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Protein

Calpain small subunit 1

Gene

CAPNS1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 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 bindingi107 – 1071Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi110 – 1101Calcium 1By similarity
Metal bindingi112 – 1121Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi117 – 1171Calcium 1By similarity
Metal bindingi135 – 1351Calcium 4By similarity
Metal bindingi150 – 1501Calcium 2By similarity
Metal bindingi152 – 1521Calcium 2By similarity
Metal bindingi154 – 1541Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi156 – 1561Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi161 – 1611Calcium 2By similarity
Metal bindingi180 – 1801Calcium 3By similarity
Metal bindingi182 – 1821Calcium 3By similarity
Metal bindingi184 – 1841Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi186 – 1861Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi191 – 1911Calcium 3By similarity
Metal bindingi223 – 2231Calcium 4By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi106 – 117121By similarityAdd
BLAST
Calcium bindingi150 – 161122By similarityAdd
BLAST
Calcium bindingi180 – 191123By similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.22.B24. 6170.
ReactomeiR-SSC-1474228. 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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 6

Subcellular locationi

  • Cytoplasm By similarity
  • Cell membrane By similarity

  • Note: Translocates to the plasma membrane upon calcium binding.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2205.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 266266Calpain small subunit 1PRO_0000073715Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei177 – 1771N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP04574.
PRIDEiP04574.

Expressioni

Gene expression databases

GenevisibleiP04574. SS.

Interactioni

Subunit structurei

Homodimer or heterodimer of a large (catalytic) and a small (regulatory) subunit. In presence of calcium, the heterodimer dissociates.1 Publication

Protein-protein interaction databases

IntActiP04574. 1 interaction.
STRINGi9823.ENSSSCP00000025968.

Chemistry

BindingDBiP04574.

Structurei

Secondary structure

1
266
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi95 – 10713Combined sources
Turni108 – 1114Combined sources
Helixi115 – 12713Combined sources
Helixi139 – 14911Combined sources
Beta strandi154 – 1574Combined sources
Helixi159 – 17921Combined sources
Beta strandi185 – 1884Combined sources
Turni189 – 1913Combined sources
Helixi192 – 1987Combined sources
Helixi205 – 21511Combined sources
Beta strandi220 – 2223Combined sources
Helixi224 – 24421Combined sources
Beta strandi245 – 2473Combined sources
Beta strandi250 – 2556Combined sources
Helixi256 – 2649Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ALVX-ray1.90A/B94-266[»]
1ALWX-ray2.03A/B94-266[»]
1NX0X-ray2.30A/B94-266[»]
1NX1X-ray2.00A/B94-266[»]
1NX2X-ray2.20A94-266[»]
1NX3X-ray2.45A94-266[»]
4PHNX-ray1.79A/B94-266[»]
ProteinModelPortaliP04574.
SMRiP04574. Positions 94-266.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04574.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini94 – 12835EF-hand 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Domaini137 – 17034EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini167 – 20236EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini203 – 23129EF-hand 4PROSITE-ProRule annotationAdd
BLAST
Domaini232 – 26635EF-hand 5PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 6767Gly-rich (hydrophobic)Add
BLAST
Compositional biasi10 – 2617Poly-GlyAdd
BLAST
Compositional biasi35 – 5420Poly-GlyAdd
BLAST
Compositional biasi76 – 816Poly-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

eggNOGiKOG0037. Eukaryota.
ENOG410YKQK. LUCA.
GeneTreeiENSGT00620000087734.
HOVERGENiHBG004492.
InParanoidiP04574.
KOiK08583.
OMAiGCLGGPH.
OrthoDBiEOG7RV9FM.
TreeFamiTF314682.

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.
PfamiPF13833. EF-hand_8. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04574-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLVNSFLKG GGGGGGGGGG LGGGLGNVLG GLISGAGGGG GGGGGGGGGG
60 70 80 90 100
GGGGTAMRIL GGVISAISEA AAQYNPEPPP PRTHYSNIEA NESEEVRQFR
110 120 130 140 150
RLFAQLAGDD MEVSATELMN ILNKVVTRHP DLKTDGFGID TCRSMVAVMD
160 170 180 190 200
SDTTGKLGFE EFKYLWNNIK KWQAIYKQFD VDRSGTIGSS ELPGAFEAAG
210 220 230 240 250
FHLNEHLYSM IIRRYSDEGG NMDFDNFISC LVRLDAMFRA FKSLDKDGTG
260
QIQVNIQEWL QLTMYS
Length:266
Mass (Da):28,068
Last modified:August 13, 1987 - v1
Checksum:i3FA81023EDC4141A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11778 mRNA. Translation: AAA31010.1.
M11779 mRNA. Translation: AAA31011.1.
AJ410870 Genomic DNA. Translation: CAC85483.2.
PIRiA25166. CIPGL.
S39392.
RefSeqiNP_999483.1. NM_214318.2.
UniGeneiSsc.54048.

Genome annotation databases

EnsembliENSSSCT00000031590; ENSSSCP00000025968; ENSSSCG00000030149.
GeneIDi397587.
KEGGissc:397587.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11778 mRNA. Translation: AAA31010.1.
M11779 mRNA. Translation: AAA31011.1.
AJ410870 Genomic DNA. Translation: CAC85483.2.
PIRiA25166. CIPGL.
S39392.
RefSeqiNP_999483.1. NM_214318.2.
UniGeneiSsc.54048.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ALVX-ray1.90A/B94-266[»]
1ALWX-ray2.03A/B94-266[»]
1NX0X-ray2.30A/B94-266[»]
1NX1X-ray2.00A/B94-266[»]
1NX2X-ray2.20A94-266[»]
1NX3X-ray2.45A94-266[»]
4PHNX-ray1.79A/B94-266[»]
ProteinModelPortaliP04574.
SMRiP04574. Positions 94-266.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP04574. 1 interaction.
STRINGi9823.ENSSSCP00000025968.

Chemistry

BindingDBiP04574.
ChEMBLiCHEMBL2205.

Proteomic databases

PaxDbiP04574.
PRIDEiP04574.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000031590; ENSSSCP00000025968; ENSSSCG00000030149.
GeneIDi397587.
KEGGissc:397587.

Organism-specific databases

CTDi826.

Phylogenomic databases

eggNOGiKOG0037. Eukaryota.
ENOG410YKQK. LUCA.
GeneTreeiENSGT00620000087734.
HOVERGENiHBG004492.
InParanoidiP04574.
KOiK08583.
OMAiGCLGGPH.
OrthoDBiEOG7RV9FM.
TreeFamiTF314682.

Enzyme and pathway databases

BRENDAi3.4.22.B24. 6170.
ReactomeiR-SSC-1474228. Degradation of the extracellular matrix.

Miscellaneous databases

EvolutionaryTraceiP04574.

Gene expression databases

GenevisibleiP04574. SS.

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.
PfamiPF13833. EF-hand_8. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A putative Ca2+-binding protein: structure of the light subunit of porcine calpain elucidated by molecular cloning and protein sequence analysis."
    Sakihama T., Kakidani H., Zenita K., Yumoto N., Kikuchi T., Sasaki T., Kannagi R., Nakanishi S., Ohmori M., Takio K., Titani K., Murachi T.
    Proc. Natl. Acad. Sci. U.S.A. 82:6075-6079(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Leeb T.
    Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Crystal structure of calcium bound domain VI of calpain at 1.9-A resolution and its role in enzyme assembly, regulation, and inhibitor binding."
    Lin G.D., Chattopadhyay D., Maki M., Wang K.K., Carson M., Jin L., Yuen P.W., Takano E., Hatanaka M., Delucas L.J., Narayana S.V.
    Nat. Struct. Biol. 4:539-547(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 94-266, DOMAIN, CALCIUM-BINDING SITES.
  4. "A structural model for the inhibition of calpain by calpastatin: crystal structures of the native domain VI of calpain and its complexes with calpastatin peptide and a small molecule inhibitor."
    Todd B., Moore D., Deivanayagam C.C., Lin G.D., Chattopadhyay D., Maki M., Wang K.K., Narayana S.V.
    J. Mol. Biol. 328:131-146(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 94-266 IN COMPLEX WITH INHIBITOR, DOMAIN, CALCIUM-BINDING SITES.

Entry informationi

Entry nameiCPNS1_PIG
AccessioniPrimary (citable) accession number: P04574
Secondary accession number(s): Q8SPJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: June 8, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.