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Q64537 (CPNS1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calpain small subunit 1

Short name=CSS1
Alternative name(s):
Calcium-activated neutral proteinase small subunit
Short name=CANP small subunit
Calcium-dependent protease small subunit
Short name=CDPS
Calcium-dependent protease small subunit 1
Calpain regulatory subunit
Gene names
Name:Capns1
Synonyms:Capn4, Css1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length270 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulatory subunit of the calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.

Subunit structure

Homodimer or heterodimer of a large (catalytic) and a small (regulatory) subunit. In presence of calcium, the heterodimer dissociates By similarity. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Subcellular location

Cytoplasm. Cell membrane. Note: Translocates to the plasma membrane upon calcium binding By similarity. Allows the formation of the homodimer and also appears to mediate the contact between the large catalytic subunit and small regulatory subunit for the formation of the heterodimer.

Domain

The contact of the 5th EF-hand domain from each monomer allows the formation of the homodimer and also appears to mediate the contact between the large catalytic subunit and small regulatory subunit for the formation of the heterodimer. Ref.3 Ref.4 Ref.5

EF-hand domains are paired. EF-hand 1 is paired with EF-hand 2 and EF-hand 3 is paired with EF-hand 4. The fifth EF-hand domain, left unpaired, does not bind the calcium but is responsible of the dimerization by EF-embrace. The first four EF-hand domains bind calcium, however it is not sure if the binding of EF-hand 4 to calcium is physiologically relevant. Ref.3 Ref.4 Ref.5

Sequence similarities

Contains 5 EF-hand domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 270270Calpain small subunit 1
PRO_0000073717

Regions

Domain98 – 13235EF-hand 1; atypical
Domain141 – 17434EF-hand 2
Domain171 – 20636EF-hand 3
Domain207 – 23529EF-hand 4
Domain236 – 27035EF-hand 5
Calcium binding110 – 121121 Ref.7 Ref.8
Calcium binding154 – 165122 Ref.7 Ref.8
Calcium binding184 – 195123 Ref.7 Ref.8
Compositional bias1 – 6666Gly-rich (hydrophobic)
Compositional bias10 – 2516Poly-Gly
Compositional bias37 – 5822Poly-Gly
Compositional bias80 – 856Poly-Pro

Sites

Metal binding1111Calcium 1; via carbonyl oxygen
Metal binding1141Calcium 1
Metal binding1161Calcium 1; via carbonyl oxygen
Metal binding1211Calcium 1
Metal binding1391Calcium 4
Metal binding1541Calcium 2
Metal binding1561Calcium 2
Metal binding1581Calcium 2; via carbonyl oxygen
Metal binding1601Calcium 2; via carbonyl oxygen
Metal binding1651Calcium 2
Metal binding1841Calcium 3
Metal binding1861Calcium 3
Metal binding1881Calcium 3; via carbonyl oxygen
Metal binding1901Calcium 3; via carbonyl oxygen
Metal binding1951Calcium 3
Metal binding2271Calcium 4

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue1811N6-acetyllysine By similarity

Experimental info

Sequence conflict871S → M in AAA64828. Ref.3

Secondary structure

............................... 270
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q64537 [UniParc].

Last modified December 6, 2005. Version 3.
Checksum: 63609614CD4D3EB7

FASTA27028,570
        10         20         30         40         50         60 
MFLVNSFLKG GGGGGGGGGL GGGLGNVLGG LISGAAGGGG GGGGGGGMGL GGGGGGGGTA 

        70         80         90        100        110        120 
MRILGGVISA ISEAAAQYNP EPPPPRSHYS NIEANESEEE RQFRKLFVQL AGDDMEVSAT 

       130        140        150        160        170        180 
ELMNILNKVV TRHPDLKTDG FGIDTCRSMV AVMDSDTTGK LGFEEFKYLW NNIKKWQGIY 

       190        200        210        220        230        240 
KRFDTDRSGT IGSNELPGAF EAAGFHLNQH IYSMIIRRYS DETGNMDFDN FISCLVRLDA 

       250        260        270 
MFRAFRSLDK NGTGQIQVNI QEWLQLTMYS 

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[2]"Primary sequences of rat mu-calpain large and small subunits are, respectively, moderately and highly similar to those of human."
Sorimachi H., Amano S., Ishiura S., Suzuki K.
Biochim. Biophys. Acta 1309:37-41(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-270.
[3]"Active recombinant rat calpain II. Bacterially produced large and small subunits associate both in vivo and in vitro."
Graham-Siegenthaler K., Gauthier S., Davies P.L., Elce J.S.
J. Biol. Chem. 269:30457-30460(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 87-270, PARTIAL PROTEIN SEQUENCE, DOMAIN, SUBUNIT, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 84-266.
[4]"Structure of a calpain Ca(2+)-binding domain reveals a novel EF-hand and Ca(2+)-induced conformational changes."
Blanchard H., Grochulski P., Li Y., Arthur J.S.C., Davies P.L., Elce J.S., Cygler M.
Nat. Struct. Biol. 4:532-538(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 98-270, SUBUNIT, DOMAIN.
[5]"A second binding site revealed by C-terminal truncation of calpain small subunit, a penta-EF-hand protein."
Leinala E.K., Arthur J.S., Grochulski P., Davies P.L., Elce J.S., Jia Z.
Proteins 53:649-655(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 91-249, DOMAIN, SUBUNIT.
[6]"Activation of calpain by Ca2+: roles of the large subunit N-terminal and domain III-IV linker peptides."
Hosfield C.M., Elce J.S., Jia Z.
J. Mol. Biol. 343:1049-1053(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) OF 88-270, SUBUNIT.
[7]"Calcium-bound structure of calpain and its mechanism of inhibition by calpastatin."
Hanna R.A., Campbell R.L., Davies P.L.
Nature 456:409-412(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 88-270 IN COMPLEX WITH CAPN2 AND CALPASTATIN, CALCIUM-BINDING SITES, SUBUNIT.
[8]"Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains."
Moldoveanu T., Gehring K., Green D.R.
Nature 456:404-408(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 88-270 IN COMPLEX WITH CAPN2 AND CALPASTATIN, CALCIUM-BINDING SITES, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC098068 mRNA. Translation: AAH98068.1.
U53859 mRNA. Translation: AAC53002.1.
U10861 mRNA. Translation: AAA64828.1.
PIRA55143.
RefSeqNP_058814.1. NM_017118.1.
UniGeneRn.3430.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJ5X-ray2.30A/B98-270[»]
1DF0X-ray2.60B88-270[»]
1DVIX-ray2.30A/B88-270[»]
1NP8X-ray2.00A/B91-249[»]
1U5IX-ray2.86B88-270[»]
3BOWX-ray2.40B88-270[»]
3DF0X-ray2.95B87-270[»]
ProteinModelPortalQ64537.
SMRQ64537. Positions 95-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-6140N.
IntActQ64537. 2 interactions.
MINTMINT-112921.

Chemistry

BindingDBQ64537.

Proteomic databases

PaxDbQ64537.
PRIDEQ64537.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID29156.
KEGGrno:29156.
UCSCRGD:2270. rat.

Organism-specific databases

CTD826.
RGD2270. Capns1.

Phylogenomic databases

eggNOGNOG277774.
HOGENOMHOG000063658.
HOVERGENHBG004492.
InParanoidQ64537.
KOK08583.
PhylomeDBQ64537.

Gene expression databases

GenevestigatorQ64537.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamPF13202. EF-hand_5. 1 hit.
[Graphical view]
SMARTSM00054. EFh. 3 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ64537.
NextBio608179.
PROQ64537.

Entry information

Entry nameCPNS1_RAT
AccessionPrimary (citable) accession number: Q64537
Secondary accession number(s): P97572, Q4V795
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 6, 2005
Last modified: July 9, 2014
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references