CANC_DROME
ID CANC_DROME Reviewed; 681 AA.
AC Q9VXH6; Q86NA1; Q95R89;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 4.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Calpain-C;
DE AltName: Full=Calcium-activated neutral proteinase homolog C;
DE Short=CANP C;
GN Name=CalpC {ECO:0000312|EMBL:AAF48591.2}; ORFNames=CG3692;
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:CAD61271.1}
RP NUCLEOTIDE SEQUENCE [MRNA], LACK OF CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12646209; DOI=10.1016/s0006-291x(03)00350-4;
RA Spadoni C., Farkas A., Sinka R., Tompa P., Friedrich P.;
RT "Molecular cloning and RNA expression of a novel Drosophila calpain,
RT Calpain C.";
RL Biochem. Biophys. Res. Commun. 303:343-349(2003).
RN [2] {ECO:0000312|EMBL:AAF48591.2}
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAF48591.2}
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAL29115.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Not known; does not seem to have protease activity.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12646209}.
CC -!- TISSUE SPECIFICITY: Localized to the salivary glands in the larva.
CC {ECO:0000269|PubMed:12646209}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development, with expression
CC highest in the pupa. {ECO:0000269|PubMed:12646209}.
CC -!- MISCELLANEOUS: Although strongly related to peptidase C2 proteins, it
CC lack the essential Cys, His and Asn residues of the catalytic triad at
CC positions 84, 242 and 267, respectively.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000255}.
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DR EMBL; AJ538040; CAD61271.1; -; mRNA.
DR EMBL; AE014298; AAF48591.2; -; Genomic_DNA.
DR EMBL; AY061567; AAL29115.1; -; mRNA.
DR RefSeq; NP_573118.2; NM_132890.3.
DR AlphaFoldDB; Q9VXH6; -.
DR SMR; Q9VXH6; -.
DR BioGRID; 58937; 3.
DR IntAct; Q9VXH6; 4.
DR MINT; Q9VXH6; -.
DR STRING; 7227.FBpp0074005; -.
DR PaxDb; Q9VXH6; -.
DR PRIDE; Q9VXH6; -.
DR EnsemblMetazoa; FBtr0074226; FBpp0074005; FBgn0260450.
DR GeneID; 32597; -.
DR KEGG; dme:Dmel_CG3692; -.
DR CTD; 32597; -.
DR FlyBase; FBgn0260450; CalpC.
DR VEuPathDB; VectorBase:FBgn0260450; -.
DR eggNOG; KOG0045; Eukaryota.
DR HOGENOM; CLU_010982_0_1_1; -.
DR InParanoid; Q9VXH6; -.
DR OMA; ASNCFWA; -.
DR OrthoDB; 704215at2759; -.
DR PhylomeDB; Q9VXH6; -.
DR BRENDA; 3.4.22.B38; 1994.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR SignaLink; Q9VXH6; -.
DR BioGRID-ORCS; 32597; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 32597; -.
DR PRO; PR:Q9VXH6; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0260450; Expressed in wing disc and 22 other tissues.
DR ExpressionAtlas; Q9VXH6; baseline and differential.
DR Genevisible; Q9VXH6; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; IPR002048; EF_hand_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
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 SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49758; SSF49758; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Metal-binding; Reference proteome.
FT CHAIN 1..681
FT /note="Calpain-C"
FT /id="PRO_0000207732"
FT DOMAIN 18..331
FT /note="Calpain catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT DOMAIN 552..587
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 332..481
FT /note="Domain III"
FT REGION 482..514
FT /note="Linker"
FT REGION 515..681
FT /note="Domain IV"
FT BINDING 565
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 567
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 569
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 571
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="S -> T (in Ref. 1; CAD61271 and 4; AAL29115)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="S -> A (in Ref. 1; CAD61271 and 4; AAL29115)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="N -> Y (in Ref. 4; AAL29115)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="M -> T (in Ref. 4; AAL29115)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 681 AA; 77448 MW; 67B4FDD05122E9D3 CRC64;
MASKYERILS DCRSKNVLWE DPDFPAVQSS VFYYQTPPFT FQWKRIMDLA DSGSGAVAAN
SSAAPVFLNE SAEFDVVPGK MGDRWLVSCL GLLSSLRNLF YRVVPADQTL ASAHGVFRFR
LWWCGEWVEV LVDDRLPTIN GRLAFMQPQA SNCFWAALLE KAIAKLHGSY EALKYGTRSD
GLTDLLGGVV RQMPILSDNI RPQTLKELLT TTCIVTCLAD KSATVAKKNL AERMPNGILV
NVNYRLSSLD KVKTLMGDSV QLVCLKDTFS SKPFGEKTHF LGDWSPMSKT WERVSQVERA
RLIRQLGPGE FWLSFCDFVE IFSTMEVVYL DTETSNDEEM LKSRPLHWKM KMHQGQWKRG
VTAGGCRNHE SFHINPQLLI SVQDEQDLVI ALNQHTAVEP KVIGFTMYTW DGEYMLSECL
QKDFFKNHVS YLNSDYGNTR HVSYHTHLEA GHYVLIPTTY EPAEEAHFTV RILGTGSFRL
SCLETQTMIL LDPFPALKST DAERCGGPKV KSVCQYEPVY MQLADENKTI NCFELHELLE
ACLPNDYIKG CANIDICRQV IALQDRSGSG RITFQQFKTF MVNLKSWQGV FKMYTKEKAG
ILRAERLRDA LCDIGFQLST DIMNCLIQRY IRKDGTLRLS DFVSAVIHLT TAFNQFHLKN
YGQVNVIEVH LHDWIKSILS C
