| Tag | Content |
|---|
| CPLM ID | CPLM-005032 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Voltage-dependent L-type calcium channel subunit alpha-1C |
Protein Synonyms/Alias | Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle; Rat brain class C; RBC; Voltage-gated calcium channel subunit alpha Cav1.2 |
Gene Name | Cacna1c |
Gene Synonyms/Alias | Cach2; Cacn2; Cacnl1a1; Cchl1a1 |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 93 | IDAARQAKLMGSAGN | ubiquitination | [1] |
|
Reference | [1] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis. Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J. J Proteome Res. 2012 Sep 7;11(9):4722-32. [ PMID: 22871113] |
Functional Description | Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1C gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin- GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing the alpha-1C subunit play an important role in excitation-contraction coupling in the heart. Binding of calmodulin or CABP1 at the same regulatory sites results in an opposit effects on the channel function. |
Sequence Annotation | REPEAT 141 438 I.
REPEAT 540 786 II.
REPEAT 917 1198 III.
REPEAT 1235 1508 IV.
REGION 458 475 Binding to the beta subunit (By
REGION 1118 1208 Dihydropyridine binding (By similarity).
REGION 1459 1527 Dihydropyridine binding (By similarity).
REGION 1473 1516 Phenylalkylamine binding (By similarity).
MOD_RES 845 845 Phosphoserine (By similarity).
MOD_RES 1516 1516 Phosphoserine; by PKA (Potential).
MOD_RES 1919 1919 Phosphoserine; by PKA (Potential).
MOD_RES 1927 1927 Phosphoserine; by PKA (Potential).
CARBOHYD 183 183 N-linked (GlcNAc...) (Potential).
CARBOHYD 358 358 N-linked (GlcNAc...) (Potential).
CARBOHYD 1417 1417 N-linked (GlcNAc...) (Potential).
CARBOHYD 1468 1468 N-linked (GlcNAc...) (Potential). |
Keyword | 3D-structure; Alternative splicing; Calcium; Calcium channel; Calcium transport; Cell membrane; Complete proteome; Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport; Voltage-gated channel. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 2169 AA |
Protein Sequence | MIRAFAQPST PPYQPLSSCL SEDTERKFKG KVVHEAQLNC FYISPGGSNY GSPRPAHANM 60
NANAAAGLAP EHIPTPGAAL SWLAAIDAAR QAKLMGSAGN ATISTVSSTQ RKRQQYGKPK 120
KQGGTTATRP PRALLCLTLK NPIRRACISI VEWKPFEIII LLTIFANCVA LAIYIPFPED 180
DSNATNSNLE RVEYLFLIIF TVEAFLKVIA YGLLFHPNAY LRNGWNLLDF IIVVVGLFSA 240
ILEQATKADG ANALGGKGAG FDVKALRAFR VLRPLRLVSG VPSLQVVLNS IIKAMVPLLH 300
IALLVLFVII IYAIIGLELF MGKMHKTCYN QEGIIDVPAE EDPSPCALET GHGRQCQNGT 360
VCKPGWDGPK HGITNFDNFA FAMLTVFQCI TMEGWTDVLY WMQDAMGYEL PWVYFVSLVI 420
FGSFFVLNLV LGVLSGEFSK EREKAKARGD FQKLREKQQL EEDLKGYLDW ITQAEDIDPE 480
NEDEGMDEDK PRNMSMPTSE TESVNTENVA GGDIEGENCG ARLAHRISKS KFSRYWRRWN 540
RFCRRKCRAA VKSNVFYWLV IFLVFLNTLT IASEHYNQPH WLTEVQDTAN KALLALFTAE 600
MLLKMYSLGL QAYFVSLFNR FDCFIVCGGI LETILVETKI MSPLGISCWR CVRLLRIFKI 660
TRYWNSLSNL VASLLNSLRS IASLLLLLFL FIIIFSLLGM QLFGGKFNFD EMQTRRSTFD 720
NFPQSLLTVF QILTGEDWNS VMYDGIMAYG GPSFPGMLVC IYFIILFISP NYILLNLFLA 780
IAVDNLADAE SLTSAQKEEE EEKERKKLAR TASPEKKQEV MEKPAVEESK EEKIELKSIT 840
ADGESPPTTK INMDDLQPSE NEDKSPHSNP DTAGEEDEEE PEMPVGPRPR PLSELHLKEK 900
AVPMPEASAF FIFSPNNRFR LQCHRIVNDT IFTNLILFFI LLSSISLAAE DPVQHTSFRN 960
HILFYFDIVF TTIFTIEIAL KMTAYGAFLH KGSFCRNYFN ILDLLVVSVS LISFGIQSSA 1020
INVVKILRVL RVLRPLRINR AKGLKHVVQC VFVAIRTIGN IVIVTTLLQF MFACIGVQLF 1080
KGKLYTCSDS SKQTEAESKG NYITYKTGEV DHPIIQPRSW ENSKFDFDNV LAAMMALFTV 1140
STFEGWPELL YRSIDSHTED KGPIYNYRVE ISIFFIIYII IIAFFMMNIF VGFVIVTFQE 1200
QGEQEYKNCE LDKNQRQCVE YALKARPLPR YIPKNQHQYK VWYVVNSTYF EYLMFVLILL 1260
NTICLAMQHY GQSCLFKIAM NILNMLFTGL FTVEMILKLI AFKPKHYFCD AWNTFDALIV 1320
VGSIVDIAIT EVHPAEHTQC SPSMSAEENS RISITFFRLF RVMRLVKLLS RGEGIRTLLW 1380
TFIKSFQALP YVALLIVMLF FIYAVIGMQV FGKIALNDTT EINRNNNFQT FPQAVLLLFR 1440
CATGEAWQDI MLACMPGKKC APESEPSNST EGETPCGSSF AVFYFISFYM LCAFLIINLF 1500
VAVIMDNFDY LTRDWSILGP HHLDEFKRIW AEYDPEAKGR IKHLDVVTLL RRIQPPLGFG 1560
KLCPHRVACK RLVSMNMPLN SDGTVMFNAT LFALVRTALR IKTEGNLEQA NEELRAIIKK 1620
IWKRTSMKLL DQVVPPAGDD EVTVGKFYAT FLIQEYFRKF KKRKEQGLVG KPSQRNALSL 1680
QAGLRTLHDI GPEIRRAISG DLTAEEELDK AMKEAVSAAS EDDIFRRAGG LFGNHVSYYQ 1740
SDSRSNFPQT FATQRPLHIN KTGNNQADTE SPSHEKLVDS TFTPSSYSST GSNANINNAN 1800
NTALGRFPHP AGYSSTVSTV EGHGPPLSPA VRVQEAAWKL SSKRCHSRES QGATVSQDMF 1860
PDETRSSVRL SEEVEYCSEP SLLSTDILSY QDDENRQLTC LEEDKREIQP CPKRSFLRSA 1920
SLGRRASFHL ECLKRQKDQG GDISQKTALP LHLVHHQALA VAGLSPLLQR SHSPSTFPRP 1980
RPTPPVTPGS RGRPLQPIPT LRLEGAESSE KLNSSFPSIH CSSWSEETTA CSGGSSMARR 2040
ARPVSLTVPS QAGAPGRQFH GSASSLVEAV LISEGLGQFA QDPKFIEVTT QELADACDMT 2100
IEEMENAADN ILSGGAQQSP NGTLLPFVNC RDPGQDRAVV PEDESCVYAL GRGRSEEALP 2160
DSRSYVSNL 2169 |
Gene Ontology | |
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