CANB_DROME
ID CANB_DROME Reviewed; 925 AA.
AC Q9VT65; A9UN95; O96454;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Calpain-B;
DE EC=3.4.22.-;
DE AltName: Full=Calcium-activated neutral proteinase B;
DE Short=CANP B;
DE Contains:
DE RecName: Full=Calpain-B catalytic subunit 1;
DE Contains:
DE RecName: Full=Calpain-B catalytic subunit 2;
GN Name=CalpB {ECO:0000312|EMBL:AAF50189.2, ECO:0000312|FlyBase:FBgn0025866};
GN ORFNames=CG8107;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAD04331.2}
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, AND AUTOCATALYTIC CLEAVAGE.
RC TISSUE=Embryo {ECO:0000269|PubMed:10446155};
RX PubMed=10446155; DOI=10.1074/jbc.274.34.23893;
RA Jekely G., Friedrich P.;
RT "Characterization of two recombinant Drosophila calpains. CALPA and a novel
RT homolog, CALPB.";
RL J. Biol. Chem. 274:23893-23900(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAD04331.2}
RP SEQUENCE REVISION TO N-TERMINUS, PARTIAL PROTEIN SEQUENCE, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AUTOCATALYTIC CLEAVAGE,
RP AND MUTAGENESIS OF 73-GLN--ALA-75 AND 223-ASN-GLN-224.
RX PubMed=14614768; DOI=10.1042/bj20031310;
RA Farkas A., Tompa P., Schad E., Sinka R., Jekely G., Friedrich P.;
RT "Autolytic activation and localization in Schneider cells (S2) of calpain B
RT from Drosophila.";
RL Biochem. J. 378:299-305(2004).
RN [3] {ECO:0000312|EMBL:AAF50189.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAF50189.2}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease.
CC {ECO:0000269|PubMed:10446155}.
CC -!- ACTIVITY REGULATION: Activated by millimolar concentrations of calcium.
CC {ECO:0000269|PubMed:10446155}.
CC -!- INTERACTION:
CC Q9VT65; P12370: Pka-C1; NbExp=2; IntAct=EBI-132069, EBI-82224;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14614768}. Membrane
CC {ECO:0000269|PubMed:14614768}. Note=Translocates to intracellular
CC membranes when calcium levels are increased.
CC -!- TISSUE SPECIFICITY: Strongly expressed in follicular and border cells
CC of the oocyte. Ubiquitously expressed in early embryos. Localized to
CC the trachea and their orifices, and to the larynx of late embryos.
CC Restricted to the salivary gland in third instar larvae.
CC {ECO:0000269|PubMed:14614768}.
CC -!- DEVELOPMENTAL STAGE: Expressed in all developmental stages, with
CC highest expression in the egg, probably of maternal origin. Very low
CC expression in the early larva, rising through larval development up to
CC the third larval stage. Constant expression in the pupa and adult.
CC {ECO:0000269|PubMed:14614768}.
CC -!- PTM: Undergoes calcium-dependent autolytic cleavage between Asn-74 and
CC Ala-75 and between Gln-224 and Asn-225 to produce two major products,
CC calpain B catalytic subunit 1 and calpain B catalytic subunit 2. This
CC autolysis is necessary for activation of the protein.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000255}.
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DR EMBL; AF062404; AAD04331.2; -; mRNA.
DR EMBL; AE014296; AAF50189.2; -; Genomic_DNA.
DR EMBL; BT031259; ABY20500.1; -; mRNA.
DR RefSeq; NP_001246706.1; NM_001259777.2.
DR RefSeq; NP_524016.4; NM_079292.5.
DR AlphaFoldDB; Q9VT65; -.
DR SMR; Q9VT65; -.
DR BioGRID; 64552; 14.
DR IntAct; Q9VT65; 6.
DR MINT; Q9VT65; -.
DR STRING; 7227.FBpp0076072; -.
DR MEROPS; C02.015; -.
DR PaxDb; Q9VT65; -.
DR PRIDE; Q9VT65; -.
DR EnsemblMetazoa; FBtr0076343; FBpp0076072; FBgn0025866.
DR EnsemblMetazoa; FBtr0304675; FBpp0293217; FBgn0025866.
DR GeneID; 39165; -.
DR KEGG; dme:Dmel_CG8107; -.
DR CTD; 39165; -.
DR FlyBase; FBgn0025866; CalpB.
DR VEuPathDB; VectorBase:FBgn0025866; -.
DR eggNOG; KOG0045; Eukaryota.
DR GeneTree; ENSGT00940000170528; -.
DR HOGENOM; CLU_010982_2_0_1; -.
DR InParanoid; Q9VT65; -.
DR OMA; ICEDPQF; -.
DR OrthoDB; 704215at2759; -.
DR PhylomeDB; Q9VT65; -.
DR BRENDA; 3.4.22.B37; 1994.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR SignaLink; Q9VT65; -.
DR BioGRID-ORCS; 39165; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39165; -.
DR PRO; PR:Q9VT65; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0025866; Expressed in spermathecum and 30 other tissues.
DR ExpressionAtlas; Q9VT65; baseline and differential.
DR Genevisible; Q9VT65; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0016322; P:neuron remodeling; IMP:FlyBase.
DR GO; GO:0016540; P:protein autoprocessing; IDA:FlyBase.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR CDD; cd00214; Calpain_III; 1.
DR CDD; cd00044; CysPc; 1.
DR InterPro; IPR033883; C2_III.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR022682; Calpain_domain_III.
DR InterPro; IPR022683; Calpain_III.
DR InterPro; IPR036213; Calpain_III_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR Pfam; PF01067; Calpain_III; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00720; calpain_III; 1.
DR SMART; SM00230; CysPc; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49758; SSF49758; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; Calcium; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Membrane; Metal-binding; Protease; Reference proteome; Repeat;
KW Thiol protease.
FT CHAIN 1..925
FT /note="Calpain-B"
FT /id="PRO_0000026499"
FT CHAIN 75..925
FT /note="Calpain-B catalytic subunit 1"
FT /id="PRO_0000026500"
FT CHAIN 225..925
FT /note="Calpain-B catalytic subunit 2"
FT /id="PRO_0000026501"
FT DOMAIN 259..558
FT /note="Calpain catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT DOMAIN 796..831
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 826..861
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 559..728
FT /note="Domain III"
FT REGION 723..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..748
FT /note="Linker"
FT REGION 749..925
FT /note="Domain IV"
FT ACT_SITE 314
FT /evidence="ECO:0000250|UniProtKB:Q07009"
FT ACT_SITE 470
FT /evidence="ECO:0000250|UniProtKB:Q07009"
FT ACT_SITE 498
FT /evidence="ECO:0000250|UniProtKB:Q07009"
FT BINDING 809
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 811
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 813
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 815
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 820
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 839
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 843
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 845
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 850
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT SITE 74..75
FT /note="Cleavage; by autolysis"
FT SITE 224..225
FT /note="Cleavage; by autolysis"
FT MUTAGEN 73..75
FT /note="QNA->GVP: Autolysis site shifted to nearby, less-
FT active sites."
FT /evidence="ECO:0000269|PubMed:14614768"
FT MUTAGEN 223..224
FT /note="NQ->AV: Autolysis site shifted to nearby, less-
FT active site(s)."
FT /evidence="ECO:0000269|PubMed:14614768"
FT CONFLICT 292
FT /note="D -> G (in Ref. 1; AAD04331)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="D -> E (in Ref. 1; AAD04331)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="N -> I (in Ref. 1; AAD04331)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="E -> D (in Ref. 1; AAD04331)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="D -> E (in Ref. 1; AAD04331)"
FT /evidence="ECO:0000305"
FT CONFLICT 911..912
FT /note="AF -> GS (in Ref. 1; AAD04331)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 925 AA; 103814 MW; 3501F616AFC8F590 CRC64;
MYGIDNYPKN YHASGIGLVN LAALGYSKNE VSGGNEGGGA PKPKAGLYPS LPYPSSESVG
GMPYVVKQTS HAQNASYAGP TMGMGMPVPE APSAPAPYPS ATPYPGSGLY PSLPSANVSS
LPYPTAPMAP YPTGMPYPTG MPQPNLPYPA APLAPYPSAM PGLPGMPMPY APMPTSPAPQ
HNIGFPALPY PTAPPPESAP TQEEEPSVGV AELSFTSVKV PENQNMFWMG RKATSARQNS
VSKGDFQSLR DSCLANGTMF EDPDFPATNA SLMYSRRPDR YYEWLRPGDI ADDPQFFVEG
YSRFDVQQGE LGDCWLLAAA ANLTQDSTLF FRVIPPDQDF QENYAGIFHF KFWQYGKWVE
VVIDDRLPTY NGELIYMHST EKNEFWSALL EKAYAKLHGS YEALKGGTTC EAMEDFTGGV
TEWYDIKEAP PNLFSIMMKA AERGSMMGCS LEPDPHVLEA ETPQGLIRGH AYSITKVCLM
DISTPNRQGK LPMIRMRNPW GNDAEWSGPW SDSSPEWRFI PEHTKEEIGL NFDRDGEFWM
SFQDFLNHFD RVEICNLSPD SLTEDQQHSS RRKWEMSMFE GEWTSGVTAG GCRNFLETFW
HNPQYIISLE DPDDEDDDGK CTAIVALMQK NRRSKRNVGI DCLTIGFAIY HLTDRDMQVK
PQGLNFFKYR ASVARSPHFI NTREVCARFK LPPGHYLIVP STFDPNEEGE FIIRVFSETR
NNMEENDDEV GFGETDDRIA PSLPPPTPKE EDDPQRIALR RLFDSVAGSD EEVDWQELKR
ILDHSMRDVM VGSDGFSKDA VRSMVAMLDK DRSGRLGFEE FEALLTDIAK WRAVFKLYDT
RRTGSIDGFH LRGALNSAGY HLNNRLLNAL AHRYGSREGQ IPFDDFLMCA IKVRTFIEMF
RERDTDNSDT AFFNLDDWLE RTIYS
