Calpain small subunit 1 - Rattus norvegicus (Rat)

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Reviewed, UniProtKB/Swiss-Prot Q64537 (CPNS1_RAT)

Last modified June 16, 2009. Version 82. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Calpain small subunit 1
      Short name=CSS1
Alternative name(s):
    Calcium-dependent protease small subunit 1
    Calcium-dependent protease small subunit
      Short name=CDPS
    Calpain regulatory subunit
    Calcium-activated neutral proteinase small subunit
      Short name=CANP small subunit

Gene names

Name:	Capns1
Synonyms:	Capn4, Css1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length	270 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.
Cofactor	Calcium By similarity.
Subunit structure	Homodimer or heterodimer of a large (catalytic) and a small (regulatory) subunit. In presence of calcium, the heterodimer dissociates By similarity.
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.5
Miscellaneous	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.
Sequence similarities	Contains 5 EF-hand domains.

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Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
Domain	Repeat
Ligand	Calcium
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Ref.3 Inferred from mutant phenotype. Source: RGD
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Ref.3 Traceable author statement. Source: RGD calcium-dependent cysteine-type endopeptidase activity Ref.3 Inferred from mutant phenotype. Source: RGD protein heterodimerization activity Ref.3 Inferred from physical interaction. Source: RGD
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
Capn2	Q07009	1	EBI-918712,EBI-1040438

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 270

270

Calpain small subunit 1

PRO_0000073717

Regions

Domain

98 – 132

EF-hand 1; atypical

Domain

141 – 174

EF-hand 2

Domain

171 – 206

EF-hand 3

Domain

207 – 235

EF-hand 4

Domain

236 – 270

EF-hand 5

Calcium binding

Calcium binding

Calcium binding

Compositional bias

Gly-rich (hydrophobic)

Compositional bias

10 – 25

Poly-Gly

Compositional bias

37 – 58

Poly-Gly

Compositional bias

80 – 85

Poly-Pro

Experimental info

Sequence conflict

S → M in AAA64828. Ref.3

Secondary structure

270

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q64537-1 [UniParc].

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

270

28,570

        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

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References

	« Hide 'large scale' referencesShow '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: 15489334] [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: 8950173] [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: 7982961] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 87-270, PARTIAL PROTEIN SEQUENCE, COFACTOR, 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: 9228945] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 98-270, SUBUNIT, COFACTOR.
[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: 14579356] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 91-249, COFACTOR, 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: 15476820] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) OF 88-270, SUBUNIT.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

BC098068 mRNA. Translation: AAH98068.1.
U53859 mRNA. Translation: AAC53002.1.
U10861 mRNA. Translation: AAA64828.1.

IPI

IPI00213536.

PIR

A55143.

RefSeq

NP_058814.1.

UniGene

Rn.3430

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AJ5	X-ray	2.30	A/B	98-270	[»]
1DF0	X-ray	2.60	B	88-270	[»]
1DVI	X-ray	2.30	A/B	88-270	[»]
1NP8	X-ray	2.00	A/B	91-249	[»]
1U5I	X-ray	2.86	B	88-270	[»]
3BOW	X-ray	2.40	B	88-270	[»]
3DF0	X-ray	2.95	B	88-270	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6140N.

IntAct

Q64537. 2 interactions.

Proteomic databases

PRIDE

Q64537.

Genome annotation databases

Ensembl

ENSRNOG00000001503. Rattus norvegicus. [Contig view]

GeneID

29156.

KEGG

rno:29156.

Organism-specific databases

RGD

2270. Capns1.

Phylogenomic databases

HOVERGEN

Q64537.

Family and domain databases

InterPro

IPR018247. EF_HAND_1.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca_bd.
[Graphical view]

ProDom

PD000012. EF-hand. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00054. EFh. 3 hits.
[Graphical view]

PROSITE

PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

608179.

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Entry information

Entry name

CPNS1_RAT

Accession

Primary (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:	June 16, 2009
This is version 82 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other Resources

Entry information

Relevant documents