CAN10_RAT
ID CAN10_RAT Reviewed; 666 AA.
AC Q9ES66;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Calpain-10;
DE EC=3.4.22.-;
DE AltName: Full=Calcium-activated neutral proteinase 10;
DE Short=CANP 10;
GN Name=Capn10;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=11375982; DOI=10.1074/jbc.m100603200;
RA Ma H., Fukiage C., Kim Y.H., Duncan M.K., Reed N.A., Shih M., Azuma M.,
RA Shearer T.R.;
RT "Characterization and expression of calpain 10. A novel ubiquitous calpain
RT with nuclear localization.";
RL J. Biol. Chem. 276:28525-28531(2001).
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease which
CC catalyzes limited proteolysis of substrates involved in cytoskeletal
CC remodeling and signal transduction. May play a role in insulin-
CC stimulated glucose uptake (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11375982}.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF227909; AAG09736.3; -; mRNA.
DR RefSeq; NP_113861.1; NM_031673.2.
DR AlphaFoldDB; Q9ES66; -.
DR SMR; Q9ES66; -.
DR STRING; 10116.ENSRNOP00000067567; -.
DR ChEMBL; CHEMBL6130; -.
DR MEROPS; C02.018; -.
DR PaxDb; Q9ES66; -.
DR PRIDE; Q9ES66; -.
DR GeneID; 63834; -.
DR KEGG; rno:63834; -.
DR CTD; 11132; -.
DR RGD; 69354; Capn10.
DR eggNOG; KOG0045; Eukaryota.
DR InParanoid; Q9ES66; -.
DR OrthoDB; 704215at2759; -.
DR PhylomeDB; Q9ES66; -.
DR BRENDA; 3.4.22.B30; 5301.
DR Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
DR PRO; PR:Q9ES66; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005938; C:cell cortex; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005856; C:cytoskeleton; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:RGD.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IDA:RGD.
DR GO; GO:0008092; F:cytoskeletal protein binding; IDA:BHF-UCL.
DR GO; GO:0000149; F:SNARE binding; IDA:BHF-UCL.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:RGD.
DR GO; GO:0007568; P:aging; IDA:RGD.
DR GO; GO:0000422; P:autophagy of mitochondrion; IMP:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:RGD.
DR GO; GO:0007005; P:mitochondrion organization; IMP:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0046326; P:positive regulation of glucose import; ISO:RGD.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISO:RGD.
DR GO; GO:0032388; P:positive regulation of intracellular transport; ISO:RGD.
DR GO; GO:2000676; P:positive regulation of type B pancreatic cell apoptotic process; ISO:RGD.
DR GO; GO:0030163; P:protein catabolic process; IDA:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR GO; GO:0009749; P:response to glucose; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IDA:RGD.
DR GO; GO:0097050; P:type B pancreatic cell apoptotic process; ISO:RGD.
DR CDD; cd00214; Calpain_III; 2.
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; IPR028791; CAPN10.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR PANTHER; PTHR10183:SF30; PTHR10183:SF30; 1.
DR Pfam; PF01067; Calpain_III; 2.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00720; calpain_III; 2.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF49758; SSF49758; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Nucleus; Protease; Reference proteome; Repeat;
KW Thiol protease.
FT CHAIN 1..666
FT /note="Calpain-10"
FT /id="PRO_0000207728"
FT DOMAIN 13..321
FT /note="Calpain catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT REGION 322..488
FT /note="Domain III 1"
FT REGION 507..648
FT /note="Domain III 2"
FT ACT_SITE 73
FT /evidence="ECO:0000250"
FT ACT_SITE 238
FT /evidence="ECO:0000250"
FT ACT_SITE 263
FT /evidence="ECO:0000250"
SQ SEQUENCE 666 AA; 74527 MW; A92263A9C8C4947D CRC64;
MRAVRAETRA RELFRDAAFP ASDSSLFYNL STPLAQFRED ITWRRPQDIC ATPQLFPDNP
WEGQVKQGLL GDCWFLCACA ALQKSRHLLD QVFPPGQPGW SDQEYQGFFT CRIWQFGHWE
EVTIDDRLPC LAGRLCFSRC QREDVFWLPL LEKAYAKVHG SYEHLWAGQV ADALVDLTGS
LAERWSLKDI RKASGQQDRP SGGEHRACQQ LLRLKDQCLL SCSVLSPRAG ARELGEFHAF
IISDLQELRS QTGQGILLLR IHNPWGRRCW QGLWREGGEG WNQVEPAKES ELLAQLQEGE
FWVEEEEFLR EFDEVTIGYP VTEAGHLQSL YTEKVLCHTR ALPGAWVTGQ SAGGCRNNSC
FPCNPKFWLR LLEPSEVCVA VLQRPRRRLV GQTRALAGAS PAPVNLPGKD YQAVGLHIWK
VEKRKISLPR VLSAPPVAGT ACHAYDREIH LRCELSPGYY LAVPSTFLKD VPGQFLLRVF
STGKISLSAV RLATKGASPG AALPAGEWET VQLQGSWRAG QTAGGSRNFA SYPCNPCLPF
SVPEGAGPRY IRITLQQHCR LSDSQLHPIG FHVFQVPADG EKQDACSLLL QEPLLSCVPH
CYAQEVSRLC LLSAGNYRIV PSTYLPDTEG TFTVTIATRI DRQSIHSQEM LGQLLQEVSF
MAVMKA
