CAN13_MOUSE
ID CAN13_MOUSE Reviewed; 665 AA.
AC Q3UW68; B2RW21;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Calpain-13;
DE EC=3.4.22.-;
DE AltName: Full=Calcium-activated neutral proteinase 13;
DE Short=CANP 13;
GN Name=Capn13; Synonyms=Gm943;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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: Probable non-lysosomal thiol-protease. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
CC -!- CAUTION: It is unlikely that this protein binds calcium as none of the
CC 2 EF-hand domains seem to contain a canonical calcium-binding site.
CC {ECO:0000305}.
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DR EMBL; AK136569; BAE23051.1; -; mRNA.
DR EMBL; BC147510; AAI47511.1; -; mRNA.
DR EMBL; BC147512; AAI47513.1; -; mRNA.
DR CCDS; CCDS37690.1; -.
DR RefSeq; NP_001028616.1; NM_001033444.2.
DR AlphaFoldDB; Q3UW68; -.
DR SMR; Q3UW68; -.
DR BioGRID; 237788; 1.
DR STRING; 10090.ENSMUSP00000092832; -.
DR MEROPS; C02.020; -.
DR PhosphoSitePlus; Q3UW68; -.
DR MaxQB; Q3UW68; -.
DR PaxDb; Q3UW68; -.
DR PeptideAtlas; Q3UW68; -.
DR PRIDE; Q3UW68; -.
DR ProteomicsDB; 265431; -.
DR Antibodypedia; 28998; 83 antibodies from 22 providers.
DR Ensembl; ENSMUST00000095208; ENSMUSP00000092832; ENSMUSG00000043705.
DR GeneID; 381122; -.
DR KEGG; mmu:381122; -.
DR UCSC; uc008dnj.1; mouse.
DR CTD; 92291; -.
DR MGI; MGI:2685789; Capn13.
DR VEuPathDB; HostDB:ENSMUSG00000043705; -.
DR eggNOG; KOG0037; Eukaryota.
DR eggNOG; KOG0045; Eukaryota.
DR GeneTree; ENSGT00940000160921; -.
DR HOGENOM; CLU_010982_0_3_1; -.
DR InParanoid; Q3UW68; -.
DR OMA; SQHAYTV; -.
DR OrthoDB; 704215at2759; -.
DR PhylomeDB; Q3UW68; -.
DR TreeFam; TF314748; -.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR BioGRID-ORCS; 381122; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q3UW68; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q3UW68; protein.
DR Bgee; ENSMUSG00000043705; Expressed in epithelium of stomach and 16 other tissues.
DR Genevisible; Q3UW68; MM.
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:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00044; CysPc; 1.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR022682; Calpain_domain_III.
DR InterPro; IPR036213; Calpain_III_sf.
DR InterPro; IPR029544; CANP13.
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:SF333; PTHR10183:SF333; 1.
DR Pfam; PF01067; Calpain_III; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49758; SSF49758; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Protease; Reference proteome; Repeat; Thiol protease.
FT CHAIN 1..665
FT /note="Calpain-13"
FT /id="PRO_0000259583"
FT DOMAIN 30..329
FT /note="Calpain catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT DOMAIN 534..569
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 632..665
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT ACT_SITE 91
FT /evidence="ECO:0000250"
FT ACT_SITE 247
FT /evidence="ECO:0000250"
FT ACT_SITE 271
FT /evidence="ECO:0000250"
SQ SEQUENCE 665 AA; 76049 MW; 7C1AA17FD2D14D6F CRC64;
MAHDAETSVV KFKNQDFRTL RDHCLSRGQL FIDDTFPAAA SSIGEKLLRG KHLSKLEWKR
PTSKDLPFYP PHFILEGASR FDIHQGIAGD CWFLAALGSL TQNPQCLQKI LMDQSYSHQY
AGIFQFRFWQ CGQWVEVVID DQLPVIGDNF LFVHPRGGNK EFWPCLMEKA YAKLLGSYSQ
LHYGYLPDAL VDLTGGVVTI INLHSSPFDL LTTVKTAIQA GSMVACATEN GLTEEAKVME
NGLVSQHAYT VTGAEKIQYQ GRWEDIIRLW NPWGKTEWKG RWKDGSKEWR ETHDPRKSQL
YENKEDGEFW MSCQDFQENF SCLFICNQIP ITMDHGVTPN ESWRQMRFTN QVISRNRAGG
HGRDMQYVFS VQEHTAGNNV VVAFTIMPQS LNTEEERFPL QFQVFKVPQF QNVQGRLPPA
FFSPFRSAAQ GTKYVSKCNF TKSFHLNPGT YVVVTTANGK EVEFLLRIFL KMPDKHRDPS
SNFNLRALKE SLPENGSRNS ISYTYMDQGL DIDATQLQSL LNQEFLTGPP GDTFSLDQCQ
SIMALMDLKV NGRLDQEEFA RLRSRLIHCQ HIFQSIQRRP GVLLSSDLWK VIENTDFLVG
IFISSELLSL MALRYSDSSG RVSFPTLVCF LIRLETMAKA FRNLSKDGKG IYLTETEWMN
LVMYS
