ID A0A287AWB1_PIG Unreviewed; 1977 AA.
AC A0A287AWB1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN Name=CACNA1F {ECO:0000313|Ensembl:ENSSSCP00000048418.2,
GN ECO:0000313|VGNC:VGNC:111741};
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:ENSSSCP00000048418.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000048418.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000048418.2,
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:ENSSSCP00000048418.2}
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: 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 STRING; 9823.ENSSSCP00000048418; -.
DR PaxDb; 9823-ENSSSCP00000021269; -.
DR Ensembl; ENSSSCT00000013447.5; ENSSSCP00000048418.2; ENSSSCG00000012298.6.
DR VGNC; VGNC:111741; CACNA1F.
DR GeneTree; ENSGT00940000159855; -.
DR InParanoid; A0A287AWB1; -.
DR Proteomes; UP000008227; Chromosome X.
DR Bgee; ENSSSCG00000012298; Expressed in epididymis and 7 other cell types or tissues.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:Ensembl.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IBA:GO_Central.
DR GO; GO:0008332; F:low voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070509; P:calcium ion import; IBA:GO_Central.
DR GO; GO:0050908; P:detection of light stimulus involved in visual perception; IEA:Ensembl.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
DR GO; GO:0035725; P:sodium ion transmembrane transport; 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; 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:SF2; VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1F; 1.
DR Pfam; PF08763; Ca_chan_IQ; 1.
DR Pfam; PF16885; CAC1F_C; 1.
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 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:UP000008227};
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 96..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 315..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 348..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 529..547
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 562..580
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 658..677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 727..749
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 871..889
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 909..929
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 941..967
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 987..1016
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1112..1137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1190..1211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1223..1242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1325..1343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1416..1440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1574..1608
FT /note="Voltage-dependent calcium channel alpha-1 subunit
FT IQ"
FT /evidence="ECO:0000259|SMART:SM01062"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1634..1776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..781
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..825
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1638..1657
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1664..1678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1702..1716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1737..1751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-1"
FT BINDING 710
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 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602077-3"
SQ SEQUENCE 1977 AA; 219961 MW; 19513602C50A31BB CRC64;
MSASEGGKDT TPEPSPANGT GPGPEWGLCP GPPATGGEIG GASGPGTPKR RTQHSKHKTV
AVASAQRSPR ALFCLTLANP LRRSCISIVE WKPFDILILL TIFANCVALG VYIPFPEDDS
NTANHNLEQV EYVFLVIFTV ETVLKIVAYG LVLHPSAYIR NGWNLLDFII VVVGLFSVLL
EQGSGRPDAP HTGGKPGGFD VKALRAFRVL RPLRLVSGVP SLHIVLNSIM KALVPLLHIA
LLVLFVIIIY AIIGLELFLG RMHKTCYFLG SDVEAEEDPS PCASSGSGRA CTLNQTECRG
RWAGPNGGIT NFDNFFFAML TVFQCITMEG WTDVLYWMQD AMGYELPWVY FVSLVIFGSF
FVLNLVLGVL SGEFSKEREK AKARGDFQKL REKQQLEEDL RGYLDWITQA EELDVDDPSA
DGNFGSVAEE GRAGHRPQLA ELISRRRGRL RWFSHSTRST HSTSSHASLP ASDTGSMAET
PGDEEEEEGP LASCTRCLNK IMKTRVCRRL RRANRGLRAS CRRAVKSTAC YWAVLLLVFL
NTLTIASEHH GQPVWLTQIQ EYANKVLLCL FTVEMLLKLY GLGPSVYVSS FFNRFDCFVV
CGGILETTLV EVGAMQPLGI SVLRCVRLLR IFKVTRHWAS LSNLVASLLN SMKSIASLLL
LLFLFIIIFS LLGMQLFGGK FNFDQTHTKR STFDTFPQAL LTVFQILTGE DWNVVMYDGI
MAYGGPFFPG MLVCVYFIIL FICGNYILLN VFLAIAVDNL ASGDAGTDKD KGREKSTEET
PKENGALVPG GENEEEEGAK NEGAGMEEEE EEEEEEEEEE EEEGGAGHVE LLQEVVPKEK
VVPIPEGSAF FCLSQTNPLR KACHTLIHHH VFTNLILVFI ILSSVSLAAE DPIRAHSFRN
HILGYFDYAF TSIFTVEILL KMTVFGAFLH RGSFCRSWFN LLDLLVVSVS LISFGIHSSA
ISVVKILRVL RVLRPLRAIN RAKGLKHVVQ CVFVAIRTIG NIMIVTTLLQ FMFACIGVQL
FKGKFYSCTD EAKHTPQECK GSFLVYPDGD VSRPLVRERL WVNSDFNFDN VLSAMMALFT
VSTFEGWPAL LYKAIDAHAE DKGPIYNYHV EISVFFIVYI IIIAFFMMNI FVGFVIITFR
AQGEQEYQDC ELDKNQRQCV EYALKAQPLR RYIPKNPHQY RVWASVNSAA FEYLMFLLIL
LNTVALAMQH YEQTAPFNYA MDILNMVFTG LFTVEMVLKI IAFKPKHYFT DAWNTFDALI
VVGSVVDIAV TEVNNGGHLG ESSEDSSRIS ITFFRLFRVM RLVKLLSKGE GIRTLLWTFI
KSFQALPYVA LLIAMIFFIY AVIGMQMFGK VALQDGTQIN RNNNFQTFPQ AVLLLFRCAT
GEAWQEIMLA SLPGSRCDPE SDYGPGEEFS CGSNFAIAYF ISFFMLCAFL IINLFVAVIM
DNFDYLTRDW SILGPHHLDE FKRIWSEYDP GAKGRIKHLD VVALLRRIQP PLGFGKLCPH
RVACKRLVAM NMPLNSDGTV TFNATLFALV RTSLKIKTEG NLEQANQELR IVIKKIWKRM
KQKLLDEVIP PADEEEVTVG KFYATFLIQD YFRKFRRRKE KGLLGTEAPP STSSALQAGL
RSLQDLGPEI RQALTCDTDE EEGEEGREGE EEEEEKDPET YKASVGSQPP SRRSSVISVS
LPAGDKPPDS LSLGPSDDDG GALNSRQPSV PQAGSHAHRR SSGVLIFTIP EEESSQPKGS
KGQEKQDEQE EVPSQLSYLD EQAGTPPRPI LVPPHRPQRY MDGHQAPRRR LLPPTPAGRK
PSFTIQCLRR QGSCEDLPIP GTYYRGRNSG PSRAQGSWAT PPQRGRLLYA PLLLVEEGAA
GEGYLGKSSG PLRTFTCLPV PGTHPDPGHG KRGSADSLVE AVLISEGLGL FARDPRFVAL
AKQEIADACR LTLDEMDSAA SDLLAQGTSS LYSDEESILS RFDEEDLGDE MACVHAL
//
