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Database: UniProt
Entry: A0A091PTL8_HALAL
LinkDB: A0A091PTL8_HALAL
Original site: A0A091PTL8_HALAL 
ID   A0A091PTL8_HALAL        Unreviewed;      1551 AA.
AC   A0A091PTL8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
DE   Flags: Fragment;
GN   ORFNames=N329_13231 {ECO:0000313|EMBL:KFQ11000.1};
OS   Haliaeetus albicilla (White-tailed sea-eagle) (Falco albicilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC   Accipitrinae; Haliaeetus.
OX   NCBI_TaxID=8969 {ECO:0000313|EMBL:KFQ11000.1, ECO:0000313|Proteomes:UP000054379};
RN   [1] {ECO:0000313|EMBL:KFQ11000.1, ECO:0000313|Proteomes:UP000054379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N329 {ECO:0000313|EMBL:KFQ11000.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-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. {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}.
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DR   EMBL; KK665431; KFQ11000.1; -; Genomic_DNA.
DR   Proteomes; UP000054379; 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; 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; 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   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:UP000054379};
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        5..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        258..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        402..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        439..456
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        528..550
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        604..630
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        764..783
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        795..817
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        837..860
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        881..914
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1005..1032
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1073..1092
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1118..1138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1213..1231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1305..1328
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1462..1495
FT                   /note="Voltage-dependent calcium channel alpha-1 subunit
FT                   IQ"
FT                   /evidence="ECO:0000259|SMART:SM01062"
FT   REGION          695..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         239
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         583
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         978
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   CARBOHYD        204
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ11000.1"
FT   NON_TER         1551
FT                   /evidence="ECO:0000313|EMBL:KFQ11000.1"
SQ   SEQUENCE   1551 AA;  177582 MW;  5A2F6D302BC4BF15 CRC64;
     RPFEIIILLT IFANCVALAV YLPMPEDDTN VANSSLEKIE YAFLIFFAIE AMLKIIAYGF
     LFHTDAYLRN GWNVLDFSIV SLGLITMTLE QVNAKQGGTS GGKGGFDVKA LRAFRVLRPL
     RLVSGVPSLQ VVLNSIIKAM VPLLHIALLV LFMIIIYAIV GQELFKGKMH KTCYYLGTDV
     IATVASEKPA PCTSSGHGRH CTINGTECRS GWPGPNNGIT HFDNFGFAML TVYQCITMEG
     WTEVLYWVND AIGNEWPWIY FVSLILLGSF FVLNLVLGVL SGEFTKEREK AKSRGTFQKL
     REKQQLEEDL KGYMDWITHA EVMDSDRARG EGSSSAWSKT LSMRVGFLTL TILERQGRDS
     LPHVLPKGSS ESLGCRSLLS RRWRRWNRMF RRKCRDVVKS KFFYWLVILL VALNTLSIAS
     EHHFQPEWLT QVQDNANRVL LALFVAEMLL KMYALGLRQY FMSLFNRFDC FVVCAGILET
     ILVELGTLSP LGISVLRCIR LLRIFKITRY WTSLSNLVAS LLNSVRSIAS LLLLLFLFII
     VFALLGMQLF GGKFDFEDME VRRSTFDNFP QALISVFQIL TGEDWNSIMY DGIMAYGGPS
     FPGMLVCIYF IILFVCGNYI LLNVFLAIAV DNLAEAESLT LAQKAKAEER KRRKMSRVWP
     TCSIWQQYWH TQLHVLSVSP LFQLKVDEFE SNVNEIKDPY PSADFPGDDE EDEPEIPLSP
     RPRPLAELQL KEKAVPMPEA SSFFIFSPTN KFRMLCHRIV NATWFTNFIL LFILLSSISL
     AAEDPIRAES FRNQILGYFD IGFTSVFTVE IVLKMTAYGA FLHKGSFCRN SFNILDLLVV
     AVSLISMGIE SSAISVVKIL RVLRALRALR AINRAKGLKH VVQCVFVAIK TIGNIVVVTT
     LLQFMFACIG VQLFKGKFYR CTDPSKMTEK ECRGYFINYV DGDPTQIELQ ERVWLHSNFH
     FDNVFSAMMS LFTVSTFEGW PELLYMAIDT NAEDTGPVYN YRVEIAMFFI IYIILIAFFM
     MNIFVGFVIV TFQEQGESEY KNCELDKNQR QCVQYALKAR PLRRYIPKNP YQYQIWYVVT
     SSYFEYLIVW TYRGLTWLLL PSPQHYNQSA EMNHISDILN VAFTILFTLE MILKLMAFKA
     KGYFGDPWNV FDFLIVIGSI IDVILSEIDD SDDNSRVSIT FFRLFRVMRL VKLLSRGEGV
     RTLLWTFIKS FQALPYVALL IVMLFFIYAV IGMQMFGKIA MVDGTQINRN NNFQTFPQAV
     LLLFRCATGE AWQEILLDCS YGKLCDPESD FAEGEEYTCG TGFAYFYFIS FYMLCAFLII
     NLFVAVIMDN FDYLTRDWSI LGPHHLDEFK RIWAEYDPEA KGRIKHLDVV TLLRRIQPPL
     GFGKFCPHRV ACKRLVCMNM PLNSDGTVTF NATLFALVRT ALKIKTEGNF EQANEELRAI
     IKKIWKRTSM KLLDQVIPPI GDDEVTVGKF YATFLIQEHF RKFMKRQEEY YGYRPKKNPV
     EIQAGLRSIE EEAAPEIHRA ISGDLTAEEE LERAMVEAAM EEGIYRVSAA L
//
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