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Protein

Calpain-1 catalytic subunit

Gene

CAPN1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.

Catalytic activityi

Broad endopeptidase specificity.

Cofactori

Ca2+By similarityNote: Binds 4 Ca2+ ions.By similarity

Enzyme regulationi

Activated by micromolar concentrations of calcium and inhibited by calpastatin.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei115By similarity1
Active sitei272By similarity1
Active sitei296By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi99 – 1061PROSITE-ProRule annotation8
Calcium bindingi302 – 3332PROSITE-ProRule annotationAdd BLAST32
Calcium bindingi598 – 6093PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi628 – 6394PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.22.52. 6170.
ReactomeiR-SSC-1474228. Degradation of the extracellular matrix.
R-SSC-6798695. Neutrophil degranulation.

Protein family/group databases

MEROPSiC02.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Calpain-1 catalytic subunit (EC:3.4.22.52)
Alternative name(s):
Calcium-activated neutral proteinase 1
Short name:
CANP 1
Calpain mu-type
Calpain-1 large subunit
Micromolar-calpain
Short name:
muCANP
Gene namesi
Name:CAPN1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 2

Subcellular locationi

  • Cytoplasm By similarity
  • Cell membrane By similarity

  • Note: Translocates to the plasma membrane upon Ca2+ binding.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4062.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002076972 – 714Calpain-1 catalytic subunitAdd BLAST713

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei354PhosphothreonineBy similarity1

Post-translational modificationi

Undergoes calcium-induced successive autoproteolytic cleavages that generate a membrane-bound 78 kDa active form and an intracellular 75 kDa active form. Calpastatin reduces with high efficiency the transition from 78 kDa to 75 kDa calpain forms (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei15 – 16Cleavage; for 78 kDa formBy similarity2
Sitei27 – 28Cleavage; for 75 kDa formBy similarity2

Keywords - PTMi

Autocatalytic cleavage, Phosphoprotein

Proteomic databases

PaxDbiP35750.
PeptideAtlasiP35750.
PRIDEiP35750.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSSSCG00000012999.
GenevisibleiP35750. SS.

Interactioni

Subunit structurei

Forms a heterodimer with a small (regulatory) subunit (CAPNS1).

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000013824.

Chemistry databases

BindingDBiP35750.

Structurei

3D structure databases

ProteinModelPortaliP35750.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini55 – 354Calpain catalyticPROSITE-ProRule annotationAdd BLAST300
Domaini585 – 618EF-hand 1PROSITE-ProRule annotationAdd BLAST34
Domaini615 – 650EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini680 – 714EF-hand 3PROSITE-ProRule annotationAdd BLAST35

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni355 – 526Domain IIIAdd BLAST172
Regioni527 – 542LinkerAdd BLAST16
Regioni543 – 713Domain IVAdd BLAST171

Sequence similaritiesi

Belongs to the peptidase C2 family.Curated
Contains 1 calpain catalytic domain.PROSITE-ProRule annotation
Contains 3 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0045. Eukaryota.
ENOG410XP0B. LUCA.
GeneTreeiENSGT00760000118971.
HOGENOMiHOG000232035.
HOVERGENiHBG012645.
InParanoidiP35750.
OMAiNYQGQMV.
OrthoDBiEOG091G049E.
TreeFamiTF314748.

Family and domain databases

CDDicd00214. Calpain_III. 1 hit.
cd00044. CysPc. 1 hit.
cd00051. EFh. 1 hit.
Gene3Di1.10.238.10. 1 hit.
InterProiIPR033883. C2_III.
IPR022684. Calpain_cysteine_protease.
IPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR029643. CAPN1.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000169. Pept_cys_AS.
IPR001300. Peptidase_C2_calpain_cat.
[Graphical view]
PANTHERiPTHR10183:SF284. PTHR10183:SF284. 1 hit.
PfamiPF01067. Calpain_III. 1 hit.
PF13833. EF-hand_8. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view]
PRINTSiPR00704. CALPAIN.
SMARTiSM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF49758. SSF49758. 1 hit.
PROSITEiPS50203. CALPAIN_CAT. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35750-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEEVITPVY CTGVSAQVQK LRAKELGLGR HENAIKYLGQ DYEQLRAHCL
60 70 80 90 100
QSGSLFRDEA FPPVPQSLGF KELGPNSSKT YGVKWKRPTE LFSNPQFIVD
110 120 130 140 150
GATRTDICQG ALGDCWLLAA IASLTLNDTL LHRVVPHGQS FQNGYAGIFH
160 170 180 190 200
FQLWQFGEWV DVVVDDLLPT KDGKLVFVHS AQGNEFWSAL LEKAYAKVNG
210 220 230 240 250
SYEALSGGST SEGFEDFTGG VTEWYELRKA PSDLYSIILK ALERGSLLGC
260 270 280 290 300
SIDISSVLDM EAVTFKKLVK GHAYSVTGAK QVNYQGQMVN LIRMRNPWGE
310 320 330 340 350
VEWTGAWSDG SSEWNGVDPY QRDQLRVRME DGEFWMSFRD FLREFTRLEI
360 370 380 390 400
CNLTPDALKS QRVRNWNTTL YEGTWRRGST AGGCRNYPAT FWVNPQFKIR
410 420 430 440 450
LEETDDPEDD YGGRESGCSF VLALMQKHRR RERRFGRDME TIGFAVYEVP
460 470 480 490 500
PELVGQPVHL KRDFFLANAS RARSEQFINL REVSTRFRLP PGEYVVVPST
510 520 530 540 550
FEPNKEGDFV LRFFSEKKAG TQELDDQVQA ILPDEQVLSE EEIDENFKAL
560 570 580 590 600
FRQLAGEDME ISVRELRTIL NRIISKHKDL RTKGFSLESC RSMVNLMDRD
610 620 630 640 650
GNGKLGLVEF NILWNRIRNY LSIFRKFDLD KSGSMSAYEM RMAIESAGFK
660 670 680 690 700
LNKKLFELII TRYSEPDLAV DFDNFVCCLV RLETMFRFFK TLDTDLDGVV
710
TFDLFKWLQL TMFA
Length:714
Mass (Da):81,739
Last modified:January 11, 2001 - v3
Checksum:i0BB31DE4FC56363A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti528V → I in AAA65125 (PubMed:8312396).Curated1
Sequence conflicti531I → N in AAA65125 (PubMed:8312396).Curated1
Sequence conflicti541E → G in AAA65125 (PubMed:8312396).Curated1
Sequence conflicti622S → A in AAA65125 (PubMed:8312396).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF263610 mRNA. Translation: AAF73444.1.
F14611 mRNA. Translation: CAA23154.1.
U01180 mRNA. Translation: AAA65125.1.
RefSeqiXP_005660758.1. XM_005660701.2.
XP_005660759.1. XM_005660702.2.
UniGeneiSsc.42541.

Genome annotation databases

EnsembliENSSSCT00000014210; ENSSSCP00000013824; ENSSSCG00000012999.
GeneIDi397027.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF263610 mRNA. Translation: AAF73444.1.
F14611 mRNA. Translation: CAA23154.1.
U01180 mRNA. Translation: AAA65125.1.
RefSeqiXP_005660758.1. XM_005660701.2.
XP_005660759.1. XM_005660702.2.
UniGeneiSsc.42541.

3D structure databases

ProteinModelPortaliP35750.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000013824.

Chemistry databases

BindingDBiP35750.
ChEMBLiCHEMBL4062.

Protein family/group databases

MEROPSiC02.001.

Proteomic databases

PaxDbiP35750.
PeptideAtlasiP35750.
PRIDEiP35750.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000014210; ENSSSCP00000013824; ENSSSCG00000012999.
GeneIDi397027.

Organism-specific databases

CTDi823.

Phylogenomic databases

eggNOGiKOG0045. Eukaryota.
ENOG410XP0B. LUCA.
GeneTreeiENSGT00760000118971.
HOGENOMiHOG000232035.
HOVERGENiHBG012645.
InParanoidiP35750.
OMAiNYQGQMV.
OrthoDBiEOG091G049E.
TreeFamiTF314748.

Enzyme and pathway databases

BRENDAi3.4.22.52. 6170.
ReactomeiR-SSC-1474228. Degradation of the extracellular matrix.
R-SSC-6798695. Neutrophil degranulation.

Miscellaneous databases

PROiP35750.

Gene expression databases

BgeeiENSSSCG00000012999.
GenevisibleiP35750. SS.

Family and domain databases

CDDicd00214. Calpain_III. 1 hit.
cd00044. CysPc. 1 hit.
cd00051. EFh. 1 hit.
Gene3Di1.10.238.10. 1 hit.
InterProiIPR033883. C2_III.
IPR022684. Calpain_cysteine_protease.
IPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR029643. CAPN1.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000169. Pept_cys_AS.
IPR001300. Peptidase_C2_calpain_cat.
[Graphical view]
PANTHERiPTHR10183:SF284. PTHR10183:SF284. 1 hit.
PfamiPF01067. Calpain_III. 1 hit.
PF13833. EF-hand_8. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view]
PRINTSiPR00704. CALPAIN.
SMARTiSM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF49758. SSF49758. 1 hit.
PROSITEiPS50203. CALPAIN_CAT. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCAN1_PIG
AccessioniPrimary (citable) accession number: P35750
Secondary accession number(s): Q29600, Q9N0M6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 11, 2001
Last modified: November 30, 2016
This is version 147 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

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  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.