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P06814

- CAN2_RABIT

UniProt

P06814 - CAN2_RABIT

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Protein

Calpain-2 catalytic subunit

Gene

CAPN2

Organism
Oryctolagus cuniculus (Rabbit)
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. Proteolytically cleaves MYOC at 'Arg-226' (By similarity).By similarity

Catalytic activityi

Broad endopeptidase specificity.

Cofactori

Ca2+By similarityNote: Binds 7 Ca(2+) ions.By similarity

Enzyme regulationi

Activated by 200-1000 micromolar concentrations of calcium and inhibited by calpastatin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei8 – 81PROSITE-ProRule annotation
Metal bindingi14 – 141Calcium 4By similarity
Metal bindingi21 – 211Calcium 4By similarity
Metal bindingi45 – 451Calcium 4; via carbonyl oxygenBy similarity
Metal bindingi264 – 2641Calcium 5; via carbonyl oxygenBy similarity
Metal bindingi267 – 2671Calcium 5By similarity
Metal bindingi269 – 2691Calcium 5; via carbonyl oxygenBy similarity
Metal bindingi274 – 2741Calcium 5By similarity
Metal bindingi307 – 3071Calcium 6By similarity
Metal bindingi309 – 3091Calcium 6By similarity
Metal bindingi311 – 3111Calcium 6; via carbonyl oxygenBy similarity
Metal bindingi313 – 3131Calcium 6; via carbonyl oxygenBy similarity
Metal bindingi318 – 3181Calcium 6By similarity
Metal bindingi337 – 3371Calcium 7By similarity
Metal bindingi339 – 3391Calcium 7By similarity
Metal bindingi341 – 3411Calcium 7; via carbonyl oxygenBy similarity
Metal bindingi343 – 3431Calcium 7; via carbonyl oxygenBy similarity
Metal bindingi348 – 3481Calcium 7By similarity
Metal bindingi380 – 3801Calcium 1By similarity
Metal bindingi383 – 3831Calcium 1By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi307 – 318121Add
BLAST
Calcium bindingi337 – 348122Add
BLAST

GO - Molecular functioni

  1. calcium-dependent cysteine-type endopeptidase activity Source: UniProtKB
  2. calcium ion binding Source: InterPro

GO - Biological processi

  1. cellular response to amino acid stimulus Source: UniProtKB
  2. proteolysis Source: UniProtKB
  3. regulation of cytoskeleton organization Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.22.53. 1749.

Protein family/group databases

MEROPSiC02.972.

Names & Taxonomyi

Protein namesi
Recommended name:
Calpain-2 catalytic subunit (EC:3.4.22.53)
Alternative name(s):
Calcium-activated neutral proteinase 2
Short name:
CANP 2
Calpain M-type
Calpain-2 large subunit
Millimolar-calpain
Short name:
M-calpain
Gene namesi
Name:CAPN2
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. dendrite Source: UniProtKB
  3. 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
Chaini‹1 – 422›422Calpain-2 catalytic subunitPRO_0000207704Add
BLAST

Proteomic databases

PRIDEiP06814.

Expressioni

Tissue specificityi

Ubiquitous.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000017627.

Structurei

3D structure databases

ProteinModelPortaliP06814.
SMRiP06814. Positions 1-422.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini‹1 – 66›66Calpain catalyticPROSITE-ProRule annotationAdd
BLAST
Domaini294 – 32734EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini324 – 35936EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini389 – 42234EF-hand 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni67 – 236170Domain IIIAdd
BLAST
Regioni237 – 25115LinkerAdd
BLAST
Regioni252 – 422171Domain 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.
HOGENOMiHOG000232035.
HOVERGENiHBG012645.
InParanoidiP06814.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR022684. Calpain_cysteine_protease.
IPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR029539. CAPN2.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001300. Peptidase_C2_calpain_cat.
[Graphical view]
PANTHERiPTHR10183:SF268. PTHR10183:SF268. 1 hit.
PfamiPF01067. Calpain_III. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view]
PRINTSiPR00704. CALPAIN.
SMARTiSM00720. calpain_III. 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.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P06814-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
QKLIRIRNPW GEVEWTGRWN DNCPNWNTVD PEVRERLAER HEDGEFWMSF
60 70 80 90 100
SDFLRHYSRL EICNLTPDTL TSDTYKKWKL TKMDGNWRRG STAGGCRNYP
110 120 130 140 150
NTFWMNPQYV IKLEEEDEDQ EDGESGCTFL VGLIQKHRRR QRKMGEDMHT
160 170 180 190 200
IGFGIYEVPE ELRGQTNIHL GKNFFLTTRA RERSDTFINL REVLNRFKLP
210 220 230 240 250
PGEYILVPST FEPNKNGDFC VRVFSEKKAD YQAVDDEIEA DLEEADVSED
260 270 280 290 300
DIDDGFRRLF AQLAGEDAEI SAFELQNILR RVLAKRQDIK TDGLSIETCK
310 320 330 340 350
IMVDMLDSDG TGKLGLKEFY VLWTKIQKYQ KIYREIDVDR SGTMNSYEMR
360 370 380 390 400
KALEEAGFKL PCQLHEVIVA RFADDQLIID FDNFVRCLVR LETLFKIFKQ
410 420
LDPDNTGMIQ LDLISWLCFS VL
Length:422
Mass (Da):49,494
Last modified:January 1, 1988 - v1
Checksum:iAE4FA3C48A333C41
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13797 mRNA. Translation: AAA31455.1.
PIRiB24815.
UniGeneiOcu.1954.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13797 mRNA. Translation: AAA31455.1 .
PIRi B24815.
UniGenei Ocu.1954.

3D structure databases

ProteinModelPortali P06814.
SMRi P06814. Positions 1-422.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9986.ENSOCUP00000017627.

Protein family/group databases

MEROPSi C02.972.

Proteomic databases

PRIDEi P06814.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG327523.
HOGENOMi HOG000232035.
HOVERGENi HBG012645.
InParanoidi P06814.

Enzyme and pathway databases

BRENDAi 3.4.22.53. 1749.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
InterProi IPR022684. Calpain_cysteine_protease.
IPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR029539. CAPN2.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001300. Peptidase_C2_calpain_cat.
[Graphical view ]
PANTHERi PTHR10183:SF268. PTHR10183:SF268. 1 hit.
Pfami PF01067. Calpain_III. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view ]
PRINTSi PR00704. CALPAIN.
SMARTi SM00720. calpain_III. 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. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Isolation and sequence analyses of cDNA clones for the large subunits of two isozymes of rabbit calcium-dependent protease."
    Emori Y., Kawasaki H., Sugihara H., Imajoh S., Kawashima S., Suzuki K.
    J. Biol. Chem. 261:9465-9471(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "E-F hand structure-domain of calcium-activated neutral protease (CANP) can bind Ca2+ ions."
    Minami Y., Emori Y., Kawasaki H., Suzuki K.
    J. Biochem. 101:889-895(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: CALCIUM-BINDING DATA.

Entry informationi

Entry nameiCAN2_RABIT
AccessioniPrimary (citable) accession number: P06814
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: November 26, 2014
This is version 125 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

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