ID I3LM43_PIG Unreviewed; 1976 AA.
AC I3LM43;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 4.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1C {ECO:0000313|Ensembl:ENSSSCP00000025163.4};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000025163.4, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000025163.4, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000025163.4,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000025163.4}
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: Cell membrane, sarcolemma, T-tubule
CC {ECO:0000256|ARBA:ARBA00024012}. Cell membrane, sarcolemma
CC {ECO:0000256|ARBA:ARBA00004415}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004415}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651}. Cell projection, dendrite
CC {ECO:0000256|ARBA:ARBA00004279}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU003808}. Perikaryon
CC {ECO:0000256|ARBA:ARBA00004484}. Postsynaptic density membrane
CC {ECO:0000256|ARBA:ARBA00034112}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1C subfamily. {ECO:0000256|ARBA:ARBA00024028}.
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DR AlphaFoldDB; I3LM43; -.
DR STRING; 9823.ENSSSCP00000025163; -.
DR PaxDb; 9823-ENSSSCP00000025163; -.
DR Ensembl; ENSSSCT00000030429.4; ENSSSCP00000025163.4; ENSSSCG00000041764.2.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000156127; -.
DR HOGENOM; CLU_500527_0_0_1; -.
DR InParanoid; I3LM43; -.
DR Proteomes; UP000008227; Chromosome 5.
DR Bgee; ENSSSCG00000041764; Expressed in heart left ventricle and 29 other cell types or tissues.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030315; C:T-tubule; IEA:UniProtKB-SubCell.
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; IPR005451; VDCC_L_a1csu.
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:SF10; VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1C; 1.
DR Pfam; PF08763; Ca_chan_IQ; 1.
DR Pfam; PF16885; CAC1F_C; 2.
DR Pfam; PF16905; GPHH; 1.
DR Pfam; PF00520; Ion_trans; 5.
DR PRINTS; PR00167; CACHANNEL.
DR PRINTS; PR01630; LVDCCALPHA1.
DR PRINTS; PR01635; LVDCCALPHA1C.
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 Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
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 115..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 196..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 229..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 372..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 409..432
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 501..520
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 571..591
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 718..740
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 760..781
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 839..868
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 964..991
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1042..1059
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1071..1093
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1105..1122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1198..1221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1291..1315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1449..1483
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 627..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1566..1587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1681..1719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1919..1976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 553
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 937
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 1976 AA; 220765 MW; A04A8AE71D9F6B4A CRC64;
HLTHPNPLAS EGCFSSTPCS GISAGQNFPN PRANDCLSSA FDSLTCPLSF PSRLFSAILE
QATKADGANA LGGKGAGFDV KALRAFRVLR PLRLVSGVPS LQVVLNSIIK AMVPLLHIAL
LVLFVIIIYA IIGLELFMGK MHKTCYNQEG VPDVPAEDDP SPCALETGHG RQCQNGTVCK
PGWDGPKHGI TNFDNFAFAM LTVFQCITME GWTDVLYWVN DAVGRDWPWI YFVTLIIIGS
FFVLNLVLGV LSGEFSKERE KAKARGDFQK LREKQQLEED LKGYLDWITQ AEDIDPENED
EGMDEEKPRN MSMPTSETES VNTENVAGGD IEGESCGARL AHRISKSKFS RYWRRWNRFC
RRKCRAAVKS SIFYWLVIFL VFLNTLTIAS EHYNQPRWLT EVQDTANKAL LALFTAEMLL
KMYSLGLQAY FVSLFNRFDC FIVCGGILET ILVETKVMSP LGISVLRCVR LLRIFKITRY
WNSLSNLVAS LLNSVRSIAS LLLLLFLFII IFSLLGMQLF GGKFNFDEMQ TRRSTFDNFP
QSLLTVFQIL TGEDWNSVMY DGIMAYGGPS FPGMLVCIYF IILFICGNCI LCSCPPTPTP
LPYPSASSLS LARTASPEKK QEVEKIELKS ITADGESPPA TKINMDDLQP NENEDKCSYP
NPETAGEEDE EEPEMPVGPR PRPLSELHLK EKAVPMPEAS AFFIFSPNNR FRLQCHRIVN
DSIFTNLILF FILLSSISLA AEDPVQHTSF RNHILGNADY VFTSIFTLEI ILKMTAYGAF
LHKGSFCRNY FNILDLLVVA VSLISFGIQS SAINVVKILR VLRVLRPLRA INRAKGLKHV
VQCVFVAIRT IGNIVIVTTL LQFMFACIGV QLFKGKLYTC SDSSKQTEAE CKGNYITYKD
GEVDHPIIQP RSWENSKFDF DNVLAAMMAL FTVSTFEGWP ELLYRSIDSH TEDKGPIYNY
RVEISVFFII YIIIIAFFMM NIFVGFVIVT FQEQGEQEYK NCELDKNQRQ CVEYALKARP
LRRYIPKNQH QYKVWYVVNS TYFEYLMFVL ILLNTICLAM QHYGQSCLFK VAMNVLNMLF
TGLFTVEMIL KLIAFKPKGY FSDPWNVFDF LIVIGSVIDV ILSETNHYFC DAWNTFDALI
VVGSIVDIAI TEVNNAEENS RISITFFRLF RVMRLVKLLS RGEGIRTLLW TFIKSFQALP
YVALLIVMLF FIYAVIGMQV FGKIALNDTT EINRNNNFQT FPQAVLLLFR CATGEAWQDI
MLACMPGKKC APESEPGNST EGETPCGSSF AVFYFISFYM LCAFLIINLF VAVIMDNFDY
LTRDWSILGP HHLDEFKRIW AEYDPEAKGR IKHLDVVTLL RRIQPPLGFG KLCPHRVACK
RLVSMNMPLN SDGTVMFNAT LFALVRTALR IKTEGNLEQA NEELRAIIKK IWKRTSMKLL
DQVVPPAGDD EVTVGKFYAT FLIQEYFRKF KKRKEQGLVG KPSQRNALSL QAGLRTLHDL
GPEIRRAISG DLTAEEELDK AMKEAVSAAS EDDIFRRAGG LFGNHVGYYP SDSRSAFPQT
FTTQRPLHIS KAGNSQGDTE SPSHEKLVDS TFTPSSYSST GSNANINNAN NTALGRCPHL
AGHPSAVSTV EGRGPPLSPA VRVQEAAWRQ SSKRHLSQES QLAMVCQEEA SRDETCDVRA
NEDEEYGSEP SLISTEMLSY QDDESRQLTP PEEDRRDIRL SPKRGFLRSA SLGRRASFHL
ECLKRQKNQG DVSQKTVLPL HLVHHQALAV AGLSPLLQRS HPPGTFPLPC TTPPATPGPG
WPLRPVPTLR LEGAESSEKL TSSFPSVHCG PRAGEPTPCG AGSGPRRARP VSLTVPSPAG
TRGRQFHGSA SSLVEAVLIS EGLGQFAQDP RFLEATTQEL ADACDMTIEE MESAADNILS
GGAGQSPNGT LLPFANCRDP GPDRAGGAED AAWAPGPEPR QGEDELLDSR AFASSL
//
