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Protein

Calpain small subunit 1

Gene

Capns1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi111Calcium 1; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi114Calcium 1Combined sources3 Publications1
Metal bindingi116Calcium 1; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi121Calcium 1Combined sources3 Publications1
Metal bindingi139Calcium 4Combined sources3 Publications1
Metal bindingi154Calcium 2Combined sources3 Publications1
Metal bindingi156Calcium 2Combined sources3 Publications1
Metal bindingi158Calcium 2; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi160Calcium 2; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi165Calcium 2Combined sources3 Publications1
Metal bindingi184Calcium 3Combined sources3 Publications1
Metal bindingi186Calcium 3Combined sources3 Publications1
Metal bindingi188Calcium 3; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi190Calcium 3; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi195Calcium 3Combined sources3 Publications1
Metal bindingi227Calcium 4Combined sources3 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi110 – 1211Combined sources3 PublicationsAdd BLAST12
Calcium bindingi154 – 1652Combined sources3 PublicationsAdd BLAST12
Calcium bindingi184 – 1953Combined sources3 PublicationsAdd BLAST12

GO - Molecular functioni

  • calcium ion binding Source: RGD
  • protein heterodimerization activity Source: RGD

GO - Biological processi

  • proteolysis Source: RGD
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.22.B24. 5301.

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
Proteomesi
  • UP000002494 Componenti: 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

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000737171 – 270Calpain small subunit 1Add BLAST270

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei6PhosphoserineBy similarity1
Modified residuei181N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ64537.
PRIDEiQ64537.

PTM databases

iPTMnetiQ64537.
PhosphoSitePlusiQ64537.

Expressioni

Gene expression databases

BgeeiENSRNOG00000045747.

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

GO - Molecular functioni

  • protein heterodimerization activity Source: RGD

Protein-protein interaction databases

DIPiDIP-6140N.
IntActiQ64537. 2 interactors.
MINTiMINT-112921.
STRINGi10116.ENSRNOP00000067513.

Structurei

Secondary structure

1270
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi98 – 111Combined sources14
Helixi112 – 114Combined sources3
Helixi119 – 132Combined sources14
Turni134 – 136Combined sources3
Helixi143 – 153Combined sources11
Beta strandi158 – 161Combined sources4
Helixi163 – 183Combined sources21
Beta strandi188 – 191Combined sources4
Turni193 – 195Combined sources3
Helixi196 – 202Combined sources7
Helixi209 – 219Combined sources11
Beta strandi224 – 226Combined sources3
Helixi228 – 243Combined sources16
Turni248 – 251Combined sources4
Beta strandi253 – 258Combined sources6
Helixi260 – 268Combined sources9

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ64537.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini98 – 132EF-hand 1; atypicalPROSITE-ProRule annotationAdd BLAST35
Domaini141 – 174EF-hand 2PROSITE-ProRule annotationAdd BLAST34
Domaini171 – 206EF-hand 3PROSITE-ProRule annotationAdd BLAST36
Domaini207 – 235EF-hand 4PROSITE-ProRule annotationAdd BLAST29
Domaini236 – 270EF-hand 5PROSITE-ProRule annotationAdd BLAST35

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1 – 66Gly-rich (hydrophobic)Add BLAST66
Compositional biasi10 – 25Poly-GlyAdd BLAST16
Compositional biasi37 – 58Poly-GlyAdd BLAST22
Compositional biasi80 – 85Poly-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.
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.
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.

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)DescriptionActionsGraphical viewLength
Sequence conflicti87S → M in AAA64828 (PubMed:7982961).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC098068 mRNA. Translation: AAH98068.1.
U53859 mRNA. Translation: AAC53002.1.
U10861 mRNA. Translation: AAA64828.1.
PIRiA55143.
RefSeqiNP_058814.1. NM_017118.1.
XP_017445520.1. XM_017590031.1.
UniGeneiRn.3430.

Genome annotation databases

GeneIDi100912380.
29156.
KEGGirno:29156.
UCSCiRGD:2270. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC098068 mRNA. Translation: AAH98068.1.
U53859 mRNA. Translation: AAC53002.1.
U10861 mRNA. Translation: AAA64828.1.
PIRiA55143.
RefSeqiNP_058814.1. NM_017118.1.
XP_017445520.1. XM_017590031.1.
UniGeneiRn.3430.

3D structure databases

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

Protein-protein interaction databases

DIPiDIP-6140N.
IntActiQ64537. 2 interactors.
MINTiMINT-112921.
STRINGi10116.ENSRNOP00000067513.

PTM databases

iPTMnetiQ64537.
PhosphoSitePlusiQ64537.

Proteomic databases

PaxDbiQ64537.
PRIDEiQ64537.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100912380.
29156.
KEGGirno:29156.
UCSCiRGD:2270. rat.

Organism-specific databases

CTDi826.
RGDi2270. Capns1.

Phylogenomic databases

eggNOGiKOG0037. Eukaryota.
ENOG410YKQK. LUCA.
HOGENOMiHOG000063658.
HOVERGENiHBG004492.
InParanoidiQ64537.
KOiK08583.
PhylomeDBiQ64537.

Enzyme and pathway databases

BRENDAi3.4.22.B24. 5301.

Miscellaneous databases

EvolutionaryTraceiQ64537.
PROiQ64537.

Gene expression databases

BgeeiENSRNOG00000045747.

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_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: November 30, 2016
This is version 142 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

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.