ID A0A3Q4MAS3_NEOBR Unreviewed; 1987 AA.
AC A0A3Q4MAS3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000005804.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000005804.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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. {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 Ensembl; ENSNBRT00000005982.1; ENSNBRP00000005804.1; ENSNBRG00000003082.1.
DR GeneTree; ENSGT00940000154839; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000003082; Expressed in brain and 1 other cell type or tissue.
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; IPR031688; CAC1F_C.
DR InterPro; IPR031649; GPHH_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR014873; VDCC_a1su_IQ.
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: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 PRINTS; PR01630; LVDCCALPHA1.
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:UP000261580};
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 49..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 447..465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 485..508
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 577..596
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 649..676
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 766..784
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 796..815
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 882..912
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 966..987
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1007..1034
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1086..1106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1118..1138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1150..1175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1216..1234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1308..1331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1465..1499
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 378..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1689..1749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1797..1817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1703..1736
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 629
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 980
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 1987 AA; 226413 MW; 8E7DAB1A3C90B096 CRC64;
HKKRQQYAKS KKQGSNANSR PPRALFCLNL NNPIRRACIS LVEWKPFDIF ILIAIFANCM
ALAVYIPFPE DDSNSTNHDL ETVEYAFLII FTIETFLKII AYGLVMHQNA YVRNGWNMLD
FVIVVIGLFS VALELLTKEE KGEVEGDNHA SMHGHGGKPG GFDVKALRAF RVLRPLRLVS
GVPSLQVVLN SIIKAMVPLL HIALLVLFVI IIYAIIGLEL FIGKMHATCY FPSTDMIAEE
EPAPCAISGH GRQCPINGTE CREGWQGPNG GITNFDNFLF AMLTVFQCIT MEGWTDVLYW
MNDAMGFELP WVYFVSLVIF GSFFVLNLVL GVLSGEFSKE REKAKARGDF QKLREKQQLE
EDLKGYLDWI TQAEDIDPDN EDEADEESKR NPSVPASETE SVNTENQNGE DEKTPCCGPL
VLCHCSRRWR RWNRFCRRKC RLAVKSVPFY WLVIILVFLN TLTISSEHYN QPLWLTQVQD
VANKVLLALF TCEMLVKMYS LGLQAYFVSL FNRFDCFVVC GGITETILVE LEIMSPLGIS
VFRCVRLLRI FKVTRHWQSL SNLVASLLNS MKSIASLLLL LFLFIIIFSL LGMQVFGGKF
NFDETQTKRS TFDNFPQALL TVFQILTGED WNAVMYDGIM AYGGPSSSGM IVCFYFIILF
ICGNYILLNV FLAIAVDNLA DAESLNTDEG DKKGDKKDDD KDDKEDNDDT AAEEEDPEVP
SGPRPVISDL VKKEKITPIP EGSAFFIFSN TNPVRVFCHR LINHHIFTNL ILVFIMLSSV
SLAAEDPIRN FSARNIILGY FDYAFTAIFT VEIVLKMTTY GAFLHKGAFC RNYFNLLDLL
VVGVSLVSFG IQSSAISVVK ILRVLRVLRP LRAINRAKGL KHVVQCVFVA IRTIGNIMIV
TTLLQFMFAC IGVQLFKGKF YRCTDEAKSS PEECKGTYIL YKDGDVNQPT VHKRVWHNSD
FNFDNVLMAM MALFTVSTFE GWPALLYKAI DSNRENLGPI YNYRVEISIF FIIYIIIIAF
FMMNIFVGFV IVTFQEQGEK EYKNCELDKN QRQCVEYALK ARPLRRYIPK NPYQYKFWYV
VNSTGFEYIM FVLIMLNTLC LAVQHYGQSA LFNYVMDILN MVFTAVFTVE MVLKLIAFKP
RGYFGDAWNV FDALVVIGSI VDIVLINVST TSFLICNARI SITFFRLFRV MRLVKLLSRG
EGIRTLLWTF IKSFQALPYV ALLIAMLFFI YAVIGMQVFG KIAMVDGTHI NRNNNFQTFP
QAVLLLFRCA TGEAWQEIML ACMPGKLCDP ESDYNPGEEM TCGSGFAIVY FITFYMLCAF
LIINLFVAVI MDNFDYLTRD WSILGPHHLD EFKRIWSEYD PEAKGRIKHL DVVTLLRRIQ
PPLGFGKLCP HRVACKRLVA MNMPLNSDGT VMFNATLFAL VRTALKIKTE GNLEQANEEL
RAVIKKIWKR TSMKLLDQVV PPAGDDEVTV GKFYATFLIQ DYFRKFKKRK EEGLVGAHPS
QNNTAIALQA GLRTLHDIGP EIRRAISCDL QDDELIDFIP EEDEEIYRRN GGLFGNHLMN
GGHRRSNGHQ TNATQRPLQV QPPPHYAHME QPVGRLSRAN SPKSTNINLN NANVSSLPNG
GHHRYYEHAP PNGYPGLRSS YYDYDKRRYY ETYVRSHRGD GRHPTIRREE EFDEDHFSGE
YYSGEEFYED DSMLSGDRYQ NSDTEYETPK GYHHPDSYYD DDEQPLYRDS RRSPKRRLLP
ATPQGHRRPS FNFECLRRQS SHDELPHQRT ALPLHLMQHQ VMAVAGLDSS RAHRLSPTRS
TRSWATPPAT PASKDQSPYY TPLIRVEHPH RESVVGSQVS VRKSSWYTDD PEFSQRTYSP
VHLQVPPEYH NQYHQKRGSA TSLVEAVLIS EGLGRYAKDP KFVAATKHEI ADACEMTIDE
MESAASHLLN GGMSPGINGV NVFPLLTPRD YELPDTAASY SDEEPETEPR GPYEEDLADE
MICITTL
//
