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Database: UniProt
Entry: A0A3Q1EIG6_9TELE
LinkDB: A0A3Q1EIG6_9TELE
Original site: A0A3Q1EIG6_9TELE 
ID   A0A3Q1EIG6_9TELE        Unreviewed;      1821 AA.
AC   A0A3Q1EIG6;
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   Acanthochromis polyacanthus (spiny chromis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Acanthochromis.
OX   NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000003279.1, ECO:0000313|Proteomes:UP000257200};
RN   [1] {ECO:0000313|Ensembl:ENSAPOP00000003279.1}
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   STRING; 80966.ENSAPOP00000003279; -.
DR   Ensembl; ENSAPOT00000012014.1; ENSAPOP00000003279.1; ENSAPOG00000000125.1.
DR   GeneTree; ENSGT00940000166169; -.
DR   InParanoid; A0A3Q1EIG6; -.
DR   Proteomes; UP000257200; 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; 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:SF2; VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1F; 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:UP000257200};
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        77..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        115..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        146..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        221..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        298..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        331..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        449..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        487..509
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        575..597
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        648..678
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        690..712
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        733..749
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        790..808
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        820..843
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        863..886
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        907..940
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1031..1058
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1110..1130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1142..1161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1245..1263
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1337..1360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1494..1528
FT                   /note="Voltage-dependent calcium channel alpha-1 subunit
FT                   IQ"
FT                   /evidence="ECO:0000259|SMART:SM01062"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1519..1538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         312
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         631
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         1004
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   CARBOHYD        277
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ   SEQUENCE   1821 AA;  205101 MW;  FEC1168282AE718D CRC64;
     RQQAGGGQQN GPQPLNAPPG GDAGKSDTLG STGSSRKRGG GAKKAMQANK SALRAPRALC
     CLTLSNPIPL TTVFKPFDIF ILLAIFANCV AMGVTKPYPD DDSNATNHQL EQVEYVFLVI
     FTIETFTKIL AYGLVMHPSA YIRSGWNLLD FIIVIVGLFS VIAEGMTDHK PGEAHHAAGK
     PGGLDVKALR AFRVLRPLRL VSGVPSLQIV LNSIMKAMVP LLHIGMLVMF VIIIYAIIGL
     ELFIGRMHKT CYFVSLMVED DPSPCAFAGS GRFCVGNGSE CRGKWEGPNG GITNFDNIFF
     AMLTVFQCIT MEGWTDVLYW MNDAIGYEIP WIYFVSLVIF GSFFIINLVL GVLSGEFSKE
     REKAVARGEL QKAQESKQME EDMIGYMDWL IEAEDVDEEG NKRYQNFCVC STESDSDDDI
     AYLDDDNGFC LCQLNHTFRK NCRVAVKTTN FYWLVLLLVF LNTVASASEH YGQPKWLTEM
     QERANKILLL LFTLEMLMKM YAFGLQIYFM ALFNRFDCFV VCGGILETLL VEFDVIPPIG
     ISVLRCIRLL RIFKMTRHWA ALSDLVNSLL NSMKAICSLL LLLFLFLIIF ALLGMQLFGG
     KFNFDETQMK RSTFDSFPQA LLTCFQILTG EDWNAVMYDG IMAYGGPIFP NMVVCIYFVI
     LFVCGNYILL NVFLAIAVDN LAGDAFGDKL VFLFAAAFTP ISYFYSNILT VYSERKRKRK
     KSGMRMKRKR MKMQGRLTCL LFVVGVAPLK PDFSGPKEKI VPIPDGSSFF ILGKKNCLRV
     ACHNLIHHPY FTNFILIFII LSSISLAAED PIKSHSFRNI VLGYADYVFT SVFTVEIVLK
     MTVYGAFLHT GSFCRNAFNL LDLLVVSVSL TSFFLHSSAI SVVKILRVLR VLRPLRAINR
     AKGLKNVVQC VFVAIRTIGN ILIVTTLLQF MFACIGVQLF KGRFYSCTDE AKHTPYECKG
     TFVVYKDGDM NHPMVRERIW QNSDFNFDNV LMGMLALFTV STFEGWPQLL YRAVDANAIN
     RGPIYNYRVE ISIFFIIYII IIAFFMMNIF VGFVIITFRE QGEAEFKNCE LNKNQRQCVY
     YALKAQPIKI YIPKNPSQLK FWKIINSSQF EYVMFVLILG NTLTLAVQHY EQSKLFTSIM
     DILNMIFTVV FTIEMIIKLL ALRAHHYFID PWNSFDALIV VGSVLDIAVS EFSGGGGHGE
     VRTDQSGKVS ITFFRLFRVL RLVKLLSKGE GIRTLLWTFV KSLQALPYVG LLIAMIFFIY
     AVIGMQTFGK VAVDDDTHIN RNCNFQTFFM AVLVLFRCAT GEQWQEIMLA ALPGRRCDPE
     SDTEPGEEFS CGSNLSYIYF ISFFMLCAYL IINLFIAVIM DNFEYLTRDW TVLGTHHLDE
     FKRVWSDYDP EATGRIKHID VVTMLRRIQP PLGFGKLCPH RVACKRLVAM NVPLHADGTV
     TFNATLFALV RTSLKIKTEG PIDQQNEELK VIIKKLWKRT KPKLIDEVIP PPRGDEVTSG
     KFYASFLIQD YFKKFRKRKE RERKSKRKDK AASLQQGLRT LQDLAPEMRL AMACDLEEEE
     ATEGEMTADE IFDSGTSANT TPASTPMPRL DMLVEQTTVI VEPEPKISNG DVITEQVTGL
     QEHQKPGSDL AGLNIVTEQP VRSELTVLHL AQFSNTSTCF LFSGRKPAFN FQCLRPQSSV
     DDLPIPGTYH GNTSPSRSRL QVEQRGKLIY TPMILVDEAT GTSQPLTFTS VRMPPPVNQG
     LVNKGSADSL VESILISEGL GVYARDPKFV NFAKREIAEA CHMSLDDMES AAADLIARGA
     SQSISRFEDE LADEMNCVIS Y
//
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