Q0PCR6

PTMD Annotation Information


※ Protein Information

Tag Content
UniProt Accession Q0PCR6_MOUSE; Q0PCR6;
Entrez ID 12288
GenBank Protein ID NM_001159533.2; NM_001159534.2; NM_001159535.2; NM_009781.4;
GenBank Nucleotide ID NP_001153005.1; NP_001153006.1; NP_001153007.1; NP_033911.2;
Protein Name Voltage-dependent L-type calcium channel subunit alpha
Gene Name Cacna1c; CaV1.2-a
Organism Mus musculus
NCBI Taxa ID 10090
Functional DescriptionVoltage-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
(Fasta)
MIRAFVQPST PPYQPLSSHS SEETERKFKG KVVHEAQLNC FYISPGGSNY GSPRPAHANM 60
NANAAAGLAP EHIPTPGAAL SWQAAIDAAR 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 MSPLGISVLR CVRLLRIFKI 660
TRYWNSLSNL VASLLNSVRS IASLLLLLFL FIIIFSLLGM QLFGGKFNFD EMQTRRSTFD 720
NFPQSLLTVF QILTGEDWNS VMYDGIMAYG GPSFPGMLVC IYFIILFICG NYILLNVFLA 780
IAVDNLADAE SLTSAQKEEE EEKERKKLAR TASPEKKQEV MEKPAVEESK EEKIELKSIT 840
ADGESPPTTK INMDDLQPSE NEDKSPHSNP DTAGEEDEEE PEMPVGPRPR PLSELHLKEK 900
AVPMPEASAF FIFSPNNRFR LQCHRIVNDT IFTNLILFFI LLSSISLAAE DPVQHTSFRN 960
HILGNADYVF TSIFTLEIIL KMTAYGAFLH KGSFCRNYFN ILDLLVVSVS LISFGIQSSA 1020
INVVKILRVL RVLRPLRAIN RAKGLKHVVQ CVFVAIRTIG NIVIVTTLLQ FMFACIGVQL 1080
FKGKLYTCSD SSKQTEAECK GNYITYKDGE VDHPIIQPRS WENSKFDFDN VLAAMMALFT 1140
VSTFEGWPEL LYRSIDSHTE DKGPIYNYRV EISIFFIIYI IIIAFFMMNI FVGFVIVTFQ 1200
EQGEQEYKNC ELDKNQRQCV EYALKARPLR RYIPKNQHQY KVWYVVNSTY FEYLMFVLIL 1260
LNTICLAMQH YGQSCLFKIA MNILNMLFTG LFTVEMILKL IAFKPKGYFS DPWNVFDFLI 1320
VIGSIIDVIL SETNPAEHTQ CSPSMSAEEN SRISITFFRL FRVMRLVKLL SRGEGIRTLL 1380
WTFIKSFQAL PYVALLIVML FFIYAVIGMQ VFGKIALNDT TEINRNNNFQ TFPQAVLLLF 1440
RCATGEAWQD IMLACMPGKK CAPESEPSNS TEGETPCGSS FAVFYFISFY MLCAFLIINL 1500
FVAVIMDNFD YLTRDWSILG PHHLDEFKRI WAEYDPEAKG RIKHLDVVTL LRRIQPPLGF 1560
GKLCPHRVAC KRLVSMNMPL NSDGTVMFNA TLFALVRTAL RIKTEGNLEQ ANEELRAIIK 1620
KIWKRTSMKL LDQVVPPAGD DEVTVGKFYA TFLIQEYFRK FKKRKEQGLV GKPSQRNALS 1680
LQAGLRTLHD IGPEIRRAIS GDLTAEEELD KAMKEAVSAA SEDDIFRRAG GLFGNHVTYY 1740
QSDSRGNFPQ TFATQRPLHI NKTGNNQADT ESPSHEKLVD STFTPSSYSS TGSNANINNA 1800
NNTALGRFPH PAGYSSTVST VEGHGPPLSP AVRVQEAAWK LSSKRCHSRE SQGATVNQEI 1860
FPDETRSVRM SEEAEYCSEP SLLSTDMFSY QEDEHRQLTC PEEDKREIQP SPKRSFLRSA 1920
SLGRRASFHL ECLKRQKDQG GDISQKTALP LHLVHHQALA VAGLSPLLQR SHSPTTFPRP 1980
CPTPPVTPGS RGRPLRPIPT LRLEGAESSE KLNSSFPSIH CSSWSEETTA CSGSSSMARR 2040
ARPVSLTVPS QAGAPGRQFH GSASSLVEAV LISEGLGQFA QDPKFIEVTT QELADACDMT 2100
IEEMENAADN ILSGGAQQSP NGTLLPFVNC RDPGQDRAVA PEDESCAYAL GRGRSEEALA 2160
DSRSYVSNL

※ PTM-Disease Association

NumPTMDiseaseCell TypeTypePTM SitePMID
1Threonine PhosphorylationHeart failurecell linesNT170427864509
[Reference]: Dual mutation of Ser1700 and a nearby casein-kinase II site (Thr1704) caused accelerated hypertrophy, heart failure, and death in mice with these mutations (STAA mice).
2Serine PhosphorylationDiabetes mellitusUS192828119464
[Reference]: Ser1928 phosphorylation by PKA stimulates the L-type Ca2+ channel CaV1.2 and vasoconstriction during acute hyperglycemia and diabetes.

※ Disease Cross-ref Annotation

DatabaseAnnotation
CTD (Curated)
(count: 9)
(view all)
MESH:D001145 ; Arrhythmias, Cardiac
MESH:D001321 ; Autistic Disorder
MESH:D001714 ; Bipolar Disorder
MESH:C567509 ; Brugada Syndrome 3
MESH:D006973 ; Hypertension
MESH:D007003 ; Hypoglycemia

※ PTM Sites

PTM Modification Sites
Phosphorylation
(count: 1)
9         IRAFVQPSTPPYQPL     dbPAF