ID A0A3Q2WCL3_HAPBU Unreviewed; 1702 AA.
AC A0A3Q2WCL3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
OS Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000022941.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000022941.1}
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. {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; ENSHBUT00000012355.1; ENSHBUP00000022941.1; ENSHBUG00000003865.1.
DR GeneTree; ENSGT00940000158289; -.
DR OMA; NFADHRP; -.
DR Proteomes; UP000264840; Unplaced.
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; 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; PF16885; CAC1F_C; 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 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:UP000264840};
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..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 453..474
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 486..511
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 545..568
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 589..613
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 625..646
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 772..795
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 807..828
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 911..930
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 979..999
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1019..1046
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1087..1108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1128..1148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1335..1359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1490..1523
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 712..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1551..1571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1583..1630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 600
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 993
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 1702 AA; 193777 MW; 11B4C167B12A26BD CRC64;
MNEEELKRKQ REKLKKLQAT GGNPRPARSL FLLNLKNPFR KACINIVEWT FEIIILLTIF
ANCIALAVFL PMPEEDTNNT NLNLESLEYI FLVIFTLECF LKIVAYGFVF HEGAYLRNCW
NILDFVIVFM SLFTLFMDTV NMVSGVPKEK GGGFDMKALR AFRVLRPLRL VSGVPLQVVM
NSILKAMLPL LHIALLVFLL VTIYAIMGLE LFKCKMHKTC YYKGTIYATA EGELPAPCAQ
AGNGRRCIIN GTECRPDWEG PNNGITHFDN IGFAMLTVYQ CITMESWTKV LYWVNDAIGN
EWPWLYFVPL ILLGSFFVLN LVLGVLSEFT KEREKARSRG EFQKLRERQQ LDEDLHGYME
WITHAEVLDA DRELLPLTSG DSDTDSLYDL EGKSRIIYYR LARRWNRFFR MKCLVYVKTR
AFYWVVMFLV FLNTLTIATE YHHQPESLTS FQVASRVLLV LFVIEMFVKM YALGPRAYFM
SLFNRFDFFV VLCGILEMIM LSAGAVAPLG FSVLRCIRLL RILKVTYWKS LSNLVASLLN
SIRSIASLLL LLFLFIVIFS LLGMQVFGGK FNFSDHRARR SNFDNFPQAL ISVFQILTGE
DWTSIMYNGI MAYGGPVIPG ILVSIYFIIL FVCGNILLNV FLAIAVDNLA EAESLTSAQK
EKAEEKLRKK LLPEKTDEER EKITKQRAKI EGMPTTAKLK IDEFESNVNE VKDPFPPADF
PDDEEEEPEI PISPRPRPMA DLQLKEEAVP LPEASSFFIF GPQNFRKLCY KIINASSFTN
LILLFILLSS ISLAAEDPID PKSPRNQFQI LAYADIVFTS VFTIEIVLKM TVYGAFMHKG
SFCRNSFNIL DLIVVGVSLL SMGMRSSAIS VVKILRVLRV LRPLRAINRA KGLKQHVVQC
VFVAIKTIGN IVLVTLLLNF MFACIGVQLF KGKFHSCTDV SKVTEEECGF YLKHMENSLQ
DTVVAKREWL NNDFNFDNVL NGILALFTVS TFEGWPLLYK AIDSAEEDMG PVFNNRVDVS
IFFIIYIIII AFFMMNIFVG FVIVTFQQQG EQEYKNCELD KNQCVQYALK ARPLKCYIPK
NPYQYRVWYI VTSCYFEYLM FFLIMLNTLC LGMQHCNQSD HVTKLSDILN LIFTVLFTVE
MILKLMAFKA RGYFGDPWNV FDFIIVIGSV VDVILSEVDS ALADSGGLYC LHGCTNPMQV
IAASENASVS ITFFRLFRVM RLVKLLNRSE GIRNLLWTFI KSFQALPHVA LLIVMLFFIY
SVVGMQIFGK IALVDGTQVN RNNNFQTFPQ AVLMLFCATG EGWQEVMMAS MYGKKCDPKS
DFLPGEEYTC GSNFAVFYFL SFYCLCAFLI LNLFVAVIMD NFDYLTRDWS LLGPHHLDEF
KKIWAEYDPE AGRIKHLDVV TLLRSIQPPL GFGKFCPHRA ACKRLVGMNM PLNSDGTVTF
NATLFALVRT ALKIKTENFE QANEELRAII KQIWKRTSMK LLDQVIPPIG DEVTVGKFYA
TFLLQDHLRK FIKRQEEYYG YRPTKKSASG PEIQAGLRSI EEEAAPEMHR AISGDLQNEE
EMERAMEEAG EEAIYQVESF STEPANTQSQ QVTNMRPLSF SESQPESPPS SASALVSGTE
FFPTAPPKSN TNNNAFAFSF ERALEKSGLV SLARDPGFVS LTKKEMAEAM HISVSDMEGV
AQGILKERSS SMTPVKKRRP IP
//
