SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P97571

- CAN1_RAT

UniProt

P97571 - CAN1_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Calpain-1 catalytic subunit
Gene
Capn1, Cls1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein 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

Binds 4 calcium 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 form By similarity
Sitei27 – 282Cleavage; for 75 kDa form By similarity
Active sitei115 – 1151 By similarity
Active sitei272 – 2721 By similarity
Active sitei296 – 2961 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi99 – 106812 Publications
Calcium bindingi302 – 3333222 Publications
Add
BLAST
Calcium bindingi597 – 608123 By similarity
Add
BLAST
Calcium bindingi627 – 638124 By similarity
Add
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: RGD
  2. calcium-dependent cysteine-type endopeptidase activity Source: UniProtKB
  3. cytoskeletal protein binding Source: RGD
  4. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. protein autoprocessing Source: RGD
  2. proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.22.52. 5301.

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
Synonyms:Cls1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2267. Capn1.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: RefGenome
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 713712Calpain-1 catalytic subunit
PRO_0000207700Add
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.

Keywords - PTMi

Autocatalytic cleavage

Proteomic databases

PaxDbiP97571.
PRIDEiP97571.

PTM databases

PhosphoSiteiP97571.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

GenevestigatoriP97571.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028431.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 393
Helixi42 – 5110
Helixi65 – 684
Beta strandi70 – 767
Helixi78 – 825
Beta strandi84 – 863
Helixi88 – 914
Beta strandi99 – 1024
Helixi104 – 1063
Beta strandi111 – 1133
Helixi115 – 12410
Helixi128 – 1347
Beta strandi147 – 1559
Beta strandi158 – 1669
Beta strandi168 – 1714
Beta strandi174 – 1774
Beta strandi181 – 1833
Helixi187 – 19913
Beta strandi200 – 2023
Helixi203 – 2053
Beta strandi206 – 2083
Helixi210 – 2167
Beta strandi221 – 2266
Helixi227 – 2293
Helixi234 – 24411
Beta strandi247 – 2515
Beta strandi255 – 2584
Beta strandi261 – 2633
Beta strandi269 – 2713
Beta strandi274 – 28411
Beta strandi287 – 2959
Helixi312 – 3165
Helixi319 – 3257
Beta strandi331 – 3377
Helixi338 – 3447
Beta strandi347 – 3526
Beta strandi370 – 3756
Turni377 – 3793
Turni388 – 3903
Helixi391 – 3933
Beta strandi398 – 4014
Beta strandi418 – 4258
Beta strandi441 – 4477
Helixi461 – 4644
Beta strandi477 – 4804
Beta strandi482 – 4876
Beta strandi490 – 50314
Beta strandi506 – 51611
Beta strandi518 – 5203
Beta strandi528 – 5303
Beta strandi556 – 5594
Turni565 – 5695
Helixi586 – 59611
Beta strandi606 – 6083
Helixi609 – 62315
Helixi624 – 6263
Helixi636 – 64510

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KXRX-ray2.07A/B27-356[»]
1QXPX-ray2.80A/B60-647[»]
1TL9X-ray1.80A27-356[»]
1TLOX-ray1.90A27-356[»]
2G8EX-ray2.25A27-356[»]
2G8JX-ray1.61A27-356[»]
2NQGX-ray2.04A27-356[»]
2NQIX-ray2.04A27-356[»]
2R9CX-ray1.80A27-356[»]
2R9FX-ray1.60A27-356[»]
ProteinModelPortaliP97571.
SMRiP97571. Positions 13-712.

Miscellaneous databases

EvolutionaryTraceiP97571.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 354300Calpain catalytic
Add
BLAST
Domaini540 – 57536EF-hand 1
Add
BLAST
Domaini584 – 61734EF-hand 2
Add
BLAST
Domaini614 – 64936EF-hand 3
Add
BLAST
Domaini679 – 71335EF-hand 4
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni355 – 525171Domain III
Add
BLAST
Regioni526 – 54116Linker
Add
BLAST
Regioni542 – 712171Domain IV
Add
BLAST

Sequence similaritiesi

Belongs to the peptidase C2 family.
Contains 4 EF-hand domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG327523.
HOGENOMiHOG000232035.
HOVERGENiHBG012645.
InParanoidiP97571.
KOiK01367.
PhylomeDBiP97571.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR022684. 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.
[Graphical view]
PfamiPF01067. Calpain_III. 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. 4 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.

P97571-1 [UniParc]FASTAAdd to Basket

« Hide

MAEELITPVY CTGVSAQVQK QRDKELGLGR HENAIKYLGQ DYENLRARCL    50
QNGVLFQDDA FPPVSHSLGF KELGPNSSKT YGIKWKRPTE LLSNPQFIVD 100
GATRTDICQG ALGDCWLLAA IASLTLNETI LHRVVPYGQS FQEGYAGIFH 150
FQLWQFGEWV DVVVDDLLPT KDGKLVFVHS AQGNEFWSAL LEKAYAKVNG 200
SYEALSGGCT SEAFEDFTGG VTEWYDLQKA PSDLYQIILK ALERGSLLGC 250
SINISDIRDL EAITFKNLVR GHAYSVTDAK QVTYQGQRVN LIRMRNPWGE 300
VEWKGPWSDN SYEWNKVDPY EREQLRVKME DGEFWMSFRD FIREFTKLEI 350
CNLTPDALKS RTLRNWNTTF YEGTWRRGST AGGCRNYPAT FWVNPQFKIR 400
LEEVDDADDY DSRESGCSFL LALMQKHRRR ERRFGRDMET IGFAVYQVPR 450
ELAGQPVHLK RDFFLANASR AQSEHFINLR EVSNRIRLPP GEYIVVPSTF 500
EPNKEGDFLL RFFSEKKAGT QELDDQIQAN LPDEKVLSEE EIDDNFKTLF 550
SKLAGDDMEI SVKELQTILN RIISKHKDLR TNGFSLESCR SMVNLMDRDG 600
NGKLGLVEFN ILWNRIRNYL TIFRKFDLDK SGSMSAYEMR MAIEAAGFKL 650
NKKLHELIIT RYSEPDLAVD FDNFVCCLVR LETMFRFFKI LDTDLDGVVT 700
FDLFKWLQLT MFA 713
Length:713
Mass (Da):82,119
Last modified:May 1, 1997 - v1
Checksum:i6E664600B0EFAEBB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U53858 mRNA. Translation: AAC53001.1.
BC061880 mRNA. Translation: AAH61880.1.
RefSeqiNP_062025.1. NM_019152.2.
UniGeneiRn.6037.

Genome annotation databases

GeneIDi29153.
KEGGirno:29153.
UCSCiRGD:2267. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U53858 mRNA. Translation: AAC53001.1 .
BC061880 mRNA. Translation: AAH61880.1 .
RefSeqi NP_062025.1. NM_019152.2.
UniGenei Rn.6037.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KXR X-ray 2.07 A/B 27-356 [» ]
1QXP X-ray 2.80 A/B 60-647 [» ]
1TL9 X-ray 1.80 A 27-356 [» ]
1TLO X-ray 1.90 A 27-356 [» ]
2G8E X-ray 2.25 A 27-356 [» ]
2G8J X-ray 1.61 A 27-356 [» ]
2NQG X-ray 2.04 A 27-356 [» ]
2NQI X-ray 2.04 A 27-356 [» ]
2R9C X-ray 1.80 A 27-356 [» ]
2R9F X-ray 1.60 A 27-356 [» ]
ProteinModelPortali P97571.
SMRi P97571. Positions 13-712.
ModBasei Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000028431.

Chemistry

BindingDBi P97571.
ChEMBLi CHEMBL3747.

Protein family/group databases

MEROPSi C02.001.

PTM databases

PhosphoSitei P97571.

Proteomic databases

PaxDbi P97571.
PRIDEi P97571.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 29153.
KEGGi rno:29153.
UCSCi RGD:2267. rat.

Organism-specific databases

CTDi 823.
RGDi 2267. Capn1.

Phylogenomic databases

eggNOGi NOG327523.
HOGENOMi HOG000232035.
HOVERGENi HBG012645.
InParanoidi P97571.
KOi K01367.
PhylomeDBi P97571.

Enzyme and pathway databases

BRENDAi 3.4.22.52. 5301.

Miscellaneous databases

EvolutionaryTracei P97571.
NextBioi 608167.
PROi P97571.

Gene expression databases

Genevestigatori P97571.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
InterProi 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.
[Graphical view ]
Pfami PF01067. Calpain_III. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view ]
PRINTSi PR00704. CALPAIN.
SMARTi SM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
SM00054. EFh. 3 hits.
[Graphical view ]
SUPFAMi SSF49758. SSF49758. 1 hit.
PROSITEi PS50203. CALPAIN_CAT. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 4 hits.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Primary sequences of rat mu-calpain large and small subunits are, respectively, moderately and highly similar to those of human."
    Sorimachi H., Amano S., Ishiura S., Suzuki K.
    Biochim. Biophys. Acta 1309:37-41(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  3. "A Ca(2+) switch aligns the active site of calpain."
    Moldoveanu T., Hosfield C.M., Lim D., Elce J.S., Jia Z., Davies P.L.
    Cell 108:649-660(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 27-356, CALCIUM-BINDING REGIONS.
  4. "Crystal structure of a micro-like calpain reveals a partially activated conformation with low Ca2+ requirement."
    Pal G.P., De Veyra T., Elce J.S., Jia Z.
    Structure 11:1521-1526(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 60-647.
  5. "Crystal structures of calpain-E64 and -leupeptin inhibitor complexes reveal mobile loops gating the active site."
    Moldoveanu T., Campbell R.L., Cuerrier D., Davies P.L.
    J. Mol. Biol. 343:1313-1326(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 27-356 IN COMPLEX WITH INHIBITORS, CALCIUM-BINDING REGIONS.

Entry informationi

Entry nameiCAN1_RAT
AccessioniPrimary (citable) accession number: P97571
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: May 1, 1997
Last modified: June 11, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi