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Protein

Calpain-B

Gene

CalpB

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.1 Publication

Catalytic activityi

Broad endopeptidase specificity.1 Publication

Enzyme regulationi

Activated by millimolar concentrations of calcium.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei314 – 3141By similarity
Active sitei470 – 4701By similarity
Active sitei498 – 4981By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi809 – 820121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi839 – 850122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  • border follicle cell migration Source: FlyBase
  • protein autoprocessing Source: FlyBase
  • proteolysis Source: UniProtKB
  • sensory perception of pain Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.22.B37. 1994.

Protein family/group databases

MEROPSiC02.015.

Names & Taxonomyi

Protein namesi
Recommended name:
Calpain-B (EC:3.4.22.-)
Alternative name(s):
Calcium-activated neutral proteinase B
Short name:
CANP B
Cleaved into the following 2 chains:
Gene namesi
Name:CalpBImported
ORF Names:CG8107
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0025866. CalpB.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Membrane 1 Publication

  • Note: Translocates to intracellular membranes when calcium levels are increased.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi73 – 753QNA → GVP: Autolysis site shifted to nearby, less-active sites. 1 Publication
Mutagenesisi223 – 2242NQ → AV: Autolysis site shifted to nearby, less-active site(s). 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 925925Calpain-BPRO_0000026499Add
BLAST
Chaini75 – 925851Calpain-B catalytic subunit 1PRO_0000026500Add
BLAST
Chaini225 – 925701Calpain-B catalytic subunit 2PRO_0000026501Add
BLAST

Post-translational modificationi

Undergoes calcium-dependent autolytic cleavage between Asn-74 and Ala-75 and between Gln-224 and Asn-225 to produce two major products, calpain B catalytic subunit 1 and calpain B catalytic subunit 2. This autolysis is necessary for activation of the protein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei74 – 752Cleavage; by autolysis
Sitei224 – 2252Cleavage; by autolysis

Keywords - PTMi

Autocatalytic cleavage

Proteomic databases

PaxDbiQ9VT65.
PRIDEiQ9VT65.

Miscellaneous databases

PMAP-CutDBQ9VT65.

Expressioni

Tissue specificityi

Strongly expressed in follicular and border cells of the oocyte. Ubiquitously expressed in early embryos. Localized to the trachea and their orifices, and to the larynx of late embryos. Restricted to the salivary gland in third instar larvae.1 Publication

Developmental stagei

Expressed in all developmental stages, with highest expression in the egg, probably of maternal origin. Very low expression in the early larva, rising through larval development up to the third larval stage. Constant expression in the pupa and adult.1 Publication

Gene expression databases

BgeeiQ9VT65.
ExpressionAtlasiQ9VT65. differential.
GenevisibleiQ9VT65. DM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Pka-C1P123702EBI-132069,EBI-82224

Protein-protein interaction databases

BioGridi64552. 8 interactions.
IntActiQ9VT65. 6 interactions.
MINTiMINT-819174.
STRINGi7227.FBpp0076072.

Structurei

3D structure databases

ProteinModelPortaliQ9VT65.
SMRiQ9VT65. Positions 245-923.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini259 – 558300Calpain catalyticPROSITE-ProRule annotationAdd
BLAST
Domaini796 – 83136EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini826 – 86136EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni559 – 728170Domain IIIAdd
BLAST
Regioni729 – 74820LinkerAdd
BLAST
Regioni749 – 925177Domain IVAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C2 family.Sequence analysis
Contains 1 calpain catalytic domain.PROSITE-ProRule annotation
Contains 2 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0045. Eukaryota.
ENOG410XP0B. LUCA.
GeneTreeiENSGT00760000118971.
InParanoidiQ9VT65.
KOiK08585.
OMAiFRAFQAF.
OrthoDBiEOG7RV9FM.
PhylomeDBiQ9VT65.

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. 2 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF49758. SSF49758. 1 hit.
PROSITEiPS50203. CALPAIN_CAT. 1 hit.
PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 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.

Q9VT65-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYGIDNYPKN YHASGIGLVN LAALGYSKNE VSGGNEGGGA PKPKAGLYPS
60 70 80 90 100
LPYPSSESVG GMPYVVKQTS HAQNASYAGP TMGMGMPVPE APSAPAPYPS
110 120 130 140 150
ATPYPGSGLY PSLPSANVSS LPYPTAPMAP YPTGMPYPTG MPQPNLPYPA
160 170 180 190 200
APLAPYPSAM PGLPGMPMPY APMPTSPAPQ HNIGFPALPY PTAPPPESAP
210 220 230 240 250
TQEEEPSVGV AELSFTSVKV PENQNMFWMG RKATSARQNS VSKGDFQSLR
260 270 280 290 300
DSCLANGTMF EDPDFPATNA SLMYSRRPDR YYEWLRPGDI ADDPQFFVEG
310 320 330 340 350
YSRFDVQQGE LGDCWLLAAA ANLTQDSTLF FRVIPPDQDF QENYAGIFHF
360 370 380 390 400
KFWQYGKWVE VVIDDRLPTY NGELIYMHST EKNEFWSALL EKAYAKLHGS
410 420 430 440 450
YEALKGGTTC EAMEDFTGGV TEWYDIKEAP PNLFSIMMKA AERGSMMGCS
460 470 480 490 500
LEPDPHVLEA ETPQGLIRGH AYSITKVCLM DISTPNRQGK LPMIRMRNPW
510 520 530 540 550
GNDAEWSGPW SDSSPEWRFI PEHTKEEIGL NFDRDGEFWM SFQDFLNHFD
560 570 580 590 600
RVEICNLSPD SLTEDQQHSS RRKWEMSMFE GEWTSGVTAG GCRNFLETFW
610 620 630 640 650
HNPQYIISLE DPDDEDDDGK CTAIVALMQK NRRSKRNVGI DCLTIGFAIY
660 670 680 690 700
HLTDRDMQVK PQGLNFFKYR ASVARSPHFI NTREVCARFK LPPGHYLIVP
710 720 730 740 750
STFDPNEEGE FIIRVFSETR NNMEENDDEV GFGETDDRIA PSLPPPTPKE
760 770 780 790 800
EDDPQRIALR RLFDSVAGSD EEVDWQELKR ILDHSMRDVM VGSDGFSKDA
810 820 830 840 850
VRSMVAMLDK DRSGRLGFEE FEALLTDIAK WRAVFKLYDT RRTGSIDGFH
860 870 880 890 900
LRGALNSAGY HLNNRLLNAL AHRYGSREGQ IPFDDFLMCA IKVRTFIEMF
910 920
RERDTDNSDT AFFNLDDWLE RTIYS
Length:925
Mass (Da):103,814
Last modified:October 1, 2002 - v2
Checksum:i3501F616AFC8F590
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti292 – 2921D → G in AAD04331 (PubMed:10446155).Curated
Sequence conflicti313 – 3131D → E in AAD04331 (PubMed:10446155).Curated
Sequence conflicti432 – 4321N → I in AAD04331 (PubMed:10446155).Curated
Sequence conflicti537 – 5371E → D in AAD04331 (PubMed:10446155).Curated
Sequence conflicti544 – 5441D → E in AAD04331 (PubMed:10446155).Curated
Sequence conflicti911 – 9122AF → GS in AAD04331 (PubMed:10446155).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062404 mRNA. Translation: AAD04331.2.
AE014296 Genomic DNA. Translation: AAF50189.2.
BT031259 mRNA. Translation: ABY20500.1.
RefSeqiNP_001246706.1. NM_001259777.2.
NP_524016.4. NM_079292.5.
UniGeneiDm.2874.

Genome annotation databases

EnsemblMetazoaiFBtr0076343; FBpp0076072; FBgn0025866.
FBtr0304675; FBpp0293217; FBgn0025866.
GeneIDi39165.
KEGGidme:Dmel_CG8107.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF062404 mRNA. Translation: AAD04331.2.
AE014296 Genomic DNA. Translation: AAF50189.2.
BT031259 mRNA. Translation: ABY20500.1.
RefSeqiNP_001246706.1. NM_001259777.2.
NP_524016.4. NM_079292.5.
UniGeneiDm.2874.

3D structure databases

ProteinModelPortaliQ9VT65.
SMRiQ9VT65. Positions 245-923.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64552. 8 interactions.
IntActiQ9VT65. 6 interactions.
MINTiMINT-819174.
STRINGi7227.FBpp0076072.

Protein family/group databases

MEROPSiC02.015.

Proteomic databases

PaxDbiQ9VT65.
PRIDEiQ9VT65.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0076343; FBpp0076072; FBgn0025866.
FBtr0304675; FBpp0293217; FBgn0025866.
GeneIDi39165.
KEGGidme:Dmel_CG8107.

Organism-specific databases

CTDi39165.
FlyBaseiFBgn0025866. CalpB.

Phylogenomic databases

eggNOGiKOG0045. Eukaryota.
ENOG410XP0B. LUCA.
GeneTreeiENSGT00760000118971.
InParanoidiQ9VT65.
KOiK08585.
OMAiFRAFQAF.
OrthoDBiEOG7RV9FM.
PhylomeDBiQ9VT65.

Enzyme and pathway databases

BRENDAi3.4.22.B37. 1994.

Miscellaneous databases

GenomeRNAii39165.
NextBioi812290.
PMAP-CutDBQ9VT65.
PROiQ9VT65.

Gene expression databases

BgeeiQ9VT65.
ExpressionAtlasiQ9VT65. differential.
GenevisibleiQ9VT65. DM.

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

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AUTOCATALYTIC CLEAVAGE.
    Tissue: Embryo1 Publication.
  2. "Autolytic activation and localization in Schneider cells (S2) of calpain B from Drosophila."
    Farkas A., Tompa P., Schad E., Sinka R., Jekely G., Friedrich P.
    Biochem. J. 378:299-305(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO N-TERMINUS, PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AUTOCATALYTIC CLEAVAGE, MUTAGENESIS OF 73-GLN--ALA-75 AND 223-ASN-GLN-224.
  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: Berkeley1 Publication.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiCANB_DROME
AccessioniPrimary (citable) accession number: Q9VT65
Secondary accession number(s): A9UN95, O96454
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: October 1, 2002
Last modified: May 11, 2016
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

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.