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Database: UniProt
Entry: A0A3Q1B9J0_AMPOC
LinkDB: A0A3Q1B9J0_AMPOC
Original site: A0A3Q1B9J0_AMPOC 
ID   A0A3Q1B9J0_AMPOC        Unreviewed;      2018 AA.
AC   A0A3Q1B9J0;
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 P/Q-type calcium channel subunit alpha-1A {ECO:0000256|ARBA:ARBA00039688};
DE   AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.1 {ECO:0000256|ARBA:ARBA00041622};
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:ENSAOCP00000006671.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000006671.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU003808}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC       1.A.1.11) family. CACNA1A subfamily. {ECO:0000256|ARBA:ARBA00037936}.
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DR   Ensembl; ENSAOCT00000004166.1; ENSAOCP00000006671.1; ENSAOCG00000010481.1.
DR   GeneTree; ENSGT00940000156518; -.
DR   OMA; AFRMIRV; -.
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; 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:SF3; VOLTAGE-DEPENDENT P_Q-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1A; 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   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        64..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        200..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        326..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        401..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        824..842
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        862..882
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        894..912
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        956..978
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1068..1093
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1149..1168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1180..1202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1259..1288
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1360..1384
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1522..1556
FT                   /note="Voltage-dependent calcium channel alpha-1 subunit
FT                   IQ"
FT                   /evidence="ECO:0000259|SMART:SM01062"
FT   REGION          528..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          584..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          771..797
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1552..1606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1620..2018
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          423..459
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        540..559
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..652
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1575..1606
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1640..1659
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1662..1685
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1699..1722
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1735..1750
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1751..1766
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1785..1812
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1850..1865
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1872..1897
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1920..1939
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1964..1979
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         45
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         380
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   BINDING         1039
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT   CARBOHYD        10
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ   SEQUENCE   2018 AA;  230503 MW;  49F0F2519FF8474F CRC64;
     NELPSRLCPN GTVCRKGWLG PNYGITQFDN ILFAVLTVFQ CITMEGWTDM LYYSNDVEGS
     AWNWMYYIPL IIIGSFFMLN LVLGVLSGEF AKERERVENR SEFLKLRRQQ QIERELNGYL
     EWICKAGQCS LTNTHCRRRP TIKTKNNKTE LLNPEEGEDN MGDAVGFARS SIKSGKDGSS
     YSKKERRMRF FIRKIVKTQA FYWTVLCLVG LNTICVAAVH YNQPELLSDF LFYAEFIFLG
     LFMSEMLIKM YGLGIQPYFH SSFNCFDCVV IVGSIFEVVW ATIKPGTSFG ISVLRALRLL
     RIFKVTKYWA PLRNLVVSLL NSMKSIVSLL FLLFLFIVVF ALLGMQLFGG QFNFEGGTPP
     TNFDTFAAAI MTVFQILTGE DWNVVMYDGI ESQGGVNDKG MVFSIFFIVL TLFGNYTLLN
     VFLAIAVDNL ANAQELTKDE EEQEEAANQK TALQKAKEVA EVSPLSAANL SIAAKEQQKN
     HTKGNKSVWE QRTSEIRRQN LMTSREALYN ELEQDDWKVS YPRKARGDMK THLDRPLVVN
     PQDNRNNNTN KTQPGELPLD QEYQRQDIDH CRRAAHYYHY HHRPHQNAIG PHSARSVSPH
     HSEGMQGNNE HRRSRQHRRA AREGEEGRRH RSRGTEGEGD RGEDGEGRKT RRHRHGNQER
     SRGHRMRNTG PNLSTTRPIQ QYNEDLDNFR NNSKLASAHE HPYALPPDHP DHPDHVNNLL
     NCRDADTHTL LHSMDSLILT SMAKPEYTTI DMPPVYPYPS TNAILQVNKN ANTDQKKSEE
     KKEEEDEGGD EDGPKPMPPY SSCFIMSTTN PFRKCCHYIL TLKYFEFSIL SVIAMSSIAL
     AAEDPVWPDS PQNNVLRYFD YVFTGVFTFE MLIKMVVLGL FLHQGSYFRD LWNILDFIVV
     SGALVAFAFT GSSKGKDIST IKSLRVLRVL RPLKTIKRLP KLKAVFDCVV NSLKNVLNIL
     IVYMLFMFIF AVVAVQLFKG RFFFCTDESK EFERDCRGEY LVYDREKVEA QKREWKKYDF
     HYDNVAWALL TLFTVSTGEG WPQVLKHSVD STYENQGPSP GYRMEMSIFY VVYFVVFPFF
     FVNIFVALII ITFQEQGDKM MEDYSLEKNE RACIDFAINA RPLTRHMPKN KLSFQYRMWQ
     FVVSQPFEYS IMALIALNTI VLMMKFDGAS DTYNDVLKNL NIVFTTFFFM ESVLKIIAFG
     PLNYFRDAWN IFDFVSVLGS ITDILVTELG NNFINLSFLR LFRAARLIKL LRQGETIRIL
     LWTFVQSFKA LPYVCLLIAM LFFIYAIIGM QLFGNLALDE EGESAINEHN NFRTFIMALM
     LLFRSATGEA WHEIMLACLG GKECDPASGN TEPECGSTFA YTYFVSFIFL CSFLMLNLFV
     AVIMDNFEYL TRDSSILGPH HLDEYVRIWA EYDPAACGRI HYKDMYSLLR VISPPLGLGK
     KCPHRVACKR LLRMDLPVAD DNTVHFNSTL MALIRTALDI KIAKGGADKH QMDAELRKEM
     MAIWPNLSQK TLDLLVTPHK AATDLTVGKI YAAMMIMEYY RQSKTKKLQA LREEQNRPPL
     MFQRMKPPSE GGGTDVQGGQ GQNGLPSTQP DNMNSIPPEG GMTESQSWMT TKAQEMFQKT
     GNWSPDRPYP DDPHDNRHNP QTITDTSPMH RSTSSLVHGR SGRGVRLDDY SLERVVSEEG
     RHGGGRRHRE RSHRTSQRSL TRYTDADTGL GTDLSTTTQS GDLPPKEHER DRGRTKDRRH
     HHHHHHHHSS MDKEHYGPDR HDYPHRHPHD RHWSRSPSEG PDGRGPRQGS SSVSGSPVPS
     TSGTSTPRRG RRQLPQTPAV PRPHVTYSPA VRKPSYGPPG PGRLRSPSPR HFSPPDHDRG
     YHHRPPSRHA SPHHGGSSSR HGSPHSPRHQ SPRSPLHGSP RSPHRSRWSG PPPGDSLEGD
     GPFYERDYEY ERHHEPPAYE QSLSHGNPHP HGGNPHPHPR SPRTARHGPP PPPHPHPRRV
     PNGYRSSSPS PHRRGPPGAG PRKGLHEPYS ETDEDDWC
//
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