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Database: UniProt
Entry: I3LM43_PIG
LinkDB: I3LM43_PIG
Original site: I3LM43_PIG 
ID   I3LM43_PIG              Unreviewed;      2046 AA.
AC   I3LM43;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   23-MAY-2018, entry version 46.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha {ECO:0000256|RuleBase:RU003808};
GN   Name=CACNA1C {ECO:0000313|Ensembl:ENSSSCP00000025163};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000025163, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000025163, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000025163};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000025163}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAY-2012) to UniProtKB.
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the
CC       entry of calcium ions into excitable cells and are also involved
CC       in a variety of calcium-dependent processes, including muscle
CC       contraction, hormone or neurotransmitter release, gene expression,
CC       cell motility, cell division and cell death. The isoform alpha-1C
CC       gives rise to L-type calcium currents. Long-lasting (L-type)
CC       calcium channels belong to the 'high-voltage activated' (HVA)
CC       group. They are blocked by dihydropyridines (DHP),
CC       phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA
CC       (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-
CC       GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA).
CC       Calcium channels containing the alpha-1C subunit play an important
CC       role in excitation-contraction coupling in the heart. Binding of
CC       calmodulin or CABP1 at the same regulatory sites results in
CC       opposite effects on the channel function.
CC       {ECO:0000256|RuleBase:RU003808}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU003808};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU003808}.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family. {ECO:0000256|RuleBase:RU003808}.
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DR   EMBL; AEMK02000037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 9823.ENSSSCP00000025163; -.
DR   PaxDb; I3LM43; -.
DR   PRIDE; I3LM43; -.
DR   Ensembl; ENSSSCT00000030429; ENSSSCP00000025163; ENSSSCG00000027725.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   GeneTree; ENSGT00830000128247; -.
DR   InParanoid; I3LM43; -.
DR   OrthoDB; EOG091G0TKO; -.
DR   Reactome; R-SSC-422356; Regulation of insulin secretion.
DR   Reactome; R-SSC-5576892; Phase 0 - rapid depolarisation.
DR   Reactome; R-SSC-5576893; Phase 2 - plateau phase.
DR   Proteomes; UP000008227; Chromosome 5.
DR   Bgee; ENSSSCG00000027725; -.
DR   ExpressionAtlas; I3LM43; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IBA:GO_Central.
DR   GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.350; -; 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   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   PRINTS; PR01635; LVDCCALPHA1C.
DR   SMART; SM01062; Ca_chan_IQ; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|RuleBase:RU003808};
KW   Calcium channel {ECO:0000256|RuleBase:RU003808};
KW   Calcium transport {ECO:0000256|RuleBase:RU003808};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008227};
KW   Ion channel {ECO:0000256|RuleBase:RU003808};
KW   Ion transport {ECO:0000256|RuleBase:RU003808};
KW   Membrane {ECO:0000256|SAAS:SAAS00085096, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00084820,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00084701,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU003808};
KW   Voltage-gated channel {ECO:0000256|RuleBase:RU003808}.
FT   TRANSMEM     79     98       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    110    127       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    183    205       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    264    285       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    297    319       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    440    457       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    477    495       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    566    588       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    642    668       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    810    829       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    841    863       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    883    906       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    927    960       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1052   1078       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1129   1150       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1162   1182       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1268   1286       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM   1362   1385       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN     1519   1553       Ca_chan_IQ. {ECO:0000259|SMART:SM01062}.
FT   COILED      671    697       {ECO:0000256|SAM:Coils}.
FT   COILED     1480   1500       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   2046 AA;  229220 MW;  04E131B383B9155A CRC64;
     MDAEQGSRKS GVPAFPSPFP EGRREAVLRA QVERPQAVNP SNAHGATIVA PWAEMEPDDG
     ASLCWAQAWQ LGELLGLEYL FLIIFTVEAF LKVIAYGLLF HPNAYLRNGW NLLDFIIVVV
     GLFSAILEQA TKADGANALG GKGAGFDVKA LRAFRVLRPL RLVSGVPSLQ VVLNSIIKAM
     VPLLHIALLV LFVIIIYAII GLELFMGKMH KTCYNQEGVP DVPAEDDPSP CALETGHGRQ
     CQNGTVCKPG WDGPKHGITN FDNFAFAMLT VFQCITMEGW TDVLYWMQDA MGYELPWVYF
     VSLVIFGSFF VLNLVLGVLS GEFSKEREKA KARGDFQKLR EKQQLEEDLK GYLDWITQAE
     DIDPENEDEG MDEEKPRNMS MPTSETESVN TENVAGGDIE GESCGARLAH RISKSKFSRY
     WRRWNRFCRR KCRAAVKSSI FYWLVIFLVF LNTLTIASEH YNQPRWLTEV QDTANKALLA
     LFTAEMLLKM YSLGLQAYFV SLFNRFDCFI VCGGILETIL VETKVMSPLG ISVLRCVRLL
     RIFKITRYWN SLSNLVASLL NSVRSIASLL LLLFLFIIIF SLLGMQLFGG KFNFDEMQTR
     RSTFDNFPQS LLTVFQILTG EDWNSVMYDG IMAYGGPSFP GMLVCIYFII LFICGNYILL
     NVFLAIAVDN LADAESLTSA QKEEEEEKER KKLARTASPE KKQEVVEKPA EKIELKSITA
     DGESPPATKI NMDDLQPNEN EDKCSYPNPE TAGEEDEEEP EMPVGPRPRP LSELHLKEKA
     VPMPEASAFF IFSPNNRFRL QCHRIVNDSI FTNLILFFIL LSSISLAAED PVQHTSFRNH
     ILFYFDIVFT TIFTIEIALK MTAYGAFLHK GSFCRNYFNI LDLLVVAVSL ISFGIQSSAI
     NVVKILRVLR VLRPLRAINR AKGLKHVVQC VFVAIRTIGN IVIVTTLLQF MFACIGVQLF
     KGKLYTCSDS SKQTEAECKG NYITYKDGEV DHPIIQPRSW ENSKFDFDNV LAAMMALFTV
     STFEGWPELL YRSIDSHTED KGPIYNYRVE ISVFFIIYII IIAFFMMNIF VGFVIVTFQE
     QGEQEYKNCE LDKNQRQCVE YALKARPLRR YIPKNQHQYK VWYVVNSTYF EYLMFVLILL
     NTICLAMQHY GQSCLFKVAM NVLNMLFTGL FTVEMILKLI AFKPKHYFCD AWNTFDALIV
     VGSIVDIAIT EVNPAEHTQC SPFMNAEENS 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
//
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