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Q64537

- CPNS1_RAT

UniProt

Q64537 - CPNS1_RAT

Protein

Calpain small subunit 1

Gene

Capns1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 3 (06 Dec 2005)
      Previous versions | rss
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    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

    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-SubCell

    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

    MFLVNSFLKG GGGGGGGGGL GGGLGNVLGG LISGAAGGGG GGGGGGGMGL    50
    GGGGGGGGTA MRILGGVISA ISEAAAQYNP EPPPPRSHYS NIEANESEEE 100
    RQFRKLFVQL AGDDMEVSAT ELMNILNKVV TRHPDLKTDG FGIDTCRSMV 150
    AVMDSDTTGK LGFEEFKYLW NNIKKWQGIY KRFDTDRSGT IGSNELPGAF 200
    EAAGFHLNQH IYSMIIRRYS DETGNMDFDN FISCLVRLDA MFRAFRSLDK 250
    NGTGQIQVNI QEWLQLTMYS 270
    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

    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 1, 2014
    This is version 120 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