CAND_DROME
ID CAND_DROME Reviewed; 1594 AA.
AC P27398; O61346; Q7KU57; Q7KU58; Q8MQP3; Q9VRH3; Q9VRH4;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Calpain-D;
DE EC=3.4.22.-;
DE AltName: Full=Calcium-activated neutral proteinase D;
DE Short=CANP D;
DE AltName: Full=Small optic lobes protein;
GN Name=sol; Synonyms=CalpD; ORFNames=CG1391;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=Canton-S; TISSUE=Brain;
RX PubMed=1714593; DOI=10.1073/pnas.88.16.7214;
RA Delaney S.J., Hayward D.C., Barleben F., Fischbach K.-F., Miklos G.L.G.;
RT "Molecular cloning and analysis of small optic lobes, a structural brain
RT gene of Drosophila melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:7214-7218(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM B).
RC STRAIN=Canton-S;
RX PubMed=9144213; DOI=10.1073/pnas.94.10.5189;
RA Miklos G.L., Yamamoto M.-T., Burns R.G., Maleszka R.;
RT "An essential cell division gene of Drosophila, absent from Saccharomyces,
RT encodes an unusual protein with tubulin-like and myosin-like peptide
RT motifs.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:5189-5194(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Embryo;
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).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Has a role in eye development. {ECO:0000269|PubMed:1714593}.
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=B {ECO:0000312|FlyBase:FBgn0003464};
CC IsoId=P27398-1; Sequence=Displayed;
CC Name=A {ECO:0000312|FlyBase:FBgn0003464};
CC IsoId=P27398-2; Sequence=VSP_011791, VSP_005246;
CC Name=E {ECO:0000312|FlyBase:FBgn0003464};
CC IsoId=P27398-5; Sequence=VSP_058143;
CC -!- DEVELOPMENTAL STAGE: Present throughout development, with expression
CC levels lower in larvae than other life stages.
CC {ECO:0000269|PubMed:1714593}.
CC -!- DISRUPTION PHENOTYPE: Mutants cause specific cells to degenerate in the
CC developing optic lobes, resulting in the absence of certain classes of
CC columnar neurons. {ECO:0000269|PubMed:1714593}.
CC -!- MISCELLANEOUS: Although homology to other calpains is high within the
CC protease domain, the lack of calcium-binding sites suggests that this
CC protein is a protease that may not be activated by calcium ions.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS65411.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M64084; AAB95431.1; -; mRNA.
DR EMBL; AF017777; AAC28409.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF50826.4; -; Genomic_DNA.
DR EMBL; AE014298; AAF50827.3; -; Genomic_DNA.
DR EMBL; AE014298; AAS65411.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AY128468; AAM75061.1; -; mRNA.
DR PIR; A41146; BVFFSL.
DR PIR; T08428; T08428.
DR RefSeq; NP_476737.3; NM_057389.6. [P27398-2]
DR RefSeq; NP_476738.3; NM_057390.6. [P27398-1]
DR RefSeq; NP_996524.2; NM_206801.3.
DR AlphaFoldDB; P27398; -.
DR SMR; P27398; -.
DR BioGRID; 68777; 75.
DR IntAct; P27398; 14.
DR STRING; 7227.FBpp0088620; -.
DR MEROPS; C02.010; -.
DR iPTMnet; P27398; -.
DR PaxDb; P27398; -.
DR PRIDE; P27398; -.
DR DNASU; 44014; -.
DR EnsemblMetazoa; FBtr0089678; FBpp0088620; FBgn0003464. [P27398-1]
DR EnsemblMetazoa; FBtr0089679; FBpp0088621; FBgn0003464. [P27398-2]
DR EnsemblMetazoa; FBtr0301583; FBpp0290798; FBgn0003464. [P27398-5]
DR GeneID; 44014; -.
DR KEGG; dme:Dmel_CG1391; -.
DR CTD; 44014; -.
DR FlyBase; FBgn0003464; sol.
DR VEuPathDB; VectorBase:FBgn0003464; -.
DR eggNOG; KOG0045; Eukaryota.
DR GeneTree; ENSGT00940000158312; -.
DR InParanoid; P27398; -.
DR PhylomeDB; P27398; -.
DR BRENDA; 3.4.22.B35; 1994.
DR SignaLink; P27398; -.
DR BioGRID-ORCS; 44014; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 44014; -.
DR PRO; PR:P27398; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003464; Expressed in secondary oocyte and 23 other tissues.
DR ExpressionAtlas; P27398; baseline and differential.
DR Genevisible; P27398; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd00044; CysPc; 1.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR Pfam; PF00648; Peptidase_C2; 1.
DR Pfam; PF00641; zf-RanBP; 6.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00230; CysPc; 1.
DR SMART; SM00547; ZnF_RBZ; 6.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF90209; SSF90209; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 5.
DR PROSITE; PS50199; ZF_RANBP2_2; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Hydrolase; Metal-binding;
KW Phosphoprotein; Protease; Reference proteome; Repeat; Sensory transduction;
KW Thiol protease; Vision; Zinc; Zinc-finger.
FT CHAIN 1..1594
FT /note="Calpain-D"
FT /id="PRO_0000207733"
FT DOMAIN 1014..1321
FT /note="Calpain catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT ZN_FING 1..35
FT /note="RanBP2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 135..164
FT /note="RanBP2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 643..673
FT /note="RanBP2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 704..733
FT /note="RanBP2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 744..774
FT /note="RanBP2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 927..956
FT /note="RanBP2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 210..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1079
FT /evidence="ECO:0000250"
FT ACT_SITE 1245
FT /evidence="ECO:0000250"
FT ACT_SITE 1265
FT /evidence="ECO:0000250"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 394..395
FT /note="VS -> YA (in isoform A)"
FT /evidence="ECO:0000303|PubMed:1714593"
FT /id="VSP_011791"
FT VAR_SEQ 396..1594
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:1714593"
FT /id="VSP_005246"
FT VAR_SEQ 701
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000305"
FT /id="VSP_058143"
FT CONFLICT 384
FT /note="Q -> H (in Ref. 1; AAB95431)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="A -> G (in Ref. 1; AAB95431)"
FT /evidence="ECO:0000305"
FT CONFLICT 679
FT /note="Q -> H (in Ref. 1; AAB95431)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="H -> HHHH (in Ref. 1; AAB95431 and 2; AAC28409)"
FT /evidence="ECO:0000305"
FT CONFLICT 836
FT /note="Q -> R (in Ref. 5; AAM75061)"
FT /evidence="ECO:0000305"
FT CONFLICT 915
FT /note="A -> G (in Ref. 2; AAC28409)"
FT /evidence="ECO:0000305"
FT CONFLICT 928
FT /note="T -> S (in Ref. 1; AAB95431 and 2; AAC28409)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1594 AA; 174313 MW; 1CDDE8090B5DA198 CRC64;
MGTISSVLQW SCTKCNTINP TESLKCFNCG TVRKVFPQQQ QQQHRSSSIT ASWTADDALE
QEQAEKGQER DKEKGRAAVA RSEYKHVYKS LLRGCLKRPQ RNSQNLPANC VDCEDTRKYI
KSSIELYRHF SNPALNRRWV CHACGTDNSS VTWHCLICDT VSYLAPIYKD AIAADRGQDL
AGSLGNRGEL LAADHSHPHH HHHYLHQELE EQHQHQLHSQ HLHKRHLKGR SASGSGSGPG
SGSGLRRTQS LSTAIDKSAS GRSCHICYAN NQSKDIFNLP QIKPAPQLTG IPPVAACSNS
RFAIANDTFC RRKQNNNNKN QNHKVVRESG AKRKYNFTIT TLSRSAAKDA GHGQMKPLRQ
VVNLNLNLQQ EPQQKSPANP QQLQRKTQRE PAAVSMNPTQ FTIPRNGVFI AVNEWSEPMA
SSSSVSSSSN HHHHHHSNSN SNSSGNSNII NNNSSSSSGS NKLYENECVA LAQQQLRAAA
AQAAQAAATA VAIASSPSAK AMAEPAPTAT MPIYAQVNKQ HKLKKKQQIA SESQTNNNTG
SGEIADAVSE SLTAGLGTST DGSGEASESE SQVEEHSIYA KVWKGPRKAT ESKIMHDPGS
SSRLSGAASA AAGTASAGAI AAAVGAAAAS RHDNKTQLGN GSRSKMWICI KCSYAYNRLW
LQTCEMCEAK AEQQQQQLQL QQQQQQQQQH HHHHLQQQQA EAPRDEPWTC KKCTLVNYST
AMACVVCGGS KLKSISSIED MTLRKGEFWT CSHCTLKNSL HSPVCSACKS HRQPQLSMAM
EAVRERPDGQ SYEEQDAAAV GGGGGSAHQS GANEVKAPTA LNLPLTSVAL PMPMLQLPTS
TAAGLRGSRS PSPRMQLLPS LQQQRNSSSS GAIPKRHSTG GSIVPRNISI AGLANYNLQQ
GQGVGSASVV SASGAGSGAG AVGASTSTKK WQCPACTYDN CAASVVCDIC SSPRGLASAV
LGEALGRKSV RVALTPADIR QESKLMENLR QLEETEALTK WQNIIQYCRD NSELFVDDSF
PPAPKSLYYN PASGAGEGNP VVQWRRPHEI NCDGGAYPPW AVFRTPLPSD ICQGVLGNCW
LLSALAVLAE REDLVKEVLV TKEICGQGAY QVRLCKDGKW TTVLVDDLLP CDKRGHLVYS
QAKRKQLWVP LIEKAVAKIH GCYEALVSGR AIEGLATLTG APCESIPLQA SSLPMPSEDE
LDKDLIWAQL LSSRCVRFLM GASCGGGNMK VDEEEYQQKG LRPRHAYSVL DVKDIQGHRL
LKLRNPWGHY SWRGDWSDDS SLWTDDLRDA LMPHGASEGV FWISFEDVLN YFDCIDICKV
RSGWNEVRLQ GTLQPLCSIS CVLLTVLEPT EAEFTLFQEG QRNSEKSQRS QLDLCVVIFR
TRSPAAPEIG RLVEHSKRQV RGFVGCHKML ERDIYLLVCL AFNHWHTGIE DPHQYPQCIL
AIHSSKRLLV EQISPSPHLL ADAIISLTLT KGQRHEGREG MTAYYLTKGW AGLVVMVENR
HENKWIHVKC DCQESYNVVS TRGELKTVDS VPPLQRQVII VLTQLEGSGG FSIAHRLTHR
LANSRGLHDW GPPGATHCPP IENVHGLHAP RLIT
