ID F1MTK5_BOVIN Unreviewed; 2183 AA.
AC F1MTK5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 2.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1D {ECO:0000313|Ensembl:ENSBTAP00000013226.5,
GN ECO:0000313|VGNC:VGNC:26674};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000013226.5, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000013226.5, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000013226.5,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000013226.5}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000013226.5};
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|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1D subfamily. {ECO:0000256|ARBA:ARBA00010354}.
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DR RefSeq; NP_001179954.1; NM_001193025.1.
DR SMR; F1MTK5; -.
DR STRING; 9913.ENSBTAP00000013226; -.
DR PaxDb; 9913-ENSBTAP00000013226; -.
DR Ensembl; ENSBTAT00000013226.6; ENSBTAP00000013226.5; ENSBTAG00000010026.6.
DR GeneID; 408013; -.
DR KEGG; bta:408013; -.
DR CTD; 776; -.
DR VEuPathDB; HostDB:ENSBTAG00000010026; -.
DR VGNC; VGNC:26674; CACNA1D.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000154839; -.
DR HOGENOM; CLU_000540_0_1_1; -.
DR InParanoid; F1MTK5; -.
DR OMA; TTIALQX; -.
DR TreeFam; TF312805; -.
DR Reactome; R-BTA-422356; Regulation of insulin secretion.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000010026; Expressed in adenohypophysis and 69 other cell types or tissues.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IBA:GO_Central.
DR GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IBA:GO_Central.
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; IPR005452; LVDCC_a1dsu.
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; 3.
DR Pfam; PF16905; GPHH; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR PRINTS; PR01630; LVDCCALPHA1.
DR PRINTS; PR01636; LVDCCALPHA1D.
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:UP000009136};
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 130..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 383..405
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 543..561
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 581..604
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 673..692
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 745..772
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 907..925
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 945..965
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 977..1003
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1023..1053
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1150..1175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1229..1247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1259..1279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1369..1387
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1461..1484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1618..1652
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 30..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1710..1789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1909..1965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2130..2174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..842
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..858
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1717..1732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1757..1782
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1909..1930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1937..1959
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 364
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 725
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 2183 AA; 247468 MW; 5DD6410FBF35A193 CRC64;
MMMMMMMKKM QHQRQQQADH ANEANYARGT RLPLSGEGPT SQPNSSKQTV LSWQAAIDAA
RQAKAAQTMS TSAPPPVGSL SQRKRQQYAK SKKQGNSSNS RPARALFCLS LNNPIRRACI
SIVEWKPFDI FILLAIFANC VALAIYIPFP EDDSNSTNHN LEKVEYAFLI IFTVETFLKI
IAYGLLLHPN AYVRNGWNLL DFVIVIVGLF SVILEQLTKE TEGGNHSSGK SGGFDVKALR
AFRVLRPLRL VSGVPSLQVV LNSIIKAMVP LLHIALLVLF VIIIYAIIGL ELFIGKMHKT
CFFADSDMVA EEDPAPCAFS GNGRQCTANG TECRSGWAGP NGGITNFDNF AFAMLTVFQC
ITMEGWTDVL YWVNDAIGWE WPWVYFVSLI ILGSFFVLNL VLGVLSGEFS KEREKAKARG
DFQKLREKQQ LEEDLKGYLD WITQAEDIDP ENEEEGGEES KRNTSMPTSE TESVNTENVS
GEGENRGCCG SLWCWWRRRG AAKAGPSGCR RWGQAISKSK LSRRWRRWNR FSRRRCRAAV
KSVTFYWLVI VLVFLNTLTI SSEHYNQPDW LTQIQDIANK VLLALFTCEM LVKMYSLGLQ
AYFVSLFNRF DCFVVCGGIT ETILVELEIM SPLGISVFRC VRLLRIFKVT RHWTSLSNLV
ASLLNSMKSI ASLLLLLFLF IIIFSLLGMQ LFGGKFNFDE TQTKRSTFDN FPQALLTVFQ
ILTGEDWNAV MYDGIMAYGG PSSSGMIVCI YFIILFICGN YILLNVFLAI AVDNLADAES
LNTAQKEEAE EKERKKIARK ESLENKKNNK PEVNQIANSD NKVTIDDYRE EDEDKDPYPP
CDVPVGEEEE EEEEDEPEVP AGPRPRRISE LNMKEKIAPI PEGSAFFILS KTNPIRVGCH
KLINHHIFTN LILVFIMLSS AALAAEDPIR SHSFRNTILG YFDYAFTAIF TVEILLKMMT
FGAFLHKGAF CRNYFNLLDM LVVGVSLVSF GIQSSAISVV KILRVLRVLR PLRAINRAKG
LKHVVQCVFV AIRTIGNIMI VTTLLQFMFA CIGVQLFKGK FYRCTDEAKS NPEECRGLFI
LYKDGDVDSP VVRERIWQNS DFNFDNVLSA MMALFTVSTF EGWPALLYKA IDSNGENVGP
IYNYRVEISI FFIIYIIIVA FFMMNIFVGF VIVTFQEQGE KEYKNCELDK NQRQCVEYAL
KARPLRRYIP KNPYQYKFWY VVNSSPFEYM MFVLIMLNTL CLAMQHYEQS KMFNDAMDIL
NMVFTGVFTV EMVLKVIAFK PKGYFSDAWN TFDSLIVIGS IVDVALSEAD PTESESVPVP
TATPGNSEES NRISITFFRL FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL PYVALLIAML
FFIYAVIGMQ MFGKVAMRDN NQINRNNNFQ TFPQAVLLLF RCATGEAWQE IMLACLPGKQ
CDPDSDYNPG EEYTCGSNFA IVYFISFYML CAFLIINLFV AVIMDNFDYL TRDWSILGPH
HLDEFKRIWS EYDPEAKGRI KHLDVVTLLR RIQPPLGFGK LCPHRVACKR LVAMNMPLNS
DGTVMFNATL FALVRTALKI KTEGNLEQAN EELRAVIKKI WKKTSMKLLD QVVPPAGDDE
VTVGKFYATF LIQDYFRKFK KRKEQGLVGK YPAKNSTIAL QAGLRTLHDI GPEIRRAISC
DLQDDDPEET KREDEEDVFK RNGALLGNHV NHVNSDRRDS LQQTNTTHRP LHVQRPSIPP
ASDTEKPLFP PAGNSVCHNH HNHNSIGKQV PSSTNANLNN ANMCKAAPGK RPSIGNLELV
SENGHHSFHK HGREPHRRCS IKRTRYYETY IRSDSGDEQF PTICREDPEI HGYFRDPHCP
GEQEYFSSEE YYEDDSSPTG SRQSYGCGYY NWYLGSSLDF EWPRGYHHPQ SFSEDDDSPV
GYDSRRSPRR RLLPPTPTSP RRSSFNFECL RRQSSQEEVP PSPAFPPRTA LPLHLMQQQI
MAVAGLDSSK AQKYSPSHST RSWATPPATP SYRDWTPCYT PLIQVERPEA PDQVNGSLPS
LHRSSWYTDE PSVSYRTFTP ASLTVPSSFH NKNSDKQRSA DSLVEAVLIS EGLGRYARDP
KFVSATKHEI ADACDLTIDE MESAASNLLN GNVHPRANGD VGPVSHRQDY ELQDFGPGYS
DEEPDPGRDE EDLADEMICI TTL
//
