ID A0A151N8W8_ALLMI Unreviewed; 1843 AA.
AC A0A151N8W8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1E {ECO:0000313|EMBL:KYO33211.1};
GN ORFNames=Y1Q_0014985 {ECO:0000313|EMBL:KYO33211.1};
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:KYO33211.1};
RN [1] {ECO:0000313|EMBL:KYO33211.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO33211.1};
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., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA 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 entry
CC of calcium ions into excitable cells and are also involved in a variety
CC of calcium-dependent processes, including muscle contraction, hormone
CC or neurotransmitter release, gene expression, cell motility, cell
CC division and cell death. {ECO:0000256|RuleBase:RU003808}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003808}; Multi-
CC pass membrane protein {ECO:0000256|RuleBase:RU003808}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. {ECO:0000256|RuleBase:RU003808}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO33211.1}.
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DR EMBL; AKHW03003787; KYO33211.1; -; Genomic_DNA.
DR RefSeq; XP_019348147.1; XM_019492602.1.
DR STRING; 8496.A0A151N8W8; -.
DR GeneID; 102563699; -.
DR CTD; 779; -.
DR eggNOG; KOG2301; Eukaryota.
DR OrthoDB; 1110761at2759; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR Gene3D; 1.10.287.70; -; 4.
DR Gene3D; 6.10.250.2180; -; 1.
DR Gene3D; 6.10.250.2500; -; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 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; IPR005450; VDCC_L_a1ssu.
DR InterPro; IPR005446; VDCC_L_a1su.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR45628; VOLTAGE-DEPENDENT CALCIUM CHANNEL TYPE A SUBUNIT ALPHA-1; 1.
DR PANTHER; PTHR45628:SF9; VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1S; 1.
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; PR01634; LVDCCALPHA1S.
DR SMART; SM01062; Ca_chan_IQ; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PIRSR:PIRSR602077-1};
KW Calcium channel {ECO:0000256|ARBA:ARBA00022673,
KW ECO:0000256|RuleBase:RU003808};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568,
KW ECO:0000256|RuleBase:RU003808};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|PIRSR:PIRSR602077-3};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602077-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW ECO:0000256|RuleBase:RU003808}.
FT TRANSMEM 58..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 434..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 471..488
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 560..582
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 636..662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 801..820
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 832..854
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 874..897
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 918..951
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1042..1069
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1120..1141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1153..1173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1248..1266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1340..1363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1497..1530
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1707..1729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1806..1843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1809..1843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 615
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1015
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 1843 AA; 209448 MW; 67937AFE3A7F730E CRC64;
MEPASVQEDQ KKKQQKEKSK KPVPPAVPRP ARALFCLTLQ NPLRKACISI VEWKPFEIII
LLTIFANCVA LAVYLPMAED DTNATNSRLE KIEYVFLFIF TIEAMLKIIA YGFLFHADAY
LRNGWNVLDF AIISLGLFTM MLEQISVMQG APPSGKGGFD VKALRAFRVL RPLRLVSGVP
SLQVVLNSII KAMVPLLHIA LLVLFMIIIY AIVGQELFKG KMHKTCYYTG TDIIATVGSE
KPAPCTSTGH GRHCTLNGTD CRGGWPGPNN GITHFDNFGF AMLTVYQCIT MEGWTEVLYW
VNDAIGNEWP WIYFVSLILL GSFFILNLVL GVLSGEFTKE REKAKSRGTF QKLREKQQLE
EDLKGYIDWI THAEVVDSVR TRGEGMLPLD EGGSETESLY EIEGMNKWIL FFRHWRRWNR
LFRRKCREVV KSKFFYWLVI LLITLNTLSI ASEHHMQPDW LTHVQDNANW VLLSLFAAEM
LLKMYALGLR QYFMSLFNRF DCFVVCAGIV ETILVEFSIM SPLGISVLRC IRLLRIFKIT
KYWTSLSNLV ASLLNSIRSI ASLLLLLFLF IVIFSLLGMQ LFGGKYDFED MEVRRSTFDN
FPQALISVFQ VLTGEDWNSI MYNGIMAYGG PSFPGMLVCI YFIILFVCGN YILLNVFLAI
AVDNLAEAES LTSAQKAKAE ERKRRKMSRG YPGKSEEEKQ LLAKKLEQKA KGEGIPTTAK
LKVDEFESNV NEIKDPYPSA DFPGDDEEDE PEIPLSPRPR PLAELQLKEK AVPMPEASAF
FIFSPTNKIR ILCHRIVNAT WFTNFILLFI LLSSISLAAE DPIRAESFRN QILGYFDIGF
TSVFTVEIVL KMTAYGAFLH KGSFCRNSFN ILDLLVVAVS LISMGIQSST ISVVKILRVL
RVLRPLRAIN RAKGLKHVVQ CVFVAIKTIG NIVIVTTLLQ FMFACIGVQL FKGKFNSCTD
PSKITEKECR GSFITYVDGD PTQIQLEQRE WQHNDFHFDN VLSAMMSLFT VSTFEGWPQL
LYKAIDTHTE DMGPIYNYRV EMAIFFIIYI ILIAFFMMNI FVGFVIVTFQ EQGESEYKNC
ELDKNQRQCV QYALKARPLR RYIPKNPYQY QIWYVVTSSY FEYLMFFLIL LNTICLGMQH
YNQSDEMNHA SDILNVTFTI LFTVEMFVKL MAFKAKGYFG DPWNVFDFLI VIGSIIDVIL
SEIDDSEDNS RVSITFFRLF RVLRLVKLLS RGEGVRTLLW TFIKSFQALP YVALLIVMLF
FIYAVIGMQM FGKVAMVDGT QINRNNNFQT FPQAVLLLFR CATGEAWQEI LLAASYGKLC
DPESDYAPGE EYTCGTGFAY FYFISFYMLC AFLIINLFVA VIMDNFDYLT RDWSILGPHH
LDEFKRIWAE YDPEAKGRIK HLDVVTLLRR IQPPLGFGKF CPHRVACKRL VCMNMPLNSD
GTVTFNATLF ALVRTALKIK TEGNFEQANE ELRAIIKKIW KRTSMKLLDQ VIPPIGDDEV
TVGKFYATFL IQEHFRKFMK HQEEYYGYRP KKNPIEIQAG LRTIEEEAAP EIHRAISGDL
TAEEELERAM VEAAMEEGIY RRQGGLFGQV DNFIEHHSPL QPHVASQRPL QFTEQGSEDI
DSPVFLDDFT PERNTNASNA NNNNAASRVE YEDELQGKKM SCQTRELSAL APKCTSHQEK
LQQELSRRRA ASVRVCPVSR LHIVPPQVPR EEASTHEQGV EEGEVQGSAW QVDGDSDLTR
EEDPAASAPA TTLLIQEALI SGGLSTLAHD PSFVTVTSNE MAAAYQMEME EVEMAAAEVL
KGRKSLEGEK TTSPGQPLSS TSLHNSHGCS VVSSQEAISA THL
//
