ID A0A2K5ZFY1_MANLE Unreviewed; 2138 AA.
AC A0A2K5ZFY1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1C {ECO:0000313|Ensembl:ENSMLEP00000026737.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000026737.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000026737.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 Ensembl; ENSMLET00000050279.1; ENSMLEP00000026737.1; ENSMLEG00000035547.1.
DR GeneTree; ENSGT00940000156127; -.
DR Proteomes; UP000233140; Unplaced.
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; 5.
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; 1.
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; 5.
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:UP000233140};
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 111..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 365..387
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 508..525
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 545..568
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 637..656
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 709..736
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 879..901
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 921..942
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1000..1029
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1125..1152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1203..1220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1232..1254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1266..1283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1359..1382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1452..1476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1610..1644
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 56..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1730..1797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1941..2009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1730..1775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1949..1966
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1978..2009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 346
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 689
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 1098
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 2138 AA; 239519 MW; 7927CB3904C48813 CRC64;
SNYGSPRPAH ANMNANAAAG LAPEHIPTPG AALSWQAAID AARQAKLMGS AGNATISTVS
STQRKRQQYG KPKKQGSTTA TRPPRALLCL TLKNPIRRAC ISIVEWKPFE IIILLTIFAN
CVALAIYIPF PEDDSNATNS NLERVEYLFL IIFTVEAFLK VIAYGLLFHP NAYLRNGWNL
LDFIIVVVGL FSAILEQATK ADGANALGGK GAGFDVKALR AFRVLRPLRL VSGVPSLQVV
LNSIIKAMVP LLHIALLVLF VIIIYAIIGL ELFMGKMHKT CYNQEGIADV PAEDDPSPCA
LETGHGRQCQ NGTVCKPGWD GPKHGITNFD NFAFAMLTVF QCITMEGWTD VLYWVNDAVG
RDWPWIYFVT LIIIGSFFVL NLVLGVLSGE FSKEREKAKA RGDFQKLREK QQLEEDLKGY
LDWITQAEDI DPENEDEGMD EEKPRNMSMP TSETESVNTE NVAGGDIEGE NCGARLAHRI
SKSKFSRYWR RWNRFCRRKC RAAVKSNVFY WLVIFLVFLN TLTIASEHYN QPHWLTEVQD
TANKALLALF TAEMLLKMYS LGLQAYFVSL FNRFDCFVVC GGILETILVE TKIMSPLGIS
VLRCVRLLRI FKITRYWNSL SNLVASLLNS VRSIASLLLL LFLFIIIFSL LGMQLFGGKF
NFDEMQTRRS TFDNFPQSLL TVFQILTGED WNSVMYDGIM AYGGPSFPGM LVCIYFIILF
ICGNYILLNV FLAIAVDNLA DAESLTSAQK EEEEEKERKK LARTASPEKK QEMVEKPAVE
ESKEEKIELK SITADGESPP TTKINMDDLQ PNENEDKSPY PNPETTGEED EEEPEMPVGP
RPRPLSELHL KEKAVPMPEA SAFFIFSSNN RFRLQCHRIV NDTIFTNLIL FFILLSSISL
AAEDPVQHTS FRNHILGNAD YVFTSIFTLE IILKMTAYGA FLHKGSFCRN YFNILDLLVV
SVSLISFGIQ SSAINVVKIL RVLRVLRPLR AINRAKGLKH VVQCVFVAIR TIGNIVIVTT
LLQFMFACIG VQLFKGKLYT CSDSSKQTEA ECKGNYITYK DGEVDHPIIQ PRSWENSKFD
FDNVLAAMMA LFTVSTFEGW PELLYRSIDS HTEDKGPIYN YRVEISIFFI IYIIIIAFFM
MNIFVGFVIV TFQEQGEQEY KNCELDKNQR QCVEYALKAR PLRRYIPKNQ HQYKVWYVVN
STYFEYLMFV LILLNTICLA MQHYGQSCLF KIAMNILNML FTGLFTVEMI LKLIAFKPKG
YFSDPWNVFD FLIVIGSIID VILSETNHYF CDAWNTFDAL IVVGSIVDIA ITEVNNAEEN
SRISITFFRL FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL PYVALLIVML FFIYAVIGMQ
VFGKIALNDT TEINRNNNFQ TFPQAVLLLF RCATGEAWQD IMLACMPGKK CAPESEPGNS
TEGETPCGSS FAVFYFISFY MLCAFLIINL FVAVIMDNFD YLTRDWSILG PHHLDEFKRI
WAEYDPEAKG RIKHLDVVTL LRRIQPPLGF GKLCPHRVAC KRLVSMNMPL NSDGTVMFNA
TLFALVRTAL RIKTEGNLEQ ANEELRAIIK KIWKRTSMKL LDQVVPPAGD DEVTVGKFYA
TFLIQEYFRK FKKRKEQGLV GKPSQRNALS LQAGLRTLHD IGPEIRRAIS GDLTAEEELD
KAMKEAVSAA SEDDIFRRAG GLFGNHVSYY QSDGRSAFPQ TFTTQRPLHI NKAGSSQGDT
ESPSHEKLVD STFTPSSYSS TGSNANINNA NNTALGRLPR PAGYPSTVST VEGHGPPLSP
AIRVQEVAWK LSSKRCHSGE SQTAMVGPEE TSQDETYEVK MNHDAEACSE PSLLSTDMLS
YQDDENRQLT LPEEDKRDIR QSPKRGFLRS ASLGRRASFH LECLKRQKDR GGDISQKTVL
PLHLVHHQAL AVAGLSPLLQ RSHSPASFPR PFATPPATPG SRGWPPQPIP TLRLEGAESS
EKLNSSFPSI HCGSWAETTP GGGDSSTTRR ARPVSLMVPS QAGAPGRQFH GSASSLVEAV
LISEGLGQFA QDPKFIEVTT QELADACDMT IEEMESAADN ILSGGAPQSP NGALLPFVNC
RDAGQDRAGG EEDAGCARAR GRLSEEELQD SRVYVSSL
//
