Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Sitei15 – 162Cleavage; for 78 kDa formBy similarity
Sitei27 – 282Cleavage; for 75 kDa formBy similarity
Active sitei115 – 1151By similarity
Active sitei272 – 2721By similarity
Active sitei296 – 2961By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi99 – 10681PROSITE-ProRule annotation
Calcium bindingi302 – 333322PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi598 – 609123PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi628 – 639124PROSITE-ProRule annotationAdd
BLAST

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.
ReactomeiREACT_279430. Degradation of the extracellular matrix.

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
ProteomesiUP000008227 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 714713Calpain-1 catalytic subunitPRO_0000207697Add
BLAST

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

Keywords - PTMi

Autocatalytic cleavage

Proteomic databases

PaxDbiP35750.
PRIDEiP35750.

Expressioni

Tissue specificityi

Ubiquitous.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000013824.

Structurei

3D structure databases

ProteinModelPortaliP35750.
SMRiP35750. Positions 13-713.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 354300Calpain catalyticPROSITE-ProRule annotationAdd
BLAST
Domaini585 – 61834EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini615 – 65036EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini680 – 71435EF-hand 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni355 – 526172Domain IIIAdd
BLAST
Regioni527 – 54216LinkerAdd
BLAST
Regioni543 – 713171Domain IVAdd
BLAST

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

eggNOGiNOG327523.
GeneTreeiENSGT00760000118971.
HOGENOMiHOG000232035.
HOVERGENiHBG012645.
InParanoidiP35750.
OMAiNYQGQMV.
OrthoDBiEOG7RV9FM.
TreeFamiTF314748.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR022684. 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.
PF13405. EF-hand_6. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view]
PRINTSiPR00704. CALPAIN.
SMARTiSM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
SM00054. EFh. 3 hits.
[Graphical view]
SUPFAMiSSF49758. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti528 – 5281V → I in AAA65125 (PubMed:8312396).Curated
Sequence conflicti531 – 5311I → N in AAA65125 (PubMed:8312396).Curated
Sequence conflicti541 – 5411E → G in AAA65125 (PubMed:8312396).Curated
Sequence conflicti622 – 6221S → A in AAA65125 (PubMed:8312396).Curated

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_005660701.1.
XP_005660759.1. XM_005660702.1.
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_005660701.1.
XP_005660759.1. XM_005660702.1.
UniGeneiSsc.42541.

3D structure databases

ProteinModelPortaliP35750.
SMRiP35750. Positions 13-713.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000013824.

Chemistry

BindingDBiP35750.
ChEMBLiCHEMBL4062.

Protein family/group databases

MEROPSiC02.001.

Proteomic databases

PaxDbiP35750.
PRIDEiP35750.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000014210; ENSSSCP00000013824; ENSSSCG00000012999.
GeneIDi397027.

Organism-specific databases

CTDi823.

Phylogenomic databases

eggNOGiNOG327523.
GeneTreeiENSGT00760000118971.
HOGENOMiHOG000232035.
HOVERGENiHBG012645.
InParanoidiP35750.
OMAiNYQGQMV.
OrthoDBiEOG7RV9FM.
TreeFamiTF314748.

Enzyme and pathway databases

BRENDAi3.4.22.52. 6170.
ReactomeiREACT_279430. Degradation of the extracellular matrix.

Miscellaneous databases

PROiP35750.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR022684. 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.
PF13405. EF-hand_6. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view]
PRINTSiPR00704. CALPAIN.
SMARTiSM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
SM00054. EFh. 3 hits.
[Graphical view]
SUPFAMiSSF49758. 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...

Publicationsi

« Hide 'large scale' publications
  1. "Rapid communication: nucleotide sequences of two isoforms of porcine micromolar calcium-activated neutral protease 1 cDNA."
    Smith T.P.L., Simmen F.A., Zhao G., Vallet J.L.
    J. Anim. Sci. 79:552-553(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Evaluation and characterization of a porcine small intestine cDNA library: analysis of 839 clones."
    Winteroe A.K., Fredholm M., Davies W.
    Mamm. Genome 7:509-517(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 326-415.
    Tissue: Small intestine.
  3. "Cloning the partial cDNAs of mu-calpain and m-calpain from porcine skeletal muscle."
    Sun W., Ji S.Q., Ebert P.J., Bidwell C.A., Hancock D.L.
    Biochimie 75:931-936(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 528-623.
    Tissue: Skeletal muscle.

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: July 22, 2015
This is version 135 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

External Data

Dasty 3

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 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.