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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)DescriptionActionsGraphical viewLength
Metal bindingi107Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi110Calcium 1By similarity1
Metal bindingi112Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi117Calcium 1By similarity1
Metal bindingi135Calcium 4By similarity1
Metal bindingi150Calcium 2By similarity1
Metal bindingi152Calcium 2By similarity1
Metal bindingi154Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi156Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi161Calcium 2By similarity1
Metal bindingi180Calcium 3By similarity1
Metal bindingi182Calcium 3By similarity1
Metal bindingi184Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi186Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi191Calcium 3By similarity1
Metal bindingi223Calcium 4By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi106 – 1171By similarityAdd BLAST12
Calcium bindingi150 – 1612By similarityAdd BLAST12
Calcium bindingi180 – 1913By similarityAdd BLAST12

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 databases

ChEMBLiCHEMBL2205.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000737151 – 266Calpain small subunit 1Add BLAST266

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei6PhosphoserineBy similarity1
Modified residuei177N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP04574.
PeptideAtlasiP04574.
PRIDEiP04574.

Expressioni

Gene expression databases

BgeeiENSSSCG00000030149.
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 interactor.
STRINGi9823.ENSSSCP00000025968.

Chemistry databases

BindingDBiP04574.

Structurei

Secondary structure

1266
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi95 – 107Combined sources13
Turni108 – 111Combined sources4
Helixi115 – 127Combined sources13
Helixi139 – 149Combined sources11
Beta strandi154 – 157Combined sources4
Helixi159 – 179Combined sources21
Beta strandi185 – 188Combined sources4
Turni189 – 191Combined sources3
Helixi192 – 198Combined sources7
Helixi205 – 215Combined sources11
Beta strandi220 – 222Combined sources3
Helixi224 – 244Combined sources21
Beta strandi245 – 247Combined sources3
Beta strandi250 – 255Combined sources6
Helixi256 – 264Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04574.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini94 – 128EF-hand 1; atypicalPROSITE-ProRule annotationAdd BLAST35
Domaini137 – 170EF-hand 2PROSITE-ProRule annotationAdd BLAST34
Domaini167 – 202EF-hand 3PROSITE-ProRule annotationAdd BLAST36
Domaini203 – 231EF-hand 4PROSITE-ProRule annotationAdd BLAST29
Domaini232 – 266EF-hand 5PROSITE-ProRule annotationAdd BLAST35

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1 – 67Gly-rich (hydrophobic)Add BLAST67
Compositional biasi10 – 26Poly-GlyAdd BLAST17
Compositional biasi35 – 54Poly-GlyAdd BLAST20
Compositional biasi76 – 81Poly-Pro6

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.
OrthoDBiEOG091G0ISY.
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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP04574. 1 interactor.
STRINGi9823.ENSSSCP00000025968.

Chemistry databases

BindingDBiP04574.
ChEMBLiCHEMBL2205.

Proteomic databases

PaxDbiP04574.
PeptideAtlasiP04574.
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.
OrthoDBiEOG091G0ISY.
TreeFamiTF314682.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP04574.

Gene expression databases

BgeeiENSSSCG00000030149.
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...

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: November 2, 2016
This is version 136 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.