CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010985
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Voltage-dependent L-type calcium channel subunit alpha-1S 
Protein Synonyms/Alias
 Calcium channel, L type, alpha-1 polypeptide, isoform 3, skeletal muscle; Voltage-gated calcium channel subunit alpha Cav1.1 
Gene Name
 Cacna1s 
Gene Synonyms/Alias
 Cach1; Cach1b; Cacn1; Cacnl1a3 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
719EGIPTTAKLKIDEFEubiquitination[1]
769AELQLKEKAVPIPEAubiquitination[1]
1083YKNCELDKNQRQCVQubiquitination[1]
1414AEYDPEAKGRIKHLDubiquitination[1]
1550YYGYRPKKDTVQIQAubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
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-1S 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-1S subunit play an important role in excitation-contraction coupling in skeletal muscle. 
Sequence Annotation
 REPEAT 38 337 I.
 REPEAT 418 664 II.
 REPEAT 768 1068 III.
 REPEAT 1105 1384 IV.
 REGION 357 374 Binding to the beta subunit (By
 REGION 988 1077 Dihydropyridine binding (By similarity).
 REGION 1337 1403 Dihydropyridine binding (By similarity).
 REGION 1349 1392 Phenylalkylamine binding (By similarity).
 MOD_RES 687 687 Phosphoserine; by PKA (By similarity).
 MOD_RES 1392 1392 Phosphoserine; by PKA (Potential).
 MOD_RES 1617 1617 Phosphoserine (By similarity).
 CARBOHYD 79 79 N-linked (GlcNAc...) (Potential).
 CARBOHYD 257 257 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1141 1141 N-linked (GlcNAc...) (Potential).  
Keyword
 Alternative splicing; Calcium; Calcium channel; Calcium transport; 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
 1880 AA 
Protein Sequence
MEPPSPQDEG LRKKQPKKPV PEILPRPPRA LFCLTLQNPL RKACISIVEW KPFETIILLT 60
IFANCVALAV YLPMPEDDNN TLNLGLEKLE YFFLIVFSIE AAMKIIAYGF LFHQDAYLRS 120
GWNVLDFIIV FLGVFTVILE QVNIIQTNTA PMSSKGAGLD VKALRAFRVL RPLRLVSGVP 180
SLQVVLNSIF KAMLPLFHIA LLVLFMVIIY AIIGLELFKG KMHKTCYFIG TDIVATVENE 240
KPSPCARTGS GRPCTINGSE CRGGWPGPNH GITHFDNFGF SMLTVYQCIS MEGWTDVLYW 300
VNDAIGNEWP WIYFVTLILL GSFFILNLVL GVLSGEFTKE REKAKSRGTF QKLREKQQLE 360
EDLRGYMSWI TQGEVMDVDD LREGKLSLDE GGSDTESLYE IEGLNKIIQF IRHWRQWNRV 420
FRWKCHDLVK SKVFYWLVIL IVALNTLSIA SEHHNQPLWL THLQDVANRV LLTLFTIEML 480
MKMYGLGLRQ YFMSIFNRFD CFVVCSGILE ILLVESGAMS PLGISVLRCI RLLRLFKITK 540
YWTSLSNLVA SLLNSIRSIA SLLLLLFLFI IIFALLGMQL FGGRYDFEDT EVRRSNFDNF 600
PQALISVFQV LTGEDWNSVM YNGIMAYGGP TYPGVLVCIY FIILFVCGNY ILLNVFLAIA 660
VDNLAEAESL TSAQKAKAEE RKRRKMSKGL PDKSEEERAT VTKKLEQKSK GEGIPTTAKL 720
KIDEFESNVN EVKDPYPSAD FPGDDEEDEP EIPVSPRPRP LAELQLKEKA VPIPEASSFF 780
IFSPTNKIRV LCHRIVNATW FTNFILLFIL LSSAALAAED PIRADSMRNQ ILEYFDYVFT 840
AVFTVEIVLK MTTYGAFLHK GSFCRNYFNI LDLLVVAVSL ISMGLESSAI SVVKILRVLR 900
VLRPLRAINR AKGLKHVVQC VFVAIRTIGN IVLVTTLLQF MFACIGVQLF KGKFYSCNDL 960
SKMTEEECRG YYYIYKDGDP TQIELRPRQW IHNDFHFDNV LSAMMSLFTV STFEGWPQLL 1020
YKAIDSNEED TGPVYNNRVE MAIFFIIYII LIAFFMMNIF VGFVIVTFQE QGETEYKNCE 1080
LDKNQRQCVQ YALKARPLRC YIPKNPYQYQ VWYVVTSSYF EYLMFALIML NTICLGMQHY 1140
NQSEQMNHIS DILNVAFTII FTLEMVLKLI AFKPRAYFGD PWNVFDFLIV IGSIIDVILS 1200
EIDTFLASSG GLYCLGGGCG NVDPDESARI SSAFFRLFRV MRLVKLLNRA EGVRTLLWTF 1260
IKSFQALPYV ALLIVMLFFI YAVIGMQMFG KIAMVDGTQI NRNNNFQTFP QAVLLLFRCA 1320
TGEAWQEILL ACSYGKLCDP ESDYAPGEEH TCGTNFAYYY FISFYMLCAF LIINLFVAVI 1380
MDNFDYLTRD WSILGPHHLD EFKAIWAEYD PEAKGRIKHL DVVTLLRRIQ PPLGFGKFCP 1440
HRVACKRLVG MNMPLNSDGT VTFNATLFAL VRTALKIKTE GNFEQANEEL RAIIKKIWKR 1500
TSMKLLDQVI PPIGDDEVTV GKFYATFLIQ EHFRKFMKRQ EEYYGYRPKK DTVQIQAGLR 1560
TIEEEAAPEI HRAISGDPTA EEELERAMVE AAMEEGIFRR TGGLFGQVDN FLERTNSLPP 1620
VMANQRPLQF AEIEMEELES PVFLEDFPQN PGTHPLARAN TNNANANVAY GNSSHRNNPV 1680
FSSICYEREF LGEADMPVTR EGPLSQPCSG SGPHSRSHVD KLKRPMTQRG MPEGQVPPSP 1740
CQLSQAEHPV QKEGKGPTSR FLETPNSRNF EEHVPRNSAH RCTAPATAML IQEALVRGGL 1800
DSLAADANFV MATGQALADA CQMEPEEVEV AATELLKQES PEAGPCLGAL SLRSSPGPPE 1860
SDDWGSQTTL ITPRCEAYTE 1880 
Gene Ontology
 GO:0016529; C:sarcoplasmic reticulum; IDA:MGI.
 GO:0030315; C:T-tubule; IDA:MGI.
 GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0005245; F:voltage-gated calcium channel activity; IDA:MGI.
 GO:0007029; P:endoplasmic reticulum organization; IMP:MGI.
 GO:0002074; P:extraocular skeletal muscle development; IMP:MGI.
 GO:0007520; P:myoblast fusion; IMP:MGI.
 GO:0007528; P:neuromuscular junction development; IMP:MGI.
 GO:0043501; P:skeletal muscle adaptation; IMP:MGI.
 GO:0001501; P:skeletal system development; IMP:MGI.
 GO:0006941; P:striated muscle contraction; IMP:MGI. 
Interpro
 IPR005821; Ion_trans_dom.
 IPR027359; K_channel_four-helix_dom.
 IPR014873; VDCC_a1su_IQ.
 IPR005450; VDCC_L_a1ssu.
 IPR005446; VDCC_L_a1su.
 IPR002077; VDCCAlpha1. 
Pfam
 PF08763; Ca_chan_IQ
 PF00520; Ion_trans 
SMART
 SM01062; Ca_chan_IQ 
PROSITE
  
PRINTS
 PR00167; CACHANNEL.
 PR01630; LVDCCALPHA1.
 PR01634; LVDCCALPHA1S.