CAN10_MOUSE
ID CAN10_MOUSE Reviewed; 666 AA.
AC Q9ESK3; Q99J13; Q9WVF0;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 153.
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; Synonyms=Capn8;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11017071; DOI=10.1038/79876;
RA Horikawa Y., Oda N., Cox N.J., Li X., Orho-Melander M., Hara M.,
RA Hinokio Y., Lindner T.H., Mashima H., Schwarz P.E.H., del Bosque-Plata L.,
RA Horikawa Y., Oda Y., Yoshiuchi I., Colilla S., Polonsky K.S., Wei S.,
RA Concannon P., Iwasaki N., Schulze J., Baier L.J., Bogardus C., Groop L.,
RA Boerwinkle E., Hanis C.L., Bell G.I.;
RT "Genetic variation in the gene encoding calpain-10 is associated with type
RT 2 diabetes mellitus.";
RL Nat. Genet. 26:163-175(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=129/SvJ;
RA Horikawa Y., Ye H., Bell G.I.;
RT "Cloning of mouse protease gene.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Lung;
RA Braun C., Seifert M., Engel M., Welter C.;
RT "Identification of a new calpain-like cDNA in mouse lung.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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DR EMBL; AF089089; AAG17967.1; -; mRNA.
DR EMBL; AF203031; AAL54919.1; -; Genomic_DNA.
DR EMBL; AF126867; AAD41779.1; -; mRNA.
DR EMBL; AK088207; BAC40211.1; -; mRNA.
DR EMBL; BC005681; AAH05681.1; -; mRNA.
DR EMBL; BC010969; AAH10969.1; -; mRNA.
DR CCDS; CCDS15181.1; -.
DR RefSeq; NP_035926.2; NM_011796.2.
DR AlphaFoldDB; Q9ESK3; -.
DR SMR; Q9ESK3; -.
DR BioGRID; 204746; 2.
DR STRING; 10090.ENSMUSP00000027488; -.
DR MEROPS; C02.018; -.
DR iPTMnet; Q9ESK3; -.
DR PhosphoSitePlus; Q9ESK3; -.
DR PaxDb; Q9ESK3; -.
DR PRIDE; Q9ESK3; -.
DR ProteomicsDB; 265521; -.
DR Antibodypedia; 1333; 172 antibodies from 24 providers.
DR DNASU; 23830; -.
DR Ensembl; ENSMUST00000027488; ENSMUSP00000027488; ENSMUSG00000026270.
DR GeneID; 23830; -.
DR KEGG; mmu:23830; -.
DR UCSC; uc007cby.1; mouse.
DR CTD; 11132; -.
DR MGI; MGI:1344392; Capn10.
DR VEuPathDB; HostDB:ENSMUSG00000026270; -.
DR eggNOG; KOG0045; Eukaryota.
DR GeneTree; ENSGT00940000159706; -.
DR HOGENOM; CLU_010982_3_3_1; -.
DR InParanoid; Q9ESK3; -.
DR OMA; CYTQDVS; -.
DR OrthoDB; 704215at2759; -.
DR PhylomeDB; Q9ESK3; -.
DR TreeFam; TF314748; -.
DR BRENDA; 3.4.22.B30; 3474.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR BioGRID-ORCS; 23830; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Capn10; mouse.
DR PRO; PR:Q9ESK3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9ESK3; protein.
DR Bgee; ENSMUSG00000026270; Expressed in spermatocyte and 254 other tissues.
DR ExpressionAtlas; Q9ESK3; baseline and differential.
DR Genevisible; Q9ESK3; MM.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR GO; GO:0000149; F:SNARE binding; ISO:MGI.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:BHF-UCL.
DR GO; GO:0007568; P:aging; ISO:MGI.
DR GO; GO:0000422; P:autophagy of mitochondrion; ISO:MGI.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IMP:BHF-UCL.
DR GO; GO:0007005; P:mitochondrion organization; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0046326; P:positive regulation of glucose import; IMP:BHF-UCL.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISO:MGI.
DR GO; GO:0032388; P:positive regulation of intracellular transport; IMP:BHF-UCL.
DR GO; GO:2000676; P:positive regulation of type B pancreatic cell apoptotic process; IMP:MGI.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0031667; P:response to nutrient levels; ISO:MGI.
DR GO; GO:0097050; P:type B pancreatic cell apoptotic process; IMP:BHF-UCL.
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 Hydrolase; Protease; Reference proteome; Repeat; Thiol protease.
FT CHAIN 1..666
FT /note="Calpain-10"
FT /id="PRO_0000207727"
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"
FT CONFLICT 481
FT /note="S -> F (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 602..605
FT /note="YAQE -> TPRK (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 663
FT /note="V -> E (in Ref. 4; BAC40211)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 666 AA; 74596 MW; A0B1B37EE1DE2371 CRC64;
MRAVRAETPA RELFRDAAFP ASDSSLFYNL STPLAQFRED ITWRRPQEIC ATPQLFPDNP
WEGQVKQGLL GDCWFLCACA ALQKSQHLLD QVFPPGQPGW SDQKYQGFFT CRIWQFGHWE
EVTIDDRLPC LAGRLCFSRC QREDVFWLPL LEKAYAKVHG SYEHLWAGQV ADALVDLTGS
LAERWSLKDV TKASGQQDRP SGGEHRTCRQ LLHLKDRCLI SCSVLSPRAG ARELGEFHAF
IISDLQELRS QTGQGILLLR IHNPWGRRCW QGLWREGGEG WNQVEPAKES ELLAQLQEGE
FWVEEEEFLR EFDEVTIGYP VTEAGHLQSL HTERVLCHTR TLPGAWVTGQ SAGGCRNNSC
FPCNPKFWLR LLEPSEVCVA VLQRPRRRLV GQTRALAGAS PAPVNLPGKD YQAVGLHIWK
VEKRKISLPR VLSAPPVAGT ACHAYDREIH LRCELSPGYY LAVPSTFLKD VPGQFLLRVF
STGKISLSAV RLATKGASPG TALPAGEWET VQLQGCWRAG QTAGGSRNFA SYPCNPCLPF
SVPEGAGPRY IRITLQQHCR LSDSQLHPIG FHVFQVPADG ENQDACSLLL QEPLLSCVPH
RYAQEVSRLC LLSVGNYRIV PSTYLPDTEG TFTVTIATRI DRQSIHSQEM LGQLLQEVSF
MAVMKA
