ID W5UIF5_ICTPU Unreviewed; 2123 AA.
AC W5UIF5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1D {ECO:0000313|EMBL:AHH41801.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|EMBL:AHH41801.1};
RN [1] {ECO:0000313|EMBL:AHH41801.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Mixed {ECO:0000313|EMBL:AHH41801.1};
RX PubMed=23127152; DOI=10.1186/1471-2164-13-595;
RA Liu S., Zhang Y., Zhou Z., Waldbieser G., Sun F., Lu J., Zhang J.,
RA Jiang Y., Zhang H., Wang X., Rajendran K.V., Khoo L., Kucuktas H.,
RA Peatman E., Liu Z.;
RT "Efficient assembly and annotation of the transcriptome of catfish by RNA-
RT Seq analysis of a doubled haploid homozygote.";
RL BMC Genomics 13:595-595(2012).
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 EMBL; JT415728; AHH41801.1; -; mRNA.
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 2: Evidence at transcript level;
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}; 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 129..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 348..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 381..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 521..539
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 559..581
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 648..670
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 726..750
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 871..890
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 902..924
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 944..967
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 988..1021
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1071..1092
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1113..1139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1182..1207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1219..1241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1253..1270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1319..1336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1410..1433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1567..1601
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 17..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1837..1885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2079..2109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..820
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2079..2096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 362
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 703
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1085
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 2123 AA; 239927 MW; 780F9FA6FF11CC35 CRC64;
MAFISWRPGR RGASYAISTR APSSGDAPPL WSESPSLSRQ SLPQSGALSW QAAITAARNA
RADGTQTIST SDSAPVGSLS QRKRQQYAKS KKQGSSTNSR PPRALFCLTL NNPIRRACIS
LVEWKPFDIF ILLSIFANCV ALAVYIPFPE DDSNSTNHDL ETVEYAFLII FTIETFLKII
AYGLVMHQNS YVRNGWNMLD FIIVIVGLFS VVLELMTKEG DSGQSGGKPG GFDVKALRAF
RVLRPLRLVS GVPSLQVVLN SIIKAMVPLL HIALLVLFVI IIYAIIGLEL FIGKMHATCY
MNGTRTLAEE EPTPCTLSGH GRHCSVNGST CRDGWQGPNN GITNFDNFLF AMLTVFQCIT
MEGWTEVLYW MNDAMGFELP WVYFVSLVIF GSFFVLNLVL GVLSGEFSKE REKAKARGDF
QKLREKQQLE EDLKGYLDWI TQAEDIDPEN DEDGDQEGKR NPSMPTSETE SVNTDSPNGE
DDKICCCGPV CQKITKSKFS RSWRRWNRFC RRKCRAAVKS TSFYWLVIVL VFLNTLTISS
EHYNQPVWLT EVQDVANKVL LAMFTCEMLI KMYSLGLQAY FVSLFNRFDC FVVCGGIVET
ILVELEIMSP LGISVFRCVR LLRIFKVTRH WASLSNLVAS LLNSMKSIAS LLLLLFLFII
IFSLLGMQLF GGKFNFDETM TKRSNFDNFP QALLTVFQIL TGEDWNAVMY DGIMAYGGPS
SSGMMVCIYF IILFICGNYI LLNVFLAIAV DNLADAESLN SAQKEQEEEN KRKKRARRKG
SMDKKEEDKG GEDGETKGAL EEDTGDEERE AVNSTDVDDD QDVPSEPRPQ KLSDFSLKEK
IPPIPEGSAF FIFSHTNPFR VGCYRLINHQ IFTNITLVFI MLSSFSLAAE DPIRNLSARN
TILGYFDYAF TAIFTVEILL KMTAYGAFLH KGAFCRNYFN LLDLLVVGVS LVSFGIQSSA
ISVVKILRVL RVLRPLRAIN RAKGLKHVVQ CVFVAIRTIG NIMIVTTLLQ FMFACIGVQL
FKGKFYRCTD EAKSSEQECK GTFILYNIGD NALPQVRERK WLNSEFNFDN VLNAMMALFT
VSTFEGWPTL LYKAIDSNRE NMGPIYNYRI EISIFFIIYI IIIAFFMMNI FVGFVIVTFQ
EQGEKEYKNC ELDKNQRQCV EYALKARPLR RYIPKNHYQY KFWYVVNSTG FEYVMFVLII
LNTLCLAVQH HGQSHRFNYA MDILNMMFTG VFTVEMILKL IAFKPRGYFG DAWNVFDALV
VIGSVVHIIL SQVDNTEDSG RISITFFRLF RVMRLVKLLS RGEGIRTLLW TFIKSFQALP
YVALLIAMLF FIYAVIGMQV FGKIAMVDGT HINRNNNFQT FPQAVLLLFR CATGEAWQEI
MLACMPGKLC DSESEITPGE EKSCGSGFAI IYFISFYMLC AFLIINLFVA VIMDNFDYLT
RDWSILGPHH LDEFKRIWSE YDPEAKGRIK HLDVVTLLRR IQPPLGFGKL CPHRVACKRL
VAMNMPLNSD GTVMFNATLF ALVRTALKIK TEGNLEQANE ELRAVIKKIW KRTSSKLLDQ
VVPPAGDDEV TVGKFYATFL IQDYFRKFKK RKELGLVGRH PTSHNTTIVL QAGLRTLHDI
GPEIRRAISC DLQDEDLVDF NPDEEDIYRR NGGLFGNHVN HVNGDHRGSS TSTNVTQRPL
HVPPLPFYVQ VEPPPQPLYA QNRPYSNPNL YFKSPKSSNS NLNNANVPCM PVLTNGGQYR
PHTDRLTRSR VSSLGSYLNL RSDAESQRKS HFKRPRYYET YIRSDSTAGF YPTICRQASL
HGDVSDDDRG SVEYYSGEEF QEDDLILAGD RRSYREYQDT VSSLESNPPH ENQDPECFYD
DDEQPICQEP KKSPMRRLLP STPQAPHRPS FNFECLCRQR SQDETPHSPS FHQHTALPLQ
LMQHQVMAVA GLDSSRARLS PTRSIQSWST PPDTPPSYTP LIQVDWHGEP PSASSTPALA
RRSSWYTQKG HDWSPKSVTP TSSLLQIPPA YSSQYLQQRG SAHSLVEAVL ISEGLGKYAK
DPNFVAAAKH EIADACEMTI DEMESAASNL LNGSLGNSVG SDGTGTPQSI IGHSLHNYSD
EETEPNSKYE EDLTDEIICI SNL
//
