS sequence.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IEA:InterPro.
DR   GO; GO:0050856; P:regulation of T cell receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0043029; P:T cell homeostasis; IEA:InterPro.
DR   GO; GO:0007601; P:visual perception; IEA:InterPro.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR030157; VDCC_L_a1F.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF184; PTHR10037:SF184; 1.
DR   Pfam; PF00520; Ion_trans; 3.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000050525};
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:UP000050525};
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    103    120       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    140    159       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    171    187       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    244    267       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    323    344       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    356    378       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    523    541       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    561    578       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    653    672       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    722    744       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    861    879       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    899    919       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    977   1006       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1061   1082       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1102   1129       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       99    389       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      524    757       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      859   1135       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   COILED     1130   1150       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1194 AA;  133160 MW;  FC5EE1023496092A CRC64;
     MEPHDHGPGK GPGAVAVAFA EAAGQALAWP LANGAATPPG GLGGPPHPGG STAAGRRRLL
     HGKHKAQGPS AEHRSPRALF CLGLANPLRR GAISLVEWKP FDILILMTIF ANCVALGVYI
     PFPEDDSNAA NHNLEQVEYV FLIIFTVETF LKIIAYGLVM HPSAYIRNGW NLLDFVIVVV
     GLFSVALEQV SHKSGDAHHM SGKPGGFDVK ALRAFRVLRP LRLVSGVPSL HIVLNSIMKA
     MVPLLHIALL VLFVIIIYAI IGLELFIGRM HKTCFFIGSD LESEEDPSPC AFSGHGRACV
     QNNTECRGRW AGPNGGITNF DNFFFAMLTV FQCVTMEGWT DVLYWMQDAM GHELPWIYFV
     SLVIFGSFFV LNLVLGVLSG EFSKEREKAK ARGDFQKLRE KQQLEEDLRG YLEWITQAEG
     LDDDEDGADG EDKHVRVTVE DLTEKRRSRL KWLRHSSHST DTHTSLPASE TTSVNTENVG
     EEEHHVTCCE VILRKLSKTK FCRRLRRANR ALRKHCRLAA KSVAFYWVVL LLVFLNTLTI
     ASEHYGQPDW LTHTQAYANK VLLSLFTLEM LLKLYGLGPH AYGASFFNRF DCFVVCGGIL
     ETALVELGIM EPLGISVLRC VRLLRIFKVT RHWASLSNLV ASLLNSMKSI ASLLLLLFLF
     IIIFSLLGMQ LFGGRFAFEG APAKRSTFDT FPQALLTVFQ ILTGEDWNAV MYDGIMAYGG
     PVFPGMLVCI YFVILFICGN YILLNVFLAI AVDNLADADN ISAAKERQKA SEAIAGNTTH
     EDGVKVKCED EEEQEEDDSE GEGEEAEGAS LAGSESGSHG DQAEDPAAEK VLPIPQGSAF
     FLLSSTNPLR VHCHALIHHH IFTNLILVFI ILSSVSLAAE DPVRAHSFRN HILGYFDYAF
     TTIFTVEILL KMTAYGAFLH KGSFCRNWFN LLDLLVVSVS LISFGIHSSA ISVVKILRVL
     RVLRPLRAIN RAKGLKHVVQ CVFVAIRTIG NIMIVTTLLQ FMFACIGVQL FKGKFYSCTD
     EAKHTPEECK GTFIVYKDGD VLHPMVRDRV WHNSDFNFDN VLAGMMALFT VSTFEGWPAL
     LYKAIDAHAE NQGPIYNYRV EISIFFIVYI IIIAFFMMNI FVGFVIITFR AQGEQEYRNC
     ELDKNQYEGE QETYHCEPDK NQVPPPHQGH PQSREPHPQI QGKQETCYCE FDNS
//
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