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Q64537

- CPNS1_RAT

UniProt

Q64537 - CPNS1_RAT

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Protein

Calpain small subunit 1

Gene

Capns1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi111 – 1111Calcium 1; via carbonyl oxygen
Metal bindingi114 – 1141Calcium 1
Metal bindingi116 – 1161Calcium 1; via carbonyl oxygen
Metal bindingi121 – 1211Calcium 1
Metal bindingi139 – 1391Calcium 4
Metal bindingi154 – 1541Calcium 2
Metal bindingi156 – 1561Calcium 2
Metal bindingi158 – 1581Calcium 2; via carbonyl oxygen
Metal bindingi160 – 1601Calcium 2; via carbonyl oxygen
Metal bindingi165 – 1651Calcium 2
Metal bindingi184 – 1841Calcium 3
Metal bindingi186 – 1861Calcium 3
Metal bindingi188 – 1881Calcium 3; via carbonyl oxygen
Metal bindingi190 – 1901Calcium 3; via carbonyl oxygen
Metal bindingi195 – 1951Calcium 3
Metal bindingi227 – 2271Calcium 4

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi110 – 121121Add
BLAST
Calcium bindingi154 – 165122Add
BLAST
Calcium bindingi184 – 195123Add
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: RGD
  2. protein heterodimerization activity Source: RGD

GO - Biological processi

  1. proteolysis Source: RGD
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_199178. Degradation of the extracellular matrix.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Capns1
Synonyms:Capn4, Css1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2270. Capns1.

Subcellular locationi

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.By similarity

GO - Cellular componenti

  1. cytoplasm Source: RefGenome
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 270270Calpain small subunit 1PRO_0000073717Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei181 – 1811N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ64537.
PRIDEiQ64537.

Expressioni

Gene expression databases

GenevestigatoriQ64537.

Interactioni

Subunit structurei

Homodimer or heterodimer of a large (catalytic) and a small (regulatory) subunit. In presence of calcium, the heterodimer dissociates (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-6140N.
IntActiQ64537. 2 interactions.
MINTiMINT-112921.

Structurei

Secondary structure

1
270
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi98 – 11114
Helixi112 – 1143
Helixi119 – 13214
Turni134 – 1363
Helixi143 – 15311
Beta strandi158 – 1614
Helixi163 – 18321
Beta strandi188 – 1914
Turni193 – 1953
Helixi196 – 2027
Helixi209 – 21911
Beta strandi224 – 2263
Helixi228 – 24316
Turni248 – 2514
Beta strandi253 – 2586
Helixi260 – 2689

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ64537.
SMRiQ64537. Positions 95-270.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ64537.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini98 – 13235EF-hand 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Domaini141 – 17434EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini171 – 20636EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini207 – 23529EF-hand 4PROSITE-ProRule annotationAdd
BLAST
Domaini236 – 27035EF-hand 5PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 6666Gly-rich (hydrophobic)Add
BLAST
Compositional biasi10 – 2516Poly-GlyAdd
BLAST
Compositional biasi37 – 5822Poly-GlyAdd
BLAST
Compositional biasi80 – 856Poly-Pro

Domaini

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.
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 similaritiesi

Contains 5 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG277774.
HOGENOMiHOG000063658.
HOVERGENiHBG004492.
InParanoidiQ64537.
KOiK08583.
PhylomeDBiQ64537.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR029642. CAPN4.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PANTHERiPTHR10183:SF38. PTHR10183:SF38. 1 hit.
PfamiPF13202. EF-hand_5. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q64537-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFLVNSFLKG GGGGGGGGGL GGGLGNVLGG LISGAAGGGG GGGGGGGMGL
60 70 80 90 100
GGGGGGGGTA MRILGGVISA ISEAAAQYNP EPPPPRSHYS NIEANESEEE
110 120 130 140 150
RQFRKLFVQL AGDDMEVSAT ELMNILNKVV TRHPDLKTDG FGIDTCRSMV
160 170 180 190 200
AVMDSDTTGK LGFEEFKYLW NNIKKWQGIY KRFDTDRSGT IGSNELPGAF
210 220 230 240 250
EAAGFHLNQH IYSMIIRRYS DETGNMDFDN FISCLVRLDA MFRAFRSLDK
260 270
NGTGQIQVNI QEWLQLTMYS
Length:270
Mass (Da):28,570
Last modified:December 6, 2005 - v3
Checksum:i63609614CD4D3EB7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871S → M in AAA64828. (PubMed:7982961)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC098068 mRNA. Translation: AAH98068.1.
U53859 mRNA. Translation: AAC53002.1.
U10861 mRNA. Translation: AAA64828.1.
PIRiA55143.
RefSeqiNP_058814.1. NM_017118.1.
UniGeneiRn.3430.

Genome annotation databases

GeneIDi29156.
KEGGirno:29156.
UCSCiRGD:2270. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC098068 mRNA. Translation: AAH98068.1 .
U53859 mRNA. Translation: AAC53002.1 .
U10861 mRNA. Translation: AAA64828.1 .
PIRi A55143.
RefSeqi NP_058814.1. NM_017118.1.
UniGenei Rn.3430.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 87-270 [» ]
ProteinModelPortali Q64537.
SMRi Q64537. Positions 95-270.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6140N.
IntActi Q64537. 2 interactions.
MINTi MINT-112921.

Chemistry

BindingDBi Q64537.

Proteomic databases

PaxDbi Q64537.
PRIDEi Q64537.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 29156.
KEGGi rno:29156.
UCSCi RGD:2270. rat.

Organism-specific databases

CTDi 826.
RGDi 2270. Capns1.

Phylogenomic databases

eggNOGi NOG277774.
HOGENOMi HOG000063658.
HOVERGENi HBG004492.
InParanoidi Q64537.
KOi K08583.
PhylomeDBi Q64537.

Enzyme and pathway databases

Reactomei REACT_199178. Degradation of the extracellular matrix.

Miscellaneous databases

EvolutionaryTracei Q64537.
NextBioi 608179.
PROi Q64537.

Gene expression databases

Genevestigatori Q64537.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
InterProi IPR029642. CAPN4.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view ]
PANTHERi PTHR10183:SF38. PTHR10183:SF38. 1 hit.
Pfami PF13202. EF-hand_5. 1 hit.
[Graphical view ]
SMARTi SM00054. EFh. 3 hits.
[Graphical view ]
PROSITEi PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiCPNS1_RAT
AccessioniPrimary (citable) accession number: Q64537
Secondary accession number(s): P97572, Q4V795
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 6, 2005
Last modified: October 29, 2014
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3