Tag | Content |
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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 |
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719 | EGIPTTAKLKIDEFE | ubiquitination | [1] | 769 | AELQLKEKAVPIPEA | ubiquitination | [1] | 1083 | YKNCELDKNQRQCVQ | ubiquitination | [1] | 1414 | AEYDPEAKGRIKHLD | ubiquitination | [1] | 1550 | YYGYRPKKDTVQIQA | ubiquitination | [1] |
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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. |
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Pfam | |
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PRINTS | |