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Database: UniProt
Entry: A0A3B4BLG3_9GOBI
LinkDB: A0A3B4BLG3_9GOBI
Original site: A0A3B4BLG3_9GOBI 
ID   A0A3B4BLG3_9GOBI        Unreviewed;      1701 AA.
AC   A0A3B4BLG3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Voltage-dependent calcium channel alpha-1 subunit IQ domain-containing protein {ECO:0000259|SMART:SM01062};
OS   Periophthalmus magnuspinnatus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX   NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000029576.1, ECO:0000313|Proteomes:UP000261520};
RN   [1] {ECO:0000313|Ensembl:ENSPMGP00000029576.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   Ensembl; ENSPMGT00000031481.1; ENSPMGP00000029576.1; ENSPMGG00000018971.1.
DR   Proteomes; UP000261520; 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; 3.
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: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   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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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}; 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        58..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        91..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        210..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        235..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        335..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        412..434
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        707..726
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        779..798
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        844..866
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        958..983
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1036..1054
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1074..1095
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1151..1169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1248..1271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1408..1442
FT                   /note="Voltage-dependent calcium channel alpha-1 subunit
FT                   IQ"
FT                   /evidence="ECO:0000259|SMART:SM01062"
FT   REGION          470..662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1504..1642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1682..1701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          430..457
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        501..526
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..541
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..592
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..662
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1504..1521
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1522..1562
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1577..1614
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1625..1639
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         72
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         388
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         929
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
SQ   SEQUENCE   1701 AA;  195444 MW;  4200BF6BD698B254 CRC64;
     MFAIIGLEFY SGKLHHTCLT VDSSELAFAC GVRKCPDKYD CNDTWIGPND GITQFDNILF
     AVLTVFQCIT MEGWTAVLYN TNDALGPTWN WLYFIPLIII GSFFVLNLVL GVLSGEFAKE
     RERVENRRAF MKLRRQQQVE RELNGYRAWI DRAEEVMLAE ESKNSGRSPL DERTKVNESG
     LLFFFISAYL RRKERMLRIS IRRMVKTDTF YLLVLSLVAL NTICVAIVHH DQPDWLTIFL
     YYAEFVFLGL FLAEMCLKMY GLGFRLYFNS SFNCFDCAVI IGSIFEVVWG FFRPGMSFGI
     SVMRALRLLR IFKITKYWAS LRNLVVSLMS SMKSIISLLF LLFLFIVVFA LLGMQLFGGR
     FIFEDYTPTN FDTFPAAIMT VFQILTGEDW NEVMYNGIRS QGGVQYGMWS SIYFIVLTLF
     GNYTLLNVFL AIAVDNLANA QELTKDEEEE EEFFNQRPYL YRKRAIHRGR PNFPDEADGG
     TGPPDEQPLN GAKAFANRRE RRRKVNMSVW EQRANQLRKR RQMASREELF SNPTEDTAET
     STIPHHGPAL SPMSESEPPM SITIPIPEPP TSEPLVNISE EKTPTSNHRT TGGSRHRMAR
     KFRGSEDGAR HRRHRHREAR AEAKSLDCTL APNEGTRVKR SLSQDPRVLD EQDEKEEERE
     KTDVVQDEDG TCIVNPYADV GEESRKFVKL SCSVCSIRRI CHYVVNLRYF EMTILLVIVA
     SSIALAAEDP VCTNSERNKV LRYFDYVFTG VFTFEMIIKM IDQGLILHDG SYFRDMWNLL
     DFIVVVGALI AFALTNVMGN NKGRDIKTIK SLRVLRVLRP LKTIKRLPKL KAVFDCVVTS
     LKNVFNILIV YQLFMFIFAV IAVQLFKGKF FYCTDSSMKT VTERYCDGYY IDYSRDKKEV
     KRREWRRHEF HYDNVCWALL TLFTVSTGEG WPQVLQHSTD VTEENMGPSR GNRMEMSIFY
     VVYFVVFPFF FVNIFVALII ITFQEQGDKM IQECSLEKNE RACIDFAISA KPMTRYMPQN
     RQTVQYRLWH FVASPSFEYT IMVMIALNTV VLMMKYHSAP TAYDYVLKHL NTAFTVLFSM
     ECILKIMAFG FVNYFRDTWN IFDFITVLGS ITEISVNTIN MSFLXXXXTK VLRQGYTIRI
     LLWTFVQSFK ALPYVCLLIA MLFFIYAIIG MQVFGNIKLN DDSHINQHNN FKTFFSALML
     LFRSATGESW QEIMLSCLSG QECEPDPSLA PFTMSPDHEG GCGTDFAYCY FVSFIFFSSF
     LMLNLFVAVI MDNFEYLTRD SSILGPHHLD EFVRIWGEYD RLACGRIHYT AMYEMLTHMS
     PPLGLGKKCP AKIAYKRLVL MNMPVDEDMT VHFTSTLMSL IRTALDIKIA RGGEDRIALD
     SELQKEISII WPYLPQKTLD LLVPINKDTD MTVGKIYASM MIMDYFKQNK AKKLRQQLEA
     QVLCCSRVTS RVRRECTGPA TRATRPLVSD VTPVRRPPLN THLFILCHCP HLLCVTAPPV
     SRSERQHAER ERRHLLSPDR SRCNSADRSQ QPSRSSSVER GNSSDSPVPS TSESSTPSGR
     RPMSRPHISY SPLASRPQPE DEDEPGSPET IRRVKSKRES KESKGERRRN PSPPRRYPSE
     PFLASQEQDD EQSPDPTGPI ETLTFEAAVA CSLGRSNTIN IGARSRTGWQ VPNGHFRKRL
     AQTTSVTGCD PLSDTEEDDR C
//
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