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Protein

Calpain-1 catalytic subunit

Gene

CAPN1

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

Broad endopeptidase specificity.By similarity

Cofactori

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

Enzyme regulationi

Activated by micromolar concentrations of calcium and inhibited by calpastatin.By similarity

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

Keywordsi

Molecular functionHydrolase, Protease, Thiol protease
LigandCalcium, Metal-binding

Protein family/group databases

MEROPSiC02.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Calpain-1 catalytic subunitCurated (EC:3.4.22.52By similarity)
Alternative name(s):
Calcium-activated neutral proteinase 1By similarity
Short name:
CANP 1By similarity
Calpain mu-typeBy similarity
Calpain-1 large subunit
Micromolar-calpainBy similarity
Short name:
muCANPBy similarity
Gene namesi
Name:CAPN1By similarity
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
Proteomesi
  • UP000001595 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002076981 – 714Calpain-1 catalytic subunitAdd BLAST714

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

PRIDEiQ5NVS7.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000003556.

Structurei

3D structure databases

ProteinModelPortaliQ5NVS7.
SMRiQ5NVS7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini55 – 354Calpain catalyticPROSITE-ProRule annotationAdd BLAST300
Domaini541 – 576EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini585 – 618EF-hand 2PROSITE-ProRule annotationAdd BLAST34
Domaini615 – 650EF-hand 3PROSITE-ProRule annotationAdd BLAST36
Domaini680 – 714EF-hand 4PROSITE-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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0045. Eukaryota.
ENOG410XP0B. LUCA.
HOVERGENiHBG012645.
InParanoidiQ5NVS7.
KOiK01367.

Family and domain databases

CDDicd00214. Calpain_III. 1 hit.
cd00044. CysPc. 1 hit.
InterProiView protein in InterPro
IPR033883. C2_III.
IPR022684. Calpain_cysteine_protease.
IPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR036213. Calpain_III_sf.
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.
PANTHERiPTHR10183:SF284. PTHR10183:SF284. 1 hit.
PfamiView protein in Pfam
PF01067. Calpain_III. 1 hit.
PF13833. EF-hand_8. 1 hit.
PF00648. Peptidase_C2. 1 hit.
PRINTSiPR00704. CALPAIN.
SMARTiView protein in SMART
SM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF49758. SSF49758. 1 hit.
PROSITEiView protein in PROSITE
PS50203. CALPAIN_CAT. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS00139. THIOL_PROTEASE_CYS. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5NVS7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEEIITPVY CTGVSAQVQK QRARELGLGR HENAIKYLGQ DYEQLRVRCL
60 70 80 90 100
QSGTLFRDEA FPPVPQSLGY KDLGPNSSKT YGIKWKRPTE LLSNPQFIVD
110 120 130 140 150
GATRTDICQG ALGDCWLLAA IASLTLNDTL LHRVVPHGQS FQNGYAGIFH
160 170 180 190 200
FQLWQFGEWV DVVVDDLLPI KDGKLVFVHS AEGNEFWSAL LEKAYAKVNG
210 220 230 240 250
SYEALSGGST SEGFEDFTGG VTEWYELRKA PSDLYQIILK ALERGSLLGC
260 270 280 290 300
SIDISSVLDM EAITFKKLVK GHAYSVTGAK QVNYRGQMVS LIRMRNPWGE
310 320 330 340 350
VEWTGAWSDS SSEWNNVDPY ERDQLRVKME DGEFWMSFRD FMREFTRLEI
360 370 380 390 400
CNLTPDALKS RTIRKWNTTL YEGTWRRGST AGGCRNYPAT FWVNPQFKIR
410 420 430 440 450
LDETDDPDDY GDRESGCSFV LALMQKHRRR ERRFGRDMET IGFAVYEVPP
460 470 480 490 500
ELAGQPAVHL KRDFFLANAS RARSEQFINL REVSTRFRLP PGEYVVVPST
510 520 530 540 550
FEPNKEGDFV LRFFSEKSAG TAELDDQIQA NLPDEQVLSE EEIDENFKAL
560 570 580 590 600
FRQLAGEDME TSVKELRTIL NRIISKHKDL RTKGFSLESC RSMVNLMDRD
610 620 630 640 650
GNGKLGLVEF NILWNRIRNY LSIFRKFDLD KSGSMSAYEM RMAIESAGFK
660 670 680 690 700
LNKKLYELII TRYSEPDLAV DFDNFVCCLV RLETMFRFFK TLDTDLDGVV
710
TFDLFKWLQL TMFA
Length:714
Mass (Da):81,854
Last modified:January 4, 2005 - v1
Checksum:i40613EBE7FBD7D3A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR925924 mRNA. Translation: CAI29586.1.
RefSeqiNP_001127061.1. NM_001133589.1.
UniGeneiPab.656.

Genome annotation databases

GeneIDi100174090.
KEGGipon:100174090.

Similar proteinsi

Entry informationi

Entry nameiCAN1_PONAB
AccessioniPrimary (citable) accession number: Q5NVS7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 4, 2005
Last modified: October 25, 2017
This is version 90 of the entry and version 1 of the sequence. See 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