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Protein

Calpain-3

Gene

Capn3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Calcium-regulated non-lysosomal thiol-protease.

Catalytic activityi

Broad endopeptidase activity.

Enzyme regulationi

Activated by micromolar concentrations of calcium and inhibited by calpastatin.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei129PROSITE-ProRule annotation1
Active sitei334PROSITE-ProRule annotation1
Active sitei358PROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi662 – 6721By similarityAdd BLAST11
Calcium bindingi705 – 7162PROSITE-ProRule annotationBy similarityAdd BLAST12
Calcium bindingi735 – 7413PROSITE-ProRule annotationBy similarity7
Calcium bindingi800 – 8064By similarity7

GO - Molecular functioni

  • calcium-dependent cysteine-type endopeptidase activity Source: RGD
  • calcium ion binding Source: UniProtKB
  • catalytic activity Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • ligase regulator activity Source: UniProtKB
  • peptidase activity Source: RGD
  • protein complex scaffold activity Source: UniProtKB
  • receptor binding Source: UniProtKB
  • sodium ion binding Source: UniProtKB
  • structural constituent of muscle Source: UniProtKB
  • titin binding Source: UniProtKB

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BRENDAi3.4.22.54. 5301.

Protein family/group databases

MEROPSiC02.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Calpain-3 (EC:3.4.22.54)
Alternative name(s):
Calcium-activated neutral proteinase 3
Short name:
CANP 3
Calpain L3
Calpain p94
Muscle-specific calcium-activated neutral protease 3
Gene namesi
Name:Capn3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2269. Capn3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • cytosol Source: UniProtKB
  • myofibril Source: UniProtKB
  • nucleus Source: RGD
  • plasma membrane Source: UniProtKB
  • protein complex Source: UniProtKB
  • T-tubule Source: UniProtKB
  • Z disc Source: UniProtKB

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002077101 – 821Calpain-3Add BLAST821

Proteomic databases

PaxDbiP16259.
PRIDEiP16259.

PTM databases

PhosphoSitePlusiP16259.

Miscellaneous databases

PMAP-CutDBiP16259.

Expressioni

Tissue specificityi

Skeletal muscle.

Interactioni

Subunit structurei

Homodimer; via EF-hand domain 4. Interacts with TTN/titin. Interacts with CMYA5; this interaction, which results in CMYA5 proteolysis, may protect CAPN3 from autolysis.By similarity

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • protein complex scaffold activity Source: UniProtKB
  • receptor binding Source: UniProtKB
  • titin binding Source: UniProtKB

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000011761.

Structurei

3D structure databases

ProteinModelPortaliP16259.
SMRiP16259.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini74 – 417Calpain catalyticPROSITE-ProRule annotationAdd BLAST344
Domaini649 – 683EF-hand 1PROSITE-ProRule annotationAdd BLAST35
Domaini692 – 725EF-hand 2PROSITE-ProRule annotationAdd BLAST34
Domaini722 – 757EF-hand 3PROSITE-ProRule annotationAdd BLAST36
Domaini787 – 821EF-hand 4PROSITE-ProRule annotationAdd BLAST35

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni418 – 586Domain IIIAdd BLAST169
Regioni587 – 649LinkerAdd BLAST63
Regioni650 – 820Domain IVAdd BLAST171

Sequence similaritiesi

Belongs to the peptidase C2 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0045. Eukaryota.
ENOG410XP0B. LUCA.
HOGENOMiHOG000232035.
HOVERGENiHBG012645.
InParanoidiP16259.
KOiK08573.
PhylomeDBiP16259.

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.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000169. Pept_cys_AS.
IPR001300. Peptidase_C2_calpain_cat.
PfamiView protein in Pfam
PF01067. Calpain_III. 1 hit.
PF13202. EF-hand_5. 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.
SM00054. EFh. 3 hits.
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. 4 hits.
PS00139. THIOL_PROTEASE_CYS. 1 hit.

Sequencei

Sequence statusi: Complete.

P16259-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTVISPTVA PRTGAEPRSP GPVPHPAQGK TTEAGGGHPG GIYSAIISRN
60 70 80 90 100
FPIIGVKEKT FEQLHKKCLE KKVLYLDPEF PPDETSLFYS QKFPIQFVWK
110 120 130 140 150
RPPEICENPR FIIGGANRTD ICQGDLGDCW LLAAIACLTL NERLLFRVIP
160 170 180 190 200
HDQSFTENYA GIFHFQFWRY GDWVDVVIDD CLPTYNNQLV FTKSNHRNEF
210 220 230 240 250
WSALLEKAYA KLHGSYEALK GGNTTEAMED FTGGVTEFFE IKDAPSDMYK
260 270 280 290 300
IMRKAIERGS LMGCSIDDGT NMTYGTSPSG LNMGELIARM VRNMDNSLLR
310 320 330 340 350
DSDLDPRASD DRPSRTIVPV QYETRMACGL VKGHAYSVTG LEEALFKGEK
360 370 380 390 400
VKLVRLRNPW GQVEWNGSWS DGWKDWSFVD KDEKARLQHQ VTEDGEFWMS
410 420 430 440 450
YDDFVYHFTK LEICNLTADA LESDKLQTWT VSVNEGRWVR GCSAGGCRNF
460 470 480 490 500
PDTFWTNPQY RLKLLEEDDD PDDSEVICSF LVALMQKNRR KDRKLGANLF
510 520 530 540 550
TIGFAIYEVP KEMHGNKQHL QKDFFLYNAS KARSKTYINM REVSQRFRLP
560 570 580 590 600
PSEYVIVPST YEPHQEGEFI LRVFSEKRNL SEEAENTISV DRPVKKKKNK
610 620 630 640 650
PIIFVSDRAN SNKELGVDQE AEEGKDKTGP DKQGESPQPR PGHTDQESEE
660 670 680 690 700
QQQFRNIFRQ IAGDDMEICA DELKNVLNTV VNKHKDLKTQ GFTLESCRSM
710 720 730 740 750
IALMDTDGSG RLNLQEFHHL WKKIKAWQKI FKHYDTDHSG TINSYEMRNA
760 770 780 790 800
VNDAGFHLNS QLYDIITMRY ADKHMNIDFD SFICCFVRLE GMFRAFHAFD
810 820
KDGDGIIKLN VLEWLQLTMY A
Length:821
Mass (Da):94,127
Last modified:August 1, 1990 - v1
Checksum:i27FAEAD2FEA19FBF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05121 mRNA. Translation: AAA41790.1.
PIRiB34488.
RefSeqiNP_058813.1. NM_017117.1.
UniGeneiRn.9726.

Genome annotation databases

GeneIDi29155.
KEGGirno:29155.
UCSCiRGD:2269. rat.

Similar proteinsi

Entry informationi

Entry nameiCAN3_RAT
AccessioniPrimary (citable) accession number: P16259
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: August 30, 2017
This is version 151 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