ID H3DB19_TETNG Unreviewed; 1904 AA.
AC H3DB19;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Calcium channel, voltage-dependent, L type, alpha 1D subunit, a {ECO:0000313|Ensembl:ENSTNIP00000017711.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000017711.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000017711.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 STRING; 99883.ENSTNIP00000017711; -.
DR Ensembl; ENSTNIT00000017934.1; ENSTNIP00000017711.1; ENSTNIG00000014681.1.
DR GeneTree; ENSGT00940000154839; -.
DR HOGENOM; CLU_000540_0_1_1; -.
DR InParanoid; H3DB19; -.
DR OMA; EPRARYE; -.
DR TreeFam; TF312805; -.
DR Proteomes; UP000007303; 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; 3.
DR InterPro; IPR031688; CAC1F_C.
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:SF11; VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1D; 1.
DR Pfam; PF08763; Ca_chan_IQ; 1.
DR Pfam; PF16885; CAC1F_C; 2.
DR Pfam; PF16905; GPHH; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
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:UP000007303};
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 79..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 191..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 395..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 487..506
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 559..586
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 678..696
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 708..727
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 794..824
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 878..899
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 919..946
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 989..1011
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1023..1045
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1124..1142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1216..1239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1373..1407
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 294..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1576..1671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1710..1738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..628
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1576..1604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1624..1657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1714..1738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 539
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 892
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 1904 AA; 216755 MW; 26883CB4EC2D1160 CRC64;
DFSFSCDRLF SVVLEFLTKE EKGNGESSQP SMHGHGGKPG GFDVKALRAF RVLRPLRLVS
GVPSLQVVLN SIIKAMVPLL HIALLVLFVI IIYAIIGLEL FIGKMHATCY IPGSDSIAEE
EPAPCAISGH GRQCPINGTE CREGWQGPNG GITNFDNFLF AMLTVFQCIT MEGWTDVLYW
MNDAMGFELP WVYFVSLVIF GSFFVLNLVL GVLSGEFSKE REKAKARGDF QKLREKQQLE
EDLKGYLDWI TQAEDIDPDN EDEADEEAKR NRVTLADLTE KKKGRFGWFS QSSDTHAASV
PASETESVNT ENQNGEDEKT TCCGPLCQKI SKSKFSRRWR RWNRFCRRKC RLAVKSVPFY
WLVIILVFLN TLTISSEHYN QPLWLTEVQD VANKVLLALF TCEMLMKMYS LGLEAYFVSL
FNRFDCFVVC GGITETILVE LEIMSPLGIS VFRCVRLLRI FKVTRHWQSL SNLVASLLNS
MKSIASLLLL LFLFIIIFSL LGMQVFGGKF NFDETQTKRS TFDNFPQALL TVFQILTGED
WNAVMYDGIM AYGGPSSSGM IVCFYFIILF ICGNYILLNV FLAIAVDNLA DAESLNKDED
KKGDKKEEDK DDKEDDEDND DTAGEEEDPE VPSGPRPVIS DLVKKEKITP IPEGSAFFIF
SSTNPVRVFC HRLINHHIFT NLILVFIMLS SVSLAAEDPI RNFSARNIIL GYFDYAFTAI
FTVEIVLKMT TYGAFLHKGA FCRNYFNLLD LLVVGVSLVS FGIQSSAISV VKILRVLRVL
RPLRAINRAK GLKHVVQCVF VAIRTIGNIM IVTTLLQFMF ACIGVQLFKG KFYRCTDEAK
SSPEECKGTY ILYKDGDVNQ PTIHKRVWHN SDFNFDNVLM AMMALFTVST FEGWPALLYK
AIDSNRENLG PIYNYRVEIS IFFIIYIIII AFFMMNIFVG FVIVTFQEQG EKEYKNCELD
KNQRQCVEYA LKARPLRRYI PKNPYQYKFW YVVNSTGFEY IMFVLIMLNT LCLAVQHYGQ
SALFNYVMDI LNMVFTAVFT VEMVLKLIAF KPRHYVCDAW NTFDALIVVG SVVDIAITEV
NNTEDSARII TFFRLFRVMR LVKLLSRGGI RTLLWTFIKS FTRALPYVAL LIAMLFFIYA
VIGMQVFGKV AMVDGTHINR NNNFQTFPQA VLLLFRCATG EAWQEIMLAC MPGKLCDPES
DYNPGEEMTC GSGFAIVYFI TFYMLCAFLI INLFVAVIMD NFDYLTRDWS ILGPHHLDEF
KRIWSEYDPE AKGRIKHLDV VTLLRRIQPP LGFGKLCPHR VACKRLVAMN MPLNSDGTVM
FNATLFALVR TALKIKTEGN LEQANEELRA VIKKIWKRTS MKLLDQVVPP AGDDEVTVGK
FYATFLIQDY FRKFKKRKEE GLVGAHPSQN STAMALQAGL RTLHDIGPEI RRAISCDLQD
DELVDFIPEE DEEIYRRNGG LFANHLMNGG HRRSNGHQTN ATQRPLQVQP PPHYAHMEQP
VGRLSRANAM YSYGKSPKST NINLNNANVS TLPNGGHHRY YEHAPPNGYP GLRNAYYNKP
RTPQTQRRRY YETYVRSHGA DGHHPTIRRE EEFDEDRLSG EYYSGEEFYE DDSMLSGDRY
QTSDTEYETP KGYHHPDAYY DDDEQPLYHD SRRSPKRRLL PATPQGNRRP SFNFECLRRQ
SSQDELPHPR TALPLHLMQH QVMAVAGLDS SRAHRLSPTR STRSWATPPA TPASKDQSPY
YTPLIRVEQP HRESGVSVRK CSWYTDDPDF PHRTYSPVHL QVPPEYHSQF HQKRGSATSL
VEAVLISEGL GRYAKDPNFV AATKHEIADA CEMTIDEMES AASHLLNGGM TPGVNGVSVF
PILTPRDFDL QETAASYSDE EPEAEPRAPY EEDLADEMIC ITTL
//
