CAN9_MOUSE
ID CAN9_MOUSE Reviewed; 690 AA.
AC Q9D805; E9QNM7; O35919;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Calpain-9;
DE EC=3.4.22.-;
DE AltName: Full=Digestive tract-specific calpain;
DE AltName: Full=New calpain 4;
DE Short=nCL-4;
GN Name=Capn9; Synonyms=Ncl4;
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=Stomach;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-690.
RC STRAIN=BALB/cJ;
RX PubMed=9524069; DOI=10.1515/bchm.1998.379.2.175;
RA Lee H.-J., Sorimachi H., Jeong S.-Y., Ishiura S., Suzuki K.;
RT "Molecular cloning and characterization of a novel tissue-specific calpain
RT predominantly expressed in the digestive tract.";
RL Biol. Chem. 379:175-183(1998).
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in stomach and small
CC intestine, although low levels of expression in other organs.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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DR EMBL; AK008629; BAB25791.1; -; mRNA.
DR EMBL; AC126930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC135015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U89513; AAB69114.1; -; mRNA.
DR CCDS; CCDS40514.1; -.
DR RefSeq; NP_076198.2; NM_023709.4.
DR AlphaFoldDB; Q9D805; -.
DR SMR; Q9D805; -.
DR CORUM; Q9D805; -.
DR STRING; 10090.ENSMUSP00000090717; -.
DR MEROPS; C02.006; -.
DR iPTMnet; Q9D805; -.
DR PhosphoSitePlus; Q9D805; -.
DR MaxQB; Q9D805; -.
DR PaxDb; Q9D805; -.
DR PRIDE; Q9D805; -.
DR ProteomicsDB; 281769; -.
DR Antibodypedia; 20792; 247 antibodies from 31 providers.
DR DNASU; 73647; -.
DR Ensembl; ENSMUST00000093033; ENSMUSP00000090717; ENSMUSG00000031981.
DR GeneID; 73647; -.
DR KEGG; mmu:73647; -.
DR UCSC; uc009nxf.2; mouse.
DR CTD; 10753; -.
DR MGI; MGI:1920897; Capn9.
DR VEuPathDB; HostDB:ENSMUSG00000031981; -.
DR eggNOG; KOG0045; Eukaryota.
DR GeneTree; ENSGT00940000158966; -.
DR HOGENOM; CLU_010982_0_3_1; -.
DR InParanoid; Q9D805; -.
DR OMA; SADHCEF; -.
DR OrthoDB; 704215at2759; -.
DR PhylomeDB; Q9D805; -.
DR TreeFam; TF314748; -.
DR BRENDA; 3.4.22.B29; 3474.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR BioGRID-ORCS; 73647; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Capn9; mouse.
DR PRO; PR:Q9D805; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9D805; protein.
DR Bgee; ENSMUSG00000031981; Expressed in pyloric antrum and 39 other tissues.
DR ExpressionAtlas; Q9D805; baseline and differential.
DR Genevisible; Q9D805; 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:0007586; P:digestion; IEA:InterPro.
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; IPR029542; CAPN9.
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 PANTHER; PTHR10183:SF385; PTHR10183:SF385; 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; 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; 3.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cytoplasm; Hydrolase; Metal-binding; Protease; Reference proteome;
KW Repeat; Thiol protease.
FT CHAIN 1..690
FT /note="Calpain-9"
FT /id="PRO_0000207723"
FT DOMAIN 42..337
FT /note="Calpain catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT DOMAIN 518..552
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 561..589
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 591..626
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..521
FT /note="Domain III"
FT REGION 522..690
FT /note="Domain IV"
FT ACT_SITE 97
FT /evidence="ECO:0000250"
FT ACT_SITE 254
FT /evidence="ECO:0000250"
FT ACT_SITE 278
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 314
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 574
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 576
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 578
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 580
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 585
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 604
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 606
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 608
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 610
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 615
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT CONFLICT 188
FT /note="K -> E (in Ref. 1; BAB25791)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="K -> R (in Ref. 3; AAB69114)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 690 AA; 78977 MW; 188F95D93E113947 CRC64;
MPYLHRSLRP QPQPVPGDAR TIHSSGQSFE QLRQGCLQSG TLFEDADFPA SNVSLFYSER
PQVPFVWKRP GEIVEKPEFI LGGATRTDIC QGELGDCWLL AAIASLTLNQ KALTRVVPQD
QGFGSGYAGI FHFQFWQHSE WLDVVIDDRL PTFKDRLVFL HSADHNEFWS ALLEKAYAKL
NGSYEALKGG SAIEAMEDFT GGVAENFQIR EAPEDFFEIL EKALKRGSLL GCSIDTLNAS
ESEARTSLGL IKGHAYTVTG LDQVNFHGQR IKLIRVRNPW GQVEWNGPWS DSSPEWRSVD
LEEQKRLGHT ALDDGEFWMA FKDFKIHFDK VEICNLTPDA LEDSALHRWE VTIHQGSWVR
GSTAGGCRNF LDTFWTNPQI KLSLTERDEG QEGCTFLAAL MQKDRRRLKR FGANMLTIGY
AIYQCPDKDG HLSRDFFRYH ASLARSKTFI NLREVSERFQ LPPGDYILIP STFEPHQEAD
FCLRIFSEKR AVTRDLDENI DIDLPELPKP TPQEEETEEE QQFRALFQRV AGEDMEVSAE
ELEYVLNAVL QKKTALKFKR LSLLSCRNII SLMDTSGNGK LEFEEFRVFW DKLKHWMDLF
LQFDVDKSGT MSSYELRTAL KAAGFQLGGH LLQLIVLRYA DEDLQLDFDD YLNCLVRLEN
ASRVFQSLSV KNKDFIHLNI NEFISLTMNI
