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Database: UniProt
Entry: A0A3Q1B2M6_AMPOC
LinkDB: A0A3Q1B2M6_AMPOC
Original site: A0A3Q1B2M6_AMPOC 
ID   A0A3Q1B2M6_AMPOC        Unreviewed;      1983 AA.
AC   A0A3Q1B2M6;
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   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000007009.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000007009.1}
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; ENSAOCT00000003601.1; ENSAOCP00000007009.1; ENSAOCG00000010953.1.
DR   GeneTree; ENSGT00940000154839; -.
DR   Proteomes; UP000257160; 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: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:UP000257160};
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        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        44..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        149..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        228..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        261..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        400..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        438..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        469..492
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        527..546
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        598..622
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        708..726
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        738..761
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        781..804
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        825..850
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        908..929
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        950..976
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1019..1044
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1056..1080
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1162..1180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1254..1277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1411..1445
FT                   /note="Voltage-dependent calcium channel alpha-1 subunit
FT                   IQ"
FT                   /evidence="ECO:0000259|SMART:SM01062"
FT   REGION          327..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          636..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1538..1562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1614..1638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1663..1690
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1713..1750
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        636..652
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1614..1633
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1669..1690
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1718..1732
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         242
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         575
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         922
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ   SEQUENCE   1983 AA;  224002 MW;  E8F1C91082BA4E18 CRC64;
     FLVEILCLSV VYSSVFVLTL SVLFCFLPSV FLPSFVSVQE TVEYAFLIIF TIETFLKIIA
     YGLVMHQNSY VRNGWNMLDF VIVIVGLFSV VLEMITKDAD SGGQSGGKPG GFDVKALRAF
     RVLRPLRLVS GVPSLQVVLN SIIKAMVPLL HIALLVLFVI IIYAIIGLEL FIGKMHATCY
     LIQTGVLAEE EPTPCAVSGH GRHCLLNGTV CREGWQGPNS GITNFDNFLF AMLTVFQCIT
     MEGWTDVLYW MNDAMGFELP WVYFVSLVIF GSFFVLNLVL GVLSGEFSKE REKAKARGDF
     QKLREKQQLE EDLKGYLDWI TQAEDIDPEN EEEGDEEGKR NPSMPSETES VNTENHNGDD
     SKSPCCGPLC QKITKSKCSR QWRRWNRFCR RKCRAAVKSV TFYWLVIILV FLNTLTIASE
     HYNQPDWLTE VQDVANKVLL ALFTLEMLVK MYSLGLQAYF VSLFNRFDCF VVCGGIVETI
     LVELAIMSPL GISVFRCVRL LRIFKVTRHW ASLSNLVASL LNSMKSIASL LLLLFLFIII
     FSLLGMQLFG GKFNFDEAVT KRSTSAGLHS ILTGEDWNTV MYDGIMAYGG PASSGMVVCI
     YFIILFICGN YILLNVFLAI AVDNLADAES LNTAQKEEEE AKKRKNMCDD DENNDNLPEV
     PSGPRPQRLS ELTIKEKTPP IPEGSAFFIF SSTNPFRVFC HKLINHQIFT NLILVFIMLS
     SVSLAAEDPI RNFSARNIIL GYADYVFTSM FTFEILVKMT AFGAFLHKGA FCRNYFNLLD
     LLVVGVSLVS FGIQSSAISV VKILRVLRVL RPLRAINRAK GLKHVVQCVF VAIRTIGNIM
     IVTTLLQFMF ACIGVQLFKG KFYQCTDDAK SSPDECKGKY ILYNNGDTAM PMVKERIWYN
     SDFNFDNVLM AMMALFTVST FEGWPTLLYK AIDSNRENMG PIYNYRIEIS IFFIIYIIII
     AFFMMNIFVG FVIVTFQEQG EKEYKNCELD KNQRQCVEYA LKARPLRRYI PKNPYQYKFW
     YVVNSTGFEY VMFVLIILNT LCLAIQHHGQ SPLFNYAMDI LNMVFTGVFT VEMILKLIAF
     KPRNYFADAW NTFDALIVVG SVVDIAITEI NVSSRLSHNT EDSARISITF FRLFRVMRLV
     KLLSRGEGIR TLLWTFIKSF QALPYVALLI AMLFFIYAVI GMQVFGKIAM VDGTQINRNN
     NFQTFPQAVL MLFRCATGEA WQEIMLACLP GKLCDSESDY NPGEERTCGS GFAIIYFISF
     YMLCAFLIIN LFVAVIMDNF DYLTRDWSIL GPHHLDEFKR IWSEYDPEAK GRIKHLDVVT
     LLRRIQPPLG FGKLCPHRVA CKRLVAMNMP LNSDGTVMFN ATLFALVRTA LKIKTEGNLE
     QANEELRAVI KKIWKRTSMK LLDQVVPPAG DDEVTVGKFY ATFLIQDYFR KFKRRKEQGL
     VGRRSWERLN TTLALQAGLR TLHDIGPEIR RAISCDLQEA GLVDANGEEE EEIYRRNGGL
     FGNHINHFSG DQPGSFHPTT VTQRPLQILP FSCSASVEPV QTERRGSGSD REGETEMNCS
     PVRYNHHPSP RLYDYPHCNS TCPQPPIPSN ANLNNANMPS LLSMTVGRQQ KCLLRRSRPS
     STRHGSSVTS YSKGVHDKPW KSHSIRTRYY EAYIRYSGGG LYPTIRREEP AAGDSDDDRG
     SGEYYSGEEF HEDDIMLTKD RYSEADFELQ VSGGDRQADG YYDDDQQPIY QDGRRSPRRW
     FLPSPQASTR PTFSFECLRR KSSHDDAPPS PSCTALPLHL VQQQVMAVAG LDASRIHRLS
     PTRSLRSWTT PPASPISRDC SPCYTPLIQV DWRSSGSVSS IPGAVKRSSW YTEGPDGPPS
     RCHSPSRLQL PAESCLRFLQ KRGSANSLVE AVLISEGLGK YARDPKFVSA TKHEIADACE
     MSIDEMESAA SNLGGGTGGG VTDQHANTLL RDHSIRDYSD EEPYVALKCE EDLTDEMICI
     TSL
//
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