ID E9QE31_DANRE Unreviewed; 723 AA.
AC E9QE31; A0A8M1P227;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 2.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Calpain-3 {ECO:0000256|ARBA:ARBA00023844, ECO:0000256|RuleBase:RU367132};
DE EC=3.4.22.54 {ECO:0000256|ARBA:ARBA00023801, ECO:0000256|RuleBase:RU367132};
GN Name=capn3b {ECO:0000313|Ensembl:ENSDARP00000063176,
GN ECO:0000313|RefSeq:NP_001230250.1,
GN ECO:0000313|ZFIN:ZDB-GENE-041001-149};
GN Synonyms=si:dkey-12h9.9 {ECO:0000313|RefSeq:NP_001230250.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000063176};
RN [1] {ECO:0000313|Ensembl:ENSDARP00000063176}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000063176};
RG Ensembl;
RL Submitted (JUL-2011) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:NP_001230250.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001230250.1};
RX PubMed=23357851; DOI=10.1038/cr.2013.16;
RA Tao T., Shi H., Guan Y., Huang D., Chen Y., Lane D.P., Chen J., Peng J.;
RT "Def defines a conserved nucleolar pathway that leads p53 to proteasome-
RT independent degradation.";
RL Cell Res. 23:620-634(2013).
RN [3] {ECO:0000313|Ensembl:ENSDARP00000063176, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000063176};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [4] {ECO:0000313|RefSeq:NP_001230250.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001230250.1};
RX PubMed=27189481;
RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA Bobe J.;
RT "Gene evolution and gene expression after whole genome duplication in fish:
RT the PhyloFish database.";
RL BMC Genomics 17:368-368(2016).
RN [5] {ECO:0000313|RefSeq:NP_001230250.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001230250.1};
RX PubMed=26908177;
RA Bugel S.M., Wehmas L.C., La Du J.K., Tanguay R.L.;
RT "Phenotype anchoring in zebrafish reveals a potential role for matrix
RT metalloproteinases (MMPs) in tamoxifen's effects on skin epithelium.";
RL Toxicol. Appl. Pharmacol. 296:31-41(2016).
RN [6] {ECO:0000313|RefSeq:NP_001230250.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001230250.1};
RX PubMed=29751158;
RA Arcanjo C., Armant O., Floriani M., Cavalie I., Camilleri V., Simon O.,
RA Orjollet D., Adam-Guillermin C., Gagnaire B.;
RT "Tritiated water exposure disrupts myofibril structure and induces mis-
RT regulation of eye opacity and DNA repair genes in zebrafish early life
RT stages.";
RL Aquat. Toxicol. 200:114-126(2018).
RN [7] {ECO:0000313|RefSeq:NP_001230250.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001230250.1};
RX PubMed=29666124; DOI=10.1242/dmm.030056;
RA Kenyon A., Gavriouchkina D., Zorman J., Chong-Morrison V., Napolitani G.,
RA Cerundolo V., Sauka-Spengler T.;
RT "Generation of a double binary transgenic zebrafish model to study myeloid
RT gene regulation in response to oncogene activation in melanocytes. .";
RL Dis. Model. Mech. 11:dmm030056-dmm030056(2018).
RN [8] {ECO:0000313|RefSeq:NP_001230250.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001230250.1};
RX PubMed=30944473;
RA Ma Z., Zhu P., Shi H., Guo L., Zhang Q., Chen Y., Chen S., Zhang Z.,
RA Peng J., Chen J.;
RT "PTC-bearing mRNA elicits a genetic compensation response via Upf3a and
RT COMPASS components.";
RL Nature 568:259-263(2019).
RN [9] {ECO:0000313|RefSeq:NP_001230250.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001230250.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease.
CC {ECO:0000256|RuleBase:RU367132}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Broad endopeptidase activity.; EC=3.4.22.54;
CC Evidence={ECO:0000256|ARBA:ARBA00023702,
CC ECO:0000256|RuleBase:RU367132};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU367132}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU367132}. Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623, ECO:0000256|RuleBase:RU367132}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00239}.
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DR EMBL; AL954831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001230250.1; NM_001243321.1.
DR STRING; 7955.ENSDARP00000063176; -.
DR PeptideAtlas; E9QE31; -.
DR Ensembl; ENSDART00000063177; ENSDARP00000063176; ENSDARG00000043035.
DR Ensembl; ENSDART00000063177.6; ENSDARP00000063176.5; ENSDARG00000043035.7.
DR GeneID; 100034405; -.
DR KEGG; dre:100034405; -.
DR AGR; ZFIN:ZDB-GENE-041001-149; -.
DR CTD; 100034405; -.
DR ZFIN; ZDB-GENE-041001-149; capn3b.
DR HOGENOM; CLU_010982_0_1_1; -.
DR OMA; QFRVIYQ; -.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000000437; Alternate scaffold 20.
DR Proteomes; UP000000437; Chromosome 20.
DR Bgee; ENSDARG00000043035; Expressed in muscle tissue and 10 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; IDA:ZFIN.
DR GO; GO:1990092; P:calcium-dependent self proteolysis; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0030163; P:protein catabolic process; IDA:ZFIN.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00214; Calpain_III; 1.
DR CDD; cd00044; CysPc; 1.
DR CDD; cd16190; EFh_PEF_CAPN3; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.10.238.10; EF-hand; 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; IPR029531; CAPN3_PEF.
DR InterPro; IPR011992; EF-hand-dom_pair.
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 PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF329; CALPAIN-3; 1.
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; 3.
DR SUPFAM; SSF49758; Calpain large subunit, middle domain (domain III); 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|RuleBase:RU367132};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU367132};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU367132};
KW Metal-binding {ECO:0000256|RuleBase:RU367132};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU367132};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU367132}.
FT DOMAIN 65..360
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT DOMAIN 624..659
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 689..723
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT ACT_SITE 120
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1"
FT ACT_SITE 277
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1"
SQ SEQUENCE 723 AA; 83174 MW; 2EEC5DEE1CB803C9 CRC64;
MAEEQKFSET SVQLTEAAPQ TVGSGFTAPG NIYSAILSRN EAVKDARRLK DFQELRDKYV
RKKVLFEDPL FPAQDSSLFY SEKFPLKLEW KRPMEICKNP QFILGGANRT DICQGDLGDC
WLLAAIACLT LNDVILKRVV PHDQSFTENY AGIFHFQFWR YGEWVDVVID DRLPTYKNKL
VFTRSGQNNE FWSALMEKAY AKLHGSYEAL KGGNSLEAME DFTGGVTEFY EITEAPKELY
NIMRKALKRG SLMGCAIDTL VPTAQRTKTA SGLVRGHAYS VTGVEQGKRK DGKDLMIRLV
RVRDPWGVAP PPACKSNDWV ELAKTEQDKQ RLQPGEQGEF WMCFEEFQKN FTKLEICNLT
PDTLEDDQMF KWNVTVHEGR WVKGCSAGGC RNFPDTYWTN PQFRLVLLEA DAKEKTCTVV
VALMQKGRRV ERCSGATLHN IGFAIYEVPK EMKGNQQQQL SKDFFLYNAS TARSKSYVNI
REVTERFCLK PGEYVIIPST FDPHKESEFL LRVFSENRST SKVIDAEIEA EPMQVDNVKK
KIKPFEEEET EEEKQFRAIF QQIAGDDMEI NANELRTVLN RVVAKHKELK TEGFSLESCR
SMIALLDTDG TGHLNLQEFK HLWNKIKQWK LVFTRFDTDK SSTISSFEMR NALTEAGFQL
NNQLYDIICM RYANEHMELD FDSYISCLVR LEGMFRAFRA FDKDGDGLIK LNVFEWLQLT
MYA
//
