logo CaMPDB: Calpain for Modulatory Proteolysis Database

SB0149 : Calpastatin

[ CaMP Format ]

* Basic Information

OrganismHomo sapiens (human)
Protein Namescalpastatin isoform m [Homo sapiens]; calpastatin isoform m; calpain inhibitor; sperm BS-17 component
Gene NamesCAST; calpastatin
Gene Locus5q15; chromosome 5
GO FunctionNot available
Entrez Protein Entrez Nucleotide Entrez Gene UniProt OMIM HGNC HPRD KEGG
NP_001177371 NM_001190442 831 N/A 114090 HGNC:1515 N/A N/A

* Information From OMIM

Description: Calpastatin is an endogenous inhibitor of calpains (see OMIM:114170) consisting of 4 inhibitory repeats, each of which neutralizes an activated calpain. Unlike proteinases, it is an intrinsically unstructured protein, adopting a defined structure only upon binding to active calpain (Moldoveanu et al., 2008; Hanna et al., 2008).

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* Structure Information

1. Primary Information

Length: 695 aa

Average Mass: 75.304 kDa

Monoisotopic Mass: 75.259 kDa

2. Domain Information

Annotated Domains: Not Available.

Computationally Assigned Domains (Pfam+HMMER):

domain namebeginendscoree-value
Calpain inhibitor 1. 328722.016.2
--- cleavage 195 ---
--- cleavage 203 ---
--- cleavage 209 ---
--- cleavage 210 ---
Maf N-terminal region 1. 21322423.00.0
--- cleavage 228 ---
--- cleavage 253 ---
--- cleavage 256 ---
Maf N-terminal region 2. 41742425.00.1
SlyX 1. 55460315.00.7
Calpain inhibitor 2. 62567853.05.1

3. Sequence Information

Fasta Sequence: SB0149.fasta

Amino Acid Sequence and Secondary Structures (PsiPred):

4. 3D Information

Not Available.

* Cleavage Information

7 [sites] cleaved by Calpain 3

Source Reference: [PubMed ID: 14594950] Ono Y, Kakinuma K, Torii F, Irie A, Nakagawa K, Labeit S, Abe K, Suzuki K, Sorimachi H, Possible regulation of the conventional calpain system by skeletal muscle-specific calpain, p94/calpain 3. J Biol Chem. 2004 Jan 23;279(4):2761-71. Epub 2003 Nov 1.

Cleavage sites (±10aa)

[Site 1] MSSTYIEELG195-KREVTIPPKY

Gly195 Lys

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Met186Ser187Ser188Thr189Tyr190Ile191Glu192Glu193Leu194Gly195
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Lys196Arg197Glu198Val199Thr200Ile201Pro202Pro203Lys204Tyr205

Sequence conservation (by blast)

[Site 2] LGKREVTIPP203-KYRELLAKPI

Pro203 Lys

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Leu194Gly195Lys196Arg197Glu198Val199Thr200Ile201Pro202Pro203
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Lys204Tyr205Arg206Glu207Leu208Leu209Ala210Lys211Pro212Ile213

Sequence conservation (by blast)

[Site 3] TIPPKYRELL209-AKPIGPDDAI

Leu209 Ala

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Thr200Ile201Pro202Pro203Lys204Tyr205Arg206Glu207Leu208Leu209
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Ala210Lys211Pro212Ile213Gly214Pro215Asp216Asp217Ala218Ile219

Sequence conservation (by blast)

[Site 4] IPPKYRELLA210-KPIGPDDAID

Ala210 Lys

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Ile201Pro202Pro203Lys204Tyr205Arg206Glu207Leu208Leu209Ala210
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Lys211Pro212Ile213Gly214Pro215Asp216Asp217Ala218Ile219Asp220

Sequence conservation (by blast)

[Site 5] IDALSSDFTC228-GSPTAAGKKT

Cys228 Gly

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Ile219Asp220Ala221Leu222Ser223Ser224Asp225Phe226Thr227Cys228
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Gly229Ser230Pro231Thr232Ala233Ala234Gly235Lys236Lys237Thr238

Sequence conservation (by blast)

[Site 6] TEVLKAQSAG253-TVRSAAPPQE

Gly253 Thr

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Thr244Glu245Val246Leu247Lys248Ala249Gln250Ser251Ala252Gly253
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Thr254Val255Arg256Ser257Ala258Ala259Pro260Pro261Gln262Glu263

Sequence conservation (by blast)

[Site 7] LKAQSAGTVR256-SAAPPQEKKR

Arg256 Ser

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
Leu247Lys248Ala249Gln250Ser251Ala252Gly253Thr254Val255Arg256
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'
Ser257Ala258Ala259Pro260Pro261Gln262Glu263Lys264Lys265Arg266

Sequence conservation (by blast)

* References

[PubMed ID: 24462690] Sun W, Feng R, Hu H, Guo F, Gao Q, Shao D, Yin D, Wang H, Sun X, Zhao M, Minobe E, Sun Y, Jiao G, Kameyama M, Hao L, The Ca(2+)-dependent interaction of calpastatin domain L with the C-terminal tail of the Cav1.2 channel. FEBS Lett. 2014 Mar 3;588(5):665-71. doi: 10.1016/j.febslet.2014.01.019. Epub

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