GenomeNet

Database: UniProt
Entry: A0A151NIY1_ALLMI
LinkDB: A0A151NIY1_ALLMI
Original site: A0A151NIY1_ALLMI 
ID   A0A151NIY1_ALLMI        Unreviewed;      1937 AA.
AC   A0A151NIY1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   28-MAR-2018, entry version 14.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   ORFNames=Y1Q_0024310 {ECO:0000313|EMBL:KYO36619.1};
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:KYO36619.1};
RN   [1] {ECO:0000313|EMBL:KYO36619.1, ECO:0000313|Proteomes:UP000050525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO36619.1};
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
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}.
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:KYO36619.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AKHW03002956; KYO36619.1; -; Genomic_DNA.
DR   Proteomes; UP000050525; 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; 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   InterPro; IPR027359; Volt_channel_dom_sf.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16885; CAC1F_C; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
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   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|SAAS:SAAS00085096, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050525};
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      7     28       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     40     57       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    113    135       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    195    216       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    228    250       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    371    388       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    408    426       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    497    519       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    573    599       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    747    766       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    778    800       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    820    843       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    864    897       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    989   1015       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1066   1087       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1099   1119       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1205   1223       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1299   1322       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1456   1490       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      602    628       {ECO:0000256|SAM:Coils}.
FT   COILED     1417   1437       {ECO:0000256|SAM:Coils}.
FT   COILED     1908   1928       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1937 AA;  218960 MW;  DA17A1CC281C0D88 CRC64;
     MAKKERVEYL FLIIFTVEAF LKVIAYGLLF HPNAYLRNGW NLLDFIIVVV GLFSAILEQA
     TKADGGNSIG GKGAGFDVKA LRAFRVLRPL RLVSGVPSLQ VVLNSIIKAM VPLLHIALLV
     LFVIIIYAII GLELFMGKMH KTCYHVHGAL ADTPAEEDPS PCAPQSAHGR QCQNGTECRA
     GWEGPKHGIT NFDNFAFAML TVFQCITMEG WTDVLYWMQD AMGYELPWVY FVSLVIFGSF
     FVLNLVLGVL SGEFSKEREK AKARGDFQKL REKQQLEEDL KGYLDWITQA EDIDPENEDE
     GMDEEKPRNM SMPTSETESV NTDNVAGADI EGENCGARLA HRISKSKFSR YWRRWNRFCR
     RKCRAAVKSN VFYWLVIFLV FLNTLTIASE HYQQSNWLTE VQDTANKVLL ALFTAEMLLK
     MYSLGLQAYF VSLFNRFDCF IVCGGILETI LVETKIMPPL GISVLRCVRL LRIFKITRYW
     NSLSNLVASL LNSVRSIASL LLLLFLFIII FSLLGMQLFG GKFNFDEMQT RRSTFDNFPQ
     SLLTVFQILT GEDWNSVMYD GIMAYGGPSF PGMLVCIYFI ILFICGNYIL LNVFLAIAVD
     NLADAESLTS AQKEEEEEKE RKKLARTASP EKKQEIEKPA VEEETKEEKI ELKSITADGE
     SPPATKINVD DYQPNENEEK NPYPTTEAPG EEDEEEPEMP VGPRPRPMSE LHLKEKAVPM
     PDASAFFIFS PSNRFRVHCH RIVNDNIFTN LILFFILLSS ISLAAEDPVR HTSFRNQILF
     YFDIVFTVIF TIEIALKMTA YGAFLHKGSF CRNYFNILDL LVVSVSLISF GIQSSAINVV
     KILRVLRVLR PLRAINRAKG LKHVVQCVFV AIRTIGNIVI VTTLLQFMFA CIGVQLFKGK
     LYSCSDSSKQ TLTECRGYFI TYKDGEVTQP MIQPRSWENS KFDFDNVLTA MMALFTVSTF
     EGWPELLYRS IDSHMEDVGP IYNHRVEISI FFIIYIIIIA FFMMNIFVGF VIVTFQEQGE
     QEYKNCELDK NQRQCVEYAL KARPLRRYIP KNQYQYKVWY VVNSTYFEYL MFVLILLNTI
     CLAMQHYGQS CMFKEAMNIL NMLFTGLFTV EMVLKLIAFK PKHYFCDAWN TFDALIVVGS
     IVDIAITEVN PAEHTQCSSS MNAEENSRIS ITFFRLFRVM RLVKLLSRGE GIRTLLWTFI
     KSFQALPYVA LLIVMLFFIY AVIGMQVFGK IALNDTTGIN RNNNFQTFPQ AVLLLFRCAT
     GEAWQEIMLA CLSGKKCDPE SEPANSTEGD HSCGSSFAIF YFISFYMLCA FLIINLFVAV
     IMDNFDYLTR DWSILGPHHL DEFKRIWAEY DPEAKGRIKH LDVVTLLRRI QPPLGFGKLC
     PHRVACKRLV SMNMPLNSDG TVMFNATLFA LVRTALRIKT EGNLEQANEE LRAIIKKIWK
     RTSMKLLDQV VPPAGDDEVT VGKFYATFLI QEYFRKFKKR KEQGLVGKPS QRNALSLQAG
     LRTLHDIGPE IRRAISGDLT AEEELDKAMK EAVSAASEDD IFRRAGGLFG NHVSYYQSDG
     RSTFPQTFTT QRPLHINKSG NNQGDTESPS HEKLVDSTFT PSSYSSSGSN ANINNANNTA
     LCRFPSPPNF PSTVSTVEGH GTPLSPTIRV QEAPWKLGSK SSGSRDSQLA IVCQEEVSQG
     ETYDENLNED VEYCSEPSLI STEMLSYQDD ENRQLTPPEN NKGEDARQSP RKGFLCSSSL
     GRRASFHLEC LKRQKNQGVD VSQKTVLPLH LVHHQALAVA GLSPLLQRSH SPTMFSRLCA
     TPPATPCSRG WPEQTIPTLR LDGAESSEKL NSSFPSIHCS SWYSDRASCS STRRARPVSL
     TVPSQTGGSG RQFHGSAGSL VEAVLISEGL MQFAQDPKFI EVTTQELADA CDMTIEEMEN
     AADNILNEVP HCSRDLE
//
DBGET integrated database retrieval system