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P97571

- CAN1_RAT

UniProt

P97571 - CAN1_RAT

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Protein

Calpain-1 catalytic subunit

Gene

Capn1

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

Ca2+By similarityNote: Binds 4 Ca(2+) 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 – 10681
Calcium bindingi302 – 333322Add
BLAST
Calcium bindingi597 – 608123PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi627 – 638124PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

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

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-KW
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 – 713712Calpain-1 catalytic subunitPRO_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).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).1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028431.

Structurei

Secondary structure

1
713
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 393Combined sources
Helixi42 – 5110Combined sources
Helixi65 – 684Combined sources
Beta strandi70 – 767Combined sources
Helixi78 – 825Combined sources
Beta strandi84 – 863Combined sources
Helixi88 – 914Combined sources
Beta strandi99 – 1024Combined sources
Helixi104 – 1063Combined sources
Beta strandi111 – 1133Combined sources
Helixi115 – 12410Combined sources
Helixi128 – 1347Combined sources
Beta strandi147 – 1559Combined sources
Beta strandi158 – 1669Combined sources
Beta strandi168 – 1714Combined sources
Beta strandi174 – 1774Combined sources
Beta strandi181 – 1833Combined sources
Helixi187 – 19913Combined sources
Beta strandi200 – 2023Combined sources
Helixi203 – 2053Combined sources
Beta strandi206 – 2083Combined sources
Helixi210 – 2167Combined sources
Beta strandi221 – 2266Combined sources
Helixi227 – 2293Combined sources
Helixi234 – 24411Combined sources
Beta strandi247 – 2515Combined sources
Beta strandi255 – 2584Combined sources
Beta strandi261 – 2633Combined sources
Beta strandi269 – 2713Combined sources
Beta strandi274 – 28411Combined sources
Beta strandi287 – 2959Combined sources
Helixi312 – 3165Combined sources
Helixi319 – 3257Combined sources
Beta strandi331 – 3377Combined sources
Helixi338 – 3447Combined sources
Beta strandi347 – 3526Combined sources
Beta strandi370 – 3756Combined sources
Turni377 – 3793Combined sources
Turni388 – 3903Combined sources
Helixi391 – 3933Combined sources
Beta strandi398 – 4014Combined sources
Beta strandi418 – 4258Combined sources
Beta strandi441 – 4477Combined sources
Helixi461 – 4644Combined sources
Beta strandi477 – 4804Combined sources
Beta strandi482 – 4876Combined sources
Beta strandi490 – 50314Combined sources
Beta strandi506 – 51611Combined sources
Beta strandi518 – 5203Combined sources
Beta strandi528 – 5303Combined sources
Beta strandi556 – 5594Combined sources
Turni565 – 5695Combined sources
Helixi586 – 59611Combined sources
Beta strandi606 – 6083Combined sources
Helixi609 – 62315Combined sources
Helixi624 – 6263Combined sources
Helixi636 – 64510Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP97571.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni355 – 525171Domain IIIAdd
BLAST
Regioni526 – 54116LinkerAdd
BLAST
Regioni542 – 712171Domain IVAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C2 family.Curated
Contains 1 calpain catalytic domain.PROSITE-ProRule annotation
Contains 4 EF-hand domains.PROSITE-ProRule annotation

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.
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.
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

        10         20         30         40         50
MAEELITPVY CTGVSAQVQK QRDKELGLGR HENAIKYLGQ DYENLRARCL
60 70 80 90 100
QNGVLFQDDA FPPVSHSLGF KELGPNSSKT YGIKWKRPTE LLSNPQFIVD
110 120 130 140 150
GATRTDICQG ALGDCWLLAA IASLTLNETI LHRVVPYGQS FQEGYAGIFH
160 170 180 190 200
FQLWQFGEWV DVVVDDLLPT KDGKLVFVHS AQGNEFWSAL LEKAYAKVNG
210 220 230 240 250
SYEALSGGCT SEAFEDFTGG VTEWYDLQKA PSDLYQIILK ALERGSLLGC
260 270 280 290 300
SINISDIRDL EAITFKNLVR GHAYSVTDAK QVTYQGQRVN LIRMRNPWGE
310 320 330 340 350
VEWKGPWSDN SYEWNKVDPY EREQLRVKME DGEFWMSFRD FIREFTKLEI
360 370 380 390 400
CNLTPDALKS RTLRNWNTTF YEGTWRRGST AGGCRNYPAT FWVNPQFKIR
410 420 430 440 450
LEEVDDADDY DSRESGCSFL LALMQKHRRR ERRFGRDMET IGFAVYQVPR
460 470 480 490 500
ELAGQPVHLK RDFFLANASR AQSEHFINLR EVSNRIRLPP GEYIVVPSTF
510 520 530 540 550
EPNKEGDFLL RFFSEKKAGT QELDDQIQAN LPDEKVLSEE EIDDNFKTLF
560 570 580 590 600
SKLAGDDMEI SVKELQTILN RIISKHKDLR TNGFSLESCR SMVNLMDRDG
610 620 630 640 650
NGKLGLVEFN ILWNRIRNYL TIFRKFDLDK SGSMSAYEMR MAIEAAGFKL
660 670 680 690 700
NKKLHELIIT RYSEPDLAVD FDNFVCCLVR LETMFRFFKI LDTDLDGVVT
710
FDLFKWLQLT MFA
Length:713
Mass (Da):82,119
Last modified:May 1, 1997 - v1
Checksum:i6E664600B0EFAEBB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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...
MobiDBi 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.
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 ]
PANTHERi PTHR10183:SF284. PTHR10183:SF284. 1 hit.
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: November 26, 2014
This is version 136 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