ID A0A0A0B1C4_CHAVO Unreviewed; 2045 AA.
AC A0A0A0B1C4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Voltage-dependent R-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
DE Flags: Fragment;
GN ORFNames=N301_09696 {ECO:0000313|EMBL:KGL99568.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL99568.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL99568.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL99568.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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-1E gives rise to R-type
CC calcium currents. {ECO:0000256|RuleBase:RU003808}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, 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}.
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DR EMBL; KL873593; KGL99568.1; -; Genomic_DNA.
DR STRING; 50402.A0A0A0B1C4; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; IPR002048; EF_hand_dom.
DR InterPro; IPR031649; GPHH_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014873; VDCC_a1su_IQ.
DR InterPro; IPR005449; VDCC_R_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:SF5; VOLTAGE-DEPENDENT R-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1E; 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; PR01633; RVDCCALPHA1.
DR SMART; SM01062; Ca_chan_IQ; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
DR PROSITE; PS50222; EF_HAND_2; 1.
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|ARBA:ARBA00023180};
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858};
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 55..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 468..486
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 568..590
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 646..668
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1073..1091
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1143..1160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1204..1226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1316..1341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1397..1415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1427..1450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1456..1474
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1521..1539
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1614..1638
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1654..1689
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 682..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1925..2045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..827
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1044
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1937..1951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1952..2009
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2010..2039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 274
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 622
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1287
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL99568.1"
FT NON_TER 2045
FT /evidence="ECO:0000313|EMBL:KGL99568.1"
SQ SEQUENCE 2045 AA; 232263 MW; 91B98C01541456E5 CRC64;
ALYNPIPVRQ NCFTVNRSLF LFGEENIVRK YAKKLIDWPY PFCTPCEPPS LLPGFALYMI
LATIIANCIV LALEQHLPED DKTPMSRRLE KTEPYFIGIF CFEAGIKIVA LGFVFHKGSY
LRNGWNVMDF IVVLSGILAT AGTHFNTHVD LRTLRAVRVL RPLKLVSGIP SLQIVLKSIM
KAMVPLLQIG LLLFFAILMF AIIGLEFYSG KLHRACYTNN SGELEELDPP HPCGVQGCPP
GYECREWIGP NDGITQFDNI LFAVLTVFQC ITMEGWTTVL YNTNDALGAT WNWLYFIPLI
IIGSFFVLNL VLGVLSGEFA KERERVENRR AFMKLRRQQQ IERELNGYRA WIDKAEEVML
AEENKNSGTS ALEVLRRATI KRNRTDAMNR DSSDEHCVDI SSVGNPLSHS GLKGARVDGA
SYLRHKERLL RISVRHMVKS QVFYWIVLSL VALNTACVAI VHHNQPAWLT HFLYYAEFLF
LGLFLLEMSL KMYGMGPRLY FHSSFNCFDC GVTVGSIFEV VWAIFRPGTS FGISVLRALR
LLRIFKITKY WASLRNLVVS LMSSMKSIIS LLFLLFLFIV VFALLGMQLF GGRFNFIDGT
PSANFDTFPA AIMTVFQILT GEDWNEVMYN GIRSQGGVRS GMWSSIYFIV LTLFGNYTLL
NVFLAIAVDN LANAQELTKD EQEEEEAFNQ KHALQKAKEV SPMSAPNMPA IERERRRRHH
MSVWEQRTSQ LRRHMQMSSQ EGINKDEPHL INPHASIFRR KKPGDGVALE KCAEEQGGKG
DRPPAEGPEQ PAPGANPGGG EDRRSPSPRA KRDKETWHQK SCHRNCEPGE QEGAGGGIED
RARMRQSQRR SRHRRARMEG KEPASALGSR SASQELGLEE TSPTEGGQDG DRLGDVAAAE
ALIQGEPEAR EEPIRTNGVP AGDAELVGTT EEGSAPQTAP EPPRGKTGSL TEQDCSSPDT
SEQALLEASR TVSRSEPDLS SITPNTEKAT ESTTIMIDIH DSAVVQISNK TDGEASPLKE
AESKEDEEEM EKKKRKKEKS ETGKAMVPHS SMFIFSTTNP VRRACHYIVN LRYFEMCILL
VIAASSIALA AEDPVLTNSD RNKVLRYFDY VFTGVFTFEM VIKMIDQGLI LQDGSYFRDL
WNILDFIVVV GALVAFALAT NKGRDIKTIK SLRVLRVLRP LKTIKRLPKL KAVFDCVVTS
LKNVFNILIV YKLFMFIFAV IAVQLFKGKF FYCTDSSKDT EKDCIGNYVD HEKNKMEVKC
REWKRHEFHY DNIIWALLTL FTVSTGEGWP QVLQHSVDVT EEDRGPSRSN RMEMSIFYVV
YFVVFPFFFV NIFVALIIIT FQEQGDKMME ECSLEKNERA CIDFAISAKP LTRYMPQNRH
TFQYRVWHFV VSPSFEYTIM AMIALNTVVL MMKYYSAPYT YELALKYLNI AFTMVFSLEC
VLKIIAFGFL NYFRDTWNIF DFITVIGSIT EIILTDTKLV NTSSFNMSFL KLFRAARLIK
LLRQGYTIRI LLWTFVQSFK ALPYVCLLIA MLFFIYAIIG MQVFGNIKLD EESHINRHNN
FRSFLGSLML LFRSATGEAW QEIMLSCLEG KGCEPDTTAT SGQNENERCG TDLAYVYFVS
FIFFCSFLML NLFVAVIMDN FEYLTRDSSI LGPHHLDEFV RIWAEYDRAA CGRIHYTEMY
EMLTLMSPPL GLGKRCPSKV AYKRLVLMNM PVAEDMTVHF TSTLMALIRT ALDIKIAKGL
DVRGPLLFPT VQGGADWQQL DSELQKEILT IWPHLSQKML DLLVPMPKTS DLTVGKIYAA
MMIMDYYKQS KAKKQRQQLE EQKNAPMFQR MEPSSLPQEI ISNAKALPYL QQDTLSGLSS
RSGFPSLSPL SPQEIFQLAC MDPAHGQFQE HQSLVVTDTS SMRRSFSTIR DKRTNSSWLD
EFSMERSSDN TYKSRRRSYH SSLQLSARRL NADTGHRSDG HRSGGRERGR SKERKHLLSP
DISRCNSEER SPQAHDESPE RRRESRSPSE GRSQTPNRQG TGSLSESSIP SISDTSTPRR
GRRQL
//
