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Protein

Calpain-A

Gene

CalpA

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calcium-regulated non-lysosomal thiol-protease. Involved in the organization of the actin-related cytoskeleton during embryogenesis.2 Publications

Catalytic activityi

Broad endopeptidase specificity.

Enzyme regulationi

Activated by millimolar concentrations of calcium, and by phosphatidylinositol 4,5-diphosphate, phosphatidylinositol 4-monophosphate, phosphatidylinositol and phosphatidic acid.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei143 – 1431By similarity
Active sitei299 – 2991By similarity
Active sitei327 – 3271By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi712 – 723121CuratedAdd
BLAST
Calcium bindingi742 – 753122CuratedAdd
BLAST

GO - Molecular functioni

  • calcium-dependent cysteine-type endopeptidase activity Source: UniProtKB
  • calcium ion binding Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton organization Source: FlyBase
  • BMP signaling pathway involved in spinal cord dorsal/ventral patterning Source: FlyBase
  • cuticle development Source: FlyBase
  • defense response to fungus Source: FlyBase
  • determination of adult lifespan Source: FlyBase
  • dorsal/ventral pattern formation Source: FlyBase
  • phagocytosis Source: FlyBase
  • protein autoprocessing Source: FlyBase
  • 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.B36. 1994.

Protein family/group databases

MEROPSiC02.014.

Names & Taxonomyi

Protein namesi
Recommended name:
Calpain-A (EC:3.4.22.-)
Alternative name(s):
Calcium-activated neutral proteinase A
Short name:
CANP A
Cleaved into the following chain:
Gene namesi
Name:CalpA
ORF Names:CG7563
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0012051. CalpA.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • actin cytoskeleton Source: UniProtKB
  • cytoplasm Source: FlyBase
  • intracellular Source: UniProtKB
  • neuronal cell body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 828828Calpain-APRO_0000026497Add
BLAST
Chaini55 – 828774Calpain-A catalytic subunitPRO_0000026498Add
BLAST

Post-translational modificationi

Undergoes calcium-dependent autolytic cleavage between Lys-54 and Asn-55, which is necessary for activation of the protein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei54 – 552Cleavage; by autolysis

Keywords - PTMi

Autocatalytic cleavage

Proteomic databases

PaxDbiQ11002.

Expressioni

Tissue specificityi

Localized to the anterior and posterior embryonic poles just after fertilization. Becomes distributed around the polar buds and just below the pole cells of the posterior pole during cleavage cycles. During these nuclear divisions anterior localization disappears. Localized to actin caps that underlie the plasma membrane, immediately above each nucleus at cleavage cycles 8 and 9. Localized to a small set of nerve, midgut and blood cells in adults.2 Publications

Gene expression databases

BgeeiQ11002.
ExpressionAtlasiQ11002. differential.
GenevisibleiQ11002. DM.

Interactioni

Protein-protein interaction databases

BioGridi62895. 1 interaction.
DIPiDIP-23245N.
IntActiQ11002. 1 interaction.
STRINGi7227.FBpp0085714.

Structurei

3D structure databases

ProteinModelPortaliQ11002.
SMRiQ11002. Positions 69-828.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 1414EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini88 – 387300Calpain catalyticPROSITE-ProRule annotationAdd
BLAST
Domaini579 – 61436EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini699 – 73436EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini729 – 76436EF-hand 4PROSITE-ProRule annotationAdd
BLAST
Domaini764 – 79936EF-hand 5PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni388 – 557170Domain IIIAdd
BLAST
Regioni558 – 57720LinkerAdd
BLAST
Regioni578 – 828251Domain IVAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C2 family.Curated
Contains 1 calpain catalytic domain.PROSITE-ProRule annotation
Contains 5 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0045. Eukaryota.
ENOG410XP0B. LUCA.
GeneTreeiENSGT00760000118971.
InParanoidiQ11002.
KOiK08585.
OMAiITPGFPT.
OrthoDBiEOG7RV9FM.
PhylomeDBiQ11002.

Family and domain databases

Gene3Di1.10.238.10. 3 hits.
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. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 2 hits.
SSF49758. SSF49758. 1 hit.
PROSITEiPS50203. CALPAIN_CAT. 1 hit.
PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 5 hits.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform B (identifier: Q11002-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDDLRGFLRQ AGQEFLNAAG EAAMGAAKDV VGSVINEIFI KKEADTKRVL
60 70 80 90 100
PSIKNMRVLG EKSSSLGPYS EVQDYETILN SCLASGSLFE DPLFPASNES
110 120 130 140 150
LQFSRRPDRH IEWLRPHEIA ENPQFFVEGY SRFDVQQGEL GDCWLLAATA
160 170 180 190 200
NLTQESNLFF RVIPAEQSFE ENYAGIFHFR FWQYGKWVDV IIDDRLPTYN
210 220 230 240 250
GELMYMHSTE KNEFWSALLE KAYAKLHGSY EALKGGSTCE AMEDFTGGVS
260 270 280 290 300
EWYDLKEAPG NLFTILQKAA ERNSMMGCSI EPDPNVTEAE TPQGLIRGHA
310 320 330 340 350
YSITKVCLID IVTPNRQGKI PMIRMRNPWG NEAEWNGPWS DSSPEWRYIP
360 370 380 390 400
EEQKAEIGLT FDRDGEFWMS FQDFLNHFDR VEICNLSPDS LTEDQQNSGK
410 420 430 440 450
RKWEMSMYEG EWTPGVTAGG CRNFLDTFWH NPQYIITLVD PDEEDEEGQC
460 470 480 490 500
TVIVALMQKN RRSKRNMGME CLTIGFAIYS LNDRELENRP QGLNFFRYKS
510 520 530 540 550
SVGRSPHFIN TREVCARFKL PPGHYLIVPS TFDPNEEGEF IIRVFSETQN
560 570 580 590 600
NMEENDDHVG YGGKADTITP GFPTPKPIDP QKEGLRRLFD SIAGKDMEVD
610 620 630 640 650
WMELKRILDH SMRDDLPKPV VFNRFSNNMA FETQAAGPGD DGAGACGLLS
660 670 680 690 700
LICGPFLKGT PFEEQLGMND QSNKRLIGDN PADGGPVTAN AIVDETHGFS
710 720 730 740 750
KDVCRSMVAM LDADKSGKLG FEEFETLLSE IAKWKAIFKV YDVENTGRVS
760 770 780 790 800
GFQLREALNS AGYHLNNRVL NVLGHRYGSR DGKIAFDDFI MCAVKIKTYI
810 820
DIFKERDTEK NETATFTLEE WIERTIYS
Length:828
Mass (Da):93,963
Last modified:October 18, 2001 - v2
Checksum:i09576D1268BD569C
GO
Isoform A (identifier: Q11002-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     554-565: ENDDHVGYGGKA → CVQVDNDNEFVY
     566-828: Missing.

Show »
Length:565
Mass (Da):64,807
Checksum:i10CDF03B086DB8D5
GO

Sequence cautioni

The sequence CAA55297.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351I → Y in CAA86993 (PubMed:7823949).Curated
Sequence conflicti35 – 351I → Y in CAA86994 (PubMed:7823949).Curated
Sequence conflicti306 – 3061V → I in CAA86994 (PubMed:7823949).Curated
Sequence conflicti397 – 3971N → H in CAA55298 (PubMed:7929201).Curated
Sequence conflicti397 – 3971N → H in CAA55297 (PubMed:7929201).Curated
Isoform A (identifier: Q11002-2)
Sequence conflicti554 – 56512CVQVD…NEFVY → RTSRQ in CAA86994 (PubMed:7823949).CuratedAdd
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei554 – 56512ENDDH…YGGKA → CVQVDNDNEFVY in isoform A. 1 PublicationVSP_005244Add
BLAST
Alternative sequencei566 – 828263Missing in isoform A. 1 PublicationVSP_005245Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78555 mRNA. Translation: CAA55298.1.
X78555 mRNA. Translation: CAA55297.1. Different initiation.
Z46891 mRNA. Translation: CAA86993.1.
Z46892 mRNA. Translation: CAA86994.1.
AE013599 Genomic DNA. Translation: AAF57563.1.
AE013599 Genomic DNA. Translation: AAF57564.1.
AY051678 mRNA. Translation: AAK93102.1.
RefSeqiNP_001097378.1. NM_001103908.2. [Q11002-1]
NP_477047.1. NM_057699.5. [Q11002-1]
NP_477048.1. NM_057700.4. [Q11002-2]
UniGeneiDm.1726.

Genome annotation databases

EnsemblMetazoaiFBtr0086529; FBpp0085714; FBgn0012051. [Q11002-1]
FBtr0112869; FBpp0111782; FBgn0012051. [Q11002-1]
GeneIDi37232.
KEGGidme:Dmel_CG7563.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78555 mRNA. Translation: CAA55298.1.
X78555 mRNA. Translation: CAA55297.1. Different initiation.
Z46891 mRNA. Translation: CAA86993.1.
Z46892 mRNA. Translation: CAA86994.1.
AE013599 Genomic DNA. Translation: AAF57563.1.
AE013599 Genomic DNA. Translation: AAF57564.1.
AY051678 mRNA. Translation: AAK93102.1.
RefSeqiNP_001097378.1. NM_001103908.2. [Q11002-1]
NP_477047.1. NM_057699.5. [Q11002-1]
NP_477048.1. NM_057700.4. [Q11002-2]
UniGeneiDm.1726.

3D structure databases

ProteinModelPortaliQ11002.
SMRiQ11002. Positions 69-828.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62895. 1 interaction.
DIPiDIP-23245N.
IntActiQ11002. 1 interaction.
STRINGi7227.FBpp0085714.

Protein family/group databases

MEROPSiC02.014.

Proteomic databases

PaxDbiQ11002.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0086529; FBpp0085714; FBgn0012051. [Q11002-1]
FBtr0112869; FBpp0111782; FBgn0012051. [Q11002-1]
GeneIDi37232.
KEGGidme:Dmel_CG7563.

Organism-specific databases

CTDi37232.
FlyBaseiFBgn0012051. CalpA.

Phylogenomic databases

eggNOGiKOG0045. Eukaryota.
ENOG410XP0B. LUCA.
GeneTreeiENSGT00760000118971.
InParanoidiQ11002.
KOiK08585.
OMAiITPGFPT.
OrthoDBiEOG7RV9FM.
PhylomeDBiQ11002.

Enzyme and pathway databases

BRENDAi3.4.22.B36. 1994.

Miscellaneous databases

GenomeRNAii37232.
PROiQ11002.

Gene expression databases

BgeeiQ11002.
ExpressionAtlasiQ11002. differential.
GenevisibleiQ11002. DM.

Family and domain databases

Gene3Di1.10.238.10. 3 hits.
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. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 2 hits.
SSF49758. SSF49758. 1 hit.
PROSITEiPS50203. CALPAIN_CAT. 1 hit.
PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 5 hits.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Calpain localization changes in coordination with actin-related cytoskeletal changes during early embryonic development of Drosophila."
    Emori Y., Saigo K.
    J. Biol. Chem. 269:25137-25142(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, TISSUE SPECIFICITY.
    Strain: Canton-S.
    Tissue: Larva.
  2. "CalpA, a Drosophila calpain homolog specifically expressed in a small set of nerve, midgut, and blood cells."
    Theopold U., Pinter M., Daffre S., Tryselius Y., Friedrich P., Nassel D.R., Hultmark D.
    Mol. Cell. Biol. 15:824-834(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: Canton-S.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
    Strain: Berkeley.
    Tissue: Embryo.
  6. "Characterization of two recombinant Drosophila calpains. CALPA and a novel homolog, CALPB."
    Jekely G., Friedrich P.
    J. Biol. Chem. 274:23893-23900(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, ENZYME REGULATION, AUTOCATALYTIC CLEAVAGE.

Entry informationi

Entry nameiCANA_DROME
AccessioniPrimary (citable) accession number: Q11002
Secondary accession number(s): Q9V8U6, Q9V8U7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 18, 2001
Last modified: June 8, 2016
This is version 155 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

This protein binds calcium.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.