ID H3AUU1_LATCH Unreviewed; 1734 AA.
AC H3AUU1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Voltage-dependent R-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1E {ECO:0000313|Ensembl:ENSLACP00000013412.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000013412.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000013412.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AFYH01031304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01031305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01031306; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01031307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01031308; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01031309; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01031310; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01031311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01031312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01031313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7897.ENSLACP00000013412; -.
DR Ensembl; ENSLACT00000013508.1; ENSLACP00000013412.1; ENSLACG00000011809.1.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000155601; -.
DR HOGENOM; CLU_000540_1_0_1; -.
DR InParanoid; H3AUU1; -.
DR OMA; XRERRRR; -.
DR TreeFam; TF312805; -.
DR Proteomes; UP000008672; 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; 3.
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:UP000008672};
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..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 440..459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 518..540
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 971..991
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1048..1066
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1116..1138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1228..1253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1309..1327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1339..1362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1434..1459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1527..1551
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1567..1602
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 558..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 494
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1199
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ SEQUENCE 1734 AA; 198484 MW; 02A63394F9EDC164 CRC64;
VKHCFAKLTS FTNHFNTHVD LRTLRAVRVL RPLKLVSGIP SLQIVLKSIM KAMVPLLQIG
LLLFFAILMF AIIGLEFYSG KLHKTCYGNN SETGEMEAHE PQYPCGTQKC PDSYECREWI
GPNDGITQFD NILFAVLTVF QCITMEGWTT VLYNTNDALG ATWNWLYFIP LIIIGSFFVL
NLVLGVLSGE FAKERERVEN RRAFMKLRRQ QQIERELNGY RAWIDKAEEV MLAEENKNSG
TSALDVLRRA TIKKGRMESI RRDPSEEHCA DISSVGTSFA RASIKSTKLD GTSYFRRQEK
LLRISVRHMV KSQAFYWTVL SLVALNTMCV AIVHHKQPVG LSNFLYYAEF LFLGLFLSEM
FLKMYGLGPR LYFHSSFNCF DCGVVVGSIF EVIWSVFRPG MSFGISVLRA LRLLRIFKIT
KYWASLRNLV VSLMNSMKSI ISLLFLLFLF IVVFALLGMQ LFGGGFNFND GTPSANFDTF
PSAIMTVFQI LTGEDWNEVM YNGIRSQGGV SSGMWSSIYF IVLTLFGNYT LLNVFLAIAV
DNLANAQELT KDEQEAEEAF NQKHALQKAK EVSPMSAPNM HSTDRCTRSR THPCLQTKFT
SYTKEKKKRH AMSIWEQRTS QLRRHRQMSS QEALYKDEME DLTSEFHQKA KLEEDISTRS
EEEEAGREDP ESGAQQTQEG DPEKLPVNNH CQGIEEKRSP SPTSPVEKES RHINSCSLTQ
DLPGQEDPLA IDGSKDKRWE RRSRHRKMRG EGEAKASSHK KGSRLASRER RGTEEDGQEG
ENSKEKKHGQ EEGKETTRER RRESYDYRVS PALDSAAAHS DATATEMNSP GTHHDETDDN
VKNNKLVLLD SSAQDSSEQA QPINQPAKPK NSFSMEESSH PLIPTDSEKL SGHTNFIIEV
TDTHGPVDSI VIPAKQKPLV MAEPVGEFFV KLSSAKVGLS RKRLHARSSG NLINCITNKI
PRNANSTLES GLFFFVCLFV FKFPVMMPVS VPSIPGFTMA PRPTWYEEKF CIDYHTHTQT
HTTFFQHIVG WMIDQGLILH EGSYFRDLWN ILDFIVVVGA LIAFALTNVM GTNKGRDIKT
IKSLRVLRVL RPLKTIKRLP KLKAVFDCVV TSLKNVFNIL IVYKLFMFIF AVIAVQLFKG
KFYYCTDRSK DLQKDCVGRF VDHEKSKITV EEREWKRHDF HYDSIIWALL TLFTVSTGEG
WPQVLQHSVD VTEEDRGPSP GNRMEMSIFY VIYFVVFPFF FVNIFVALII ITFQEQGDKM
MEECSLEKNE RACIDFAISA KPLTRYMPQN RHTYQYRVWH FVVSPSFEYT ILTMIALNTV
VLMMKYYSAP TAYDLVLKYL NIAFTVLFSL ECILKIIAFG FLNYFRDTWN IFDFITVVGS
ITEIILSDSK LVSAKTFNMS FLKLFRAARL IKLLRQGYTI RILLWTFVQS FKALPYVCLL
IAMLFFIYAI IGMQVFGNIK LNEETQINRH NNFRTFFSSL MLLFRSATGE AWQEIMLSCL
SGKKCEIDTS ATNGTDENVE SCGTDLAYFY FVSFIFLCSF LMLNLFVAVI MDNFEYLTRD
SSILGPHHLD EFVRIWAEYD KAACGRIHYT DMYEMLTHMS PPLGLGKKCP SKVAYKRLVL
MNMPVDEDMT VHFTSTLMGL IRTALDIKIA KGGADRQQLD SELQKEILLI WPHISQRMLD
LLVPIHKASD LTIGKIYAAM MIMDYYKQSK AKKQRQQLEE QVLHSNSVPL FSRL
//
