CAN11_MOUSE
ID CAN11_MOUSE Reviewed; 714 AA.
AC Q6J756;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Calpain-11 {ECO:0000312|EMBL:AAT27434.1};
DE EC=3.4.22.-;
DE AltName: Full=Calcium-activated neutral proteinase 11 {ECO:0000250|UniProtKB:Q9UMQ6};
DE Short=CANP 11 {ECO:0000250|UniProtKB:Q9UMQ6};
GN Name=Capn11 {ECO:0000312|EMBL:AAT27434.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAT27434.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAT27434.1};
RC TISSUE=Testis {ECO:0000312|EMBL:AAT27434.1};
RX PubMed=16541461; DOI=10.1002/mrd.20466;
RA Ben-Aharon I., Brown P.R., Shalgi R., Eddy E.M.;
RT "Calpain 11 is unique to mouse spermatogenic cells.";
RL Mol. Reprod. Dev. 73:767-773(2006).
RN [2] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=10559499; DOI=10.1016/s0925-4773(99)00214-2;
RA Dear T.N., Boehm T.;
RT "Diverse mRNA expression patterns of the mouse calpain genes Capn5, Capn6
RT and Capn11 during development.";
RL Mech. Dev. 89:201-209(1999).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease which
CC catalyzes limited proteolysis of substrates involved in cytoskeletal
CC remodeling and signal transduction. {ECO:0000250|UniProtKB:Q9UMQ6}.
CC -!- SUBUNIT: Heterodimer of a large (catalytic) and a small (regulatory)
CC subunit. {ECO:0000250|UniProtKB:Q9UMQ6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome
CC {ECO:0000269|PubMed:16541461}.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in testis, where it is
CC restricted to spermatocytes and during the later stages of meiosis (at
CC protein level). {ECO:0000269|PubMed:10559499,
CC ECO:0000269|PubMed:16541461}.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000255}.
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DR EMBL; AY578330; AAT27434.1; -; mRNA.
DR CCDS; CCDS50121.1; -.
DR RefSeq; NP_001013789.1; NM_001013767.2.
DR AlphaFoldDB; Q6J756; -.
DR SMR; Q6J756; -.
DR STRING; 10090.ENSMUSP00000113132; -.
DR MEROPS; C02.013; -.
DR iPTMnet; Q6J756; -.
DR PhosphoSitePlus; Q6J756; -.
DR PaxDb; Q6J756; -.
DR PRIDE; Q6J756; -.
DR ProteomicsDB; 281762; -.
DR Antibodypedia; 4328; 176 antibodies from 26 providers.
DR DNASU; 268958; -.
DR Ensembl; ENSMUST00000120717; ENSMUSP00000113132; ENSMUSG00000058626.
DR GeneID; 268958; -.
DR KEGG; mmu:268958; -.
DR UCSC; uc008crh.1; mouse.
DR CTD; 11131; -.
DR MGI; MGI:1352490; Capn11.
DR VEuPathDB; HostDB:ENSMUSG00000058626; -.
DR eggNOG; KOG0045; Eukaryota.
DR GeneTree; ENSGT00940000158672; -.
DR HOGENOM; CLU_010982_0_1_1; -.
DR InParanoid; Q6J756; -.
DR OMA; KNWRLGQ; -.
DR OrthoDB; 704215at2759; -.
DR PhylomeDB; Q6J756; -.
DR TreeFam; TF314748; -.
DR BRENDA; 3.4.22.B31; 3474.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR BioGRID-ORCS; 268958; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Capn11; mouse.
DR PRO; PR:Q6J756; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q6J756; protein.
DR Bgee; ENSMUSG00000058626; Expressed in spermatocyte and 36 other tissues.
DR ExpressionAtlas; Q6J756; baseline and differential.
DR Genevisible; Q6J756; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasmic vesicle; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Repeat; Thiol protease.
FT CHAIN 1..714
FT /note="Calpain-11"
FT /id="PRO_0000356219"
FT DOMAIN 55..354
FT /note="Calpain catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT DOMAIN 586..621
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 623..651
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 355..527
FT /note="Domain III"
FT /evidence="ECO:0000250|UniProtKB:Q9UMQ6"
FT REGION 528..543
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:Q9UMQ6"
FT REGION 544..713
FT /note="Domain IV"
FT /evidence="ECO:0000250|UniProtKB:Q9UMQ6"
FT ACT_SITE 115
FT /evidence="ECO:0000255"
FT ACT_SITE 272
FT /evidence="ECO:0000255"
FT ACT_SITE 296
FT /evidence="ECO:0000255"
FT BINDING 599
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 601
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 603
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 605
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 610
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 629
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 631
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 633
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 635
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 640
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 714 AA; 82970 MW; FB65F4C3C2D9D09D CRC64;
MLNYSDISWA EKGMVATINH SRLKDKGVGQ HQNAYNYKNQ NYEDLRAECL RKGELFEDPF
FPAEPRSIGV KNLGPNSEHM QNIYWQRPKD IIHNPQFITN DFSPTDICQG ILGDCWLLAA
IGSLTTCPKL LYRVVPRNQS FKKNYAGIFH FQLWQFGHWL NVVVDDRLPT RNNKLVFVHA
SHRQDFWSAL LEKAYAKLIG SYGALSGGST LEGLEDFTGG VAQCIPLQKP PGNMLRLLKK
ALEKSSLMGC SIEVTDNSEV ETMTHNMLVR GHAYAVTGLE DVYYRDKLET LIRIQNPWGR
VEWNGAWSDK ATEWEEVSPD VRVQLLHKKD DGDFWMSYED FMSNFTLLEI CNLTPDALNT
WDYKSRWHST FYEGSWRRGS TAGGCRNHPE TFWSNPQFKI SLPEVDDPED DSEKNEMVCT
CLVALMQKNW RHAREGPQLL TIGFVIFSVP KEFQNLRDIH LKKDFFLKYR DHGFSEIFIN
SREVNSHLRL PPGEYVIIPS TYEPHKDADF LLRVFTEKHS ETWLLDDANR FEHLQEETVT
DKDLDKDSLQ LFKIMANEDG EVDMYALHKL LNRMTAKLRN FKTKGFSLEV CRRMINLLDK
DGSGKLELHE FQVLWKKIKK WTEIFKECDE DRSGNLNSYE MRLAIEKAGI KMNNRVTEVV
VARYSDNMIV DFDSFLNCFL RLKAMFAFFL SMDTKKTGSI CLDINQWLQI TMWG
