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Database: UniProt
Entry: A0A151MLA6_ALLMI
LinkDB: A0A151MLA6_ALLMI
Original site: A0A151MLA6_ALLMI 
ID   A0A151MLA6_ALLMI        Unreviewed;      2187 AA.
AC   A0A151MLA6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Voltage-dependent P/Q-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   ORFNames=Y1Q_0009019 {ECO:0000313|EMBL:KYO25233.1};
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:KYO25233.1};
RN   [1] {ECO:0000313|EMBL:KYO25233.1, ECO:0000313|Proteomes:UP000050525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO25233.1};
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. The isoform alpha-1A gives rise to P and/or Q-
CC       type calcium currents. {ECO:0000256|RuleBase:RU003808}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU003808}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC       1.A.1.11) family. CACNA1A subfamily. {ECO:0000256|ARBA:ARBA00037936}.
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:KYO25233.1}.
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DR   EMBL; AKHW03005909; KYO25233.1; -; Genomic_DNA.
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; IPR005448; CACNA1A.
DR   InterPro; IPR031649; GPHH_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
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:SF3; VOLTAGE-DEPENDENT P_Q-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1A; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF16905; GPHH; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01632; PQVDCCALPHA1.
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}; Coiled coil {ECO:0000256|SAM:Coils};
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        56..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        176..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        289..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        438..457
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        469..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        501..521
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        564..586
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        640..664
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1172..1190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1252..1270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1316..1338
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1428..1453
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1509..1527
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1539..1562
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1568..1586
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1631..1653
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1721..1745
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1882..1916
FT                   /note="Voltage-dependent calcium channel alpha-1 subunit
FT                   IQ"
FT                   /evidence="ECO:0000259|SMART:SM01062"
FT   REGION          763..1144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1910..2187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          660..687
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        778..792
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        809..823
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..895
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        902..970
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1003..1028
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1039..1057
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1068..1089
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1120..1142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1960..1977
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2055..2097
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2131..2148
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2149..2170
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         270
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         618
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         1399
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ   SEQUENCE   2187 AA;  250114 MW;  80F15C8EFA09E6DB CRC64;
     MYKQSMAQRA RTMALYNPIP VRQNCLTVNR SLFLFSEDNV VRKYAKKITE WPPFEYMILA
     TIIANCIVLA LEQHLPDEDK TPMSERLDDT EPYFIGIFCF EAGIKIIALG FAFHKGSYLR
     NGWNVMDFVV VLTGILAKVG SEFDLRTLRA VRVLRPLKLV SGIPSLQVVL KSIMKAMIPL
     LQIGLLLFFA ILIFAIIGLE FYMGKFHTTC FDSVTGEIKD RVPCGMDEPA RTCPNGTRCS
     KYWEGPNYGI TQFDNILFAV LTVFQCITME GWTDLLYNSN DASGNTWNWL YFIPLIIIGS
     FFMLNLVLGV LSGEFAKERE RVENRRAFLK LRRQQQIERE LNGYMEWISK AEVILAEDET
     EGEQRHPFDA LQRAAIKKSK TDLLNPEEAD DQLADIASVG SPFARASIKS AKLENSTFFH
     KRERRMRFYI RRMVKTQAFY WTVLSLVALN TLCVAVVHYS QPDWLSDFLY YAEFIFLGLF
     MSEMFIKMYG LGTRPYFHSS FNCFDCAVII GSIFEVVWAV MKPGTSFGIS VLRALRLLRI
     FKVTKYWASL RNLVVSLLNS MKSIISLLFL LFLFIVVFAL LGMQLFGGQF NFDTGTPATN
     FDTFPAAIMT VFQILTGEDW NMVMYDGIKS QGGVKRGMVF SVYFIVLTLF GNYTLLNVFL
     AIAVDNLANA QELTKDEQEE EEAATQKLAL QKAKEVAEVS PLSAASMSIA VKEQQKNQKS
     SKSVWEQRTS EMRKHNLLAS REALYNELDP EERWKVSYAR PSRPDIKTHL DRPLVVDPQE
     NRNNNTNKTR PSDPPLEPRF GPPQAEDFLR KPPRYHDRPR DPGSGRTYPP PESGVPELRR
     PHSGSREMEP PVEERSYHEA DPERLKAAEP PRRHPHHQAG GKESRGGSPR DGDREHRRHR
     GHRRAGEDGG GTDEGPKSER RPRHRPGEGE MPDGERRRRH RHAAQSTYDG DGKREDKERR
     HRRRKENQGP VPVHGPHLST TRPIQQDMGR PEPPVAEDID NMKNNKLATT ETSNPHPQSP
     TKLGNHANCT PSRAPDALGQ LPPNSQNVAN RWAPDNPSQP SNPRPPKTPE NSLIVTNPGP
     QNNPTKTAKK PEYTAVEIPT TFPPPIHNTV VQVNKNANPE PLPKKDEEKK EEEADDQEEN
     RPKPMVPYSS MFILSTTNPF RRLCHYIVNL RYFEMCILMV IAMSSIALAA EDPVQPNAPR
     NNSEQSVRCR GSAGLHATPX XXXFTGVFTF EMVIKMVDLG LVLHQGAYFR DLWNILDFIV
     VSGALVAFAF TGSKGKDINT IKSLRVLRVL RPLKTIKRLP KLKAVFDCVV NSLKNVLNIL
     IVYMLFMFIF AVVAVQLFKG KFFYCTDESK EFENDCRGEY LVYEKDEVKA EKREWKKYEF
     HYDNVLWALL TLFTVSTGEG WPQVLKHSVD ATYENQGPSP GYRMEMSIFY VVYFVVFPFF
     FVNIFVALII ITFQEQGDKM MEEYSLEKNE RACIDFAISA KPLTRHMPQN KQSFQYRMWQ
     FVVSPPFEYT IMAMIALNTV VLMMKFYGAS DAYENVLKMF NNVFTSLFSL ECLLKIMAFG
     VLNYFRDAWN IFDFVTVLGS ITDILVTEFG NNFINLSFLR LFRAARLIKL LRQGYTIRIL
     LWTFVQSFKA LPYVCLLIAM LFFIYAIIGM QVFGNIGIDD KDDESAITEH NNFRTFFQAL
     MLLFRSATGE GWQEIMLSCL SGKPCDENSG IMEHECGNEF AYFYFVSFIF LCSFLMLNLF
     VAVIMDNFEY LTRDSSILGP HHLDEYVRVW AEYDPAAWGR LTFTDMYEML RHMSPPLGLG
     KKCPPRVAYK RLLRMDLPVA DDNTVHFNST LMALIRTALD IKIAKGGADK QQMDAELRKE
     MMAIWPNLSQ KTLDLLVTPH KSTDLTVGKI YAAMMIMEYY RQSKAKKLQA MREEQNRTPL
     MFQRMEPPSP GQEGGPGQDA LPPPPLDQGG GLGHEGGMKE SQSWVTQRAQ EMFQKTGTWS
     PERARPDDLP NSRPSSQSVE MREIGKDGYS DSDHYPPMQG HGRAASMPRL PAENQTIPDV
     SPMKRSASVL GHPRARGIRL DDYSLERVPP DDAQRHHLRR RDRDRDRAHR ASDRSLGRYA
     DADAGLGTDL SMTPPSGELP LKERDGERGR PKDRRHHHHH HHHHHRHEDG RPRDRDRDRR
     WSRSPSEARD HPPPRQVGAP YPTPLIL
//
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