ID   CAN5_MOUSE              Reviewed;         640 AA.
AC   O08688; Q91YU0;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   24-JAN-2024, entry version 179.
DE   RecName: Full=Calpain-5;
DE            EC=3.4.22.-;
DE   AltName: Full=New calpain 3;
DE            Short=nCL-3;
GN   Name=Capn5; Synonyms=Ncl3;
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].
RC   STRAIN=BALB/cJ;
RX   PubMed=9339374; DOI=10.1006/geno.1997.4870;
RA   Dear T.N., Matena K., Vingron M., Boehm T.;
RT   "A new subfamily of vertebrate calpains lacking a calmodulin-like domain:
RT   implications for calpain regulation and evolution.";
RL   Genomics 45:175-184(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-427.
RX   PubMed=9503024; DOI=10.1006/geno.1997.5133;
RA   Matena K., Boehm T., Dear N.T.;
RT   "Genomic organization of mouse Capn5 and Capn6 genes confirms that they are
RT   a distinct calpain subfamily.";
RL   Genomics 48:117-120(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Algate P.A.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-427.
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).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Lung, and Spleen;
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.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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DR   EMBL; Y10656; CAA71666.1; -; mRNA.
DR   EMBL; U85020; AAD00559.1; -; mRNA.
DR   EMBL; BC014767; AAH14767.1; -; mRNA.
DR   CCDS; CCDS21465.1; -.
DR   RefSeq; NP_001288179.1; NM_001301250.1.
DR   RefSeq; NP_031628.1; NM_007602.4.
DR   AlphaFoldDB; O08688; -.
DR   SMR; O08688; -.
DR   BioGRID; 198474; 13.
DR   IntAct; O08688; 1.
DR   MINT; O08688; -.
DR   STRING; 10090.ENSMUSP00000048183; -.
DR   MEROPS; C02.011; -.
DR   iPTMnet; O08688; -.
DR   PhosphoSitePlus; O08688; -.
DR   SwissPalm; O08688; -.
DR   EPD; O08688; -.
DR   jPOST; O08688; -.
DR   PaxDb; 10090-ENSMUSP00000048183; -.
DR   PeptideAtlas; O08688; -.
DR   ProteomicsDB; 273908; -.
DR   Pumba; O08688; -.
DR   Antibodypedia; 31220; 299 antibodies from 29 providers.
DR   DNASU; 12337; -.
DR   Ensembl; ENSMUST00000040971.14; ENSMUSP00000048183.8; ENSMUSG00000035547.15.
DR   Ensembl; ENSMUST00000107112.2; ENSMUSP00000102729.2; ENSMUSG00000035547.15.
DR   GeneID; 12337; -.
DR   KEGG; mmu:12337; -.
DR   UCSC; uc009ikc.2; mouse.
DR   AGR; MGI:1100859; -.
DR   CTD; 726; -.
DR   MGI; MGI:1100859; Capn5.
DR   VEuPathDB; HostDB:ENSMUSG00000035547; -.
DR   eggNOG; KOG0045; Eukaryota.
DR   GeneTree; ENSGT00940000156536; -.
DR   HOGENOM; CLU_010982_3_2_1; -.
DR   InParanoid; O08688; -.
DR   OMA; DICENPR; -.
DR   OrthoDB; 142935at2759; -.
DR   PhylomeDB; O08688; -.
DR   TreeFam; TF314748; -.
DR   BRENDA; 3.4.22.B25; 3474.
DR   Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR   BioGRID-ORCS; 12337; 2 hits in 81 CRISPR screens.
DR   ChiTaRS; Capn5; mouse.
DR   PRO; PR:O08688; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; O08688; Protein.
DR   Bgee; ENSMUSG00000035547; Expressed in urinary bladder urothelium and 187 other cell types or tissues.
DR   ExpressionAtlas; O08688; baseline and differential.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
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; cd04046; C2_Calpain; 1.
DR   CDD; cd00214; Calpain_III; 1.
DR   CDD; cd00044; CysPc; 1.
DR   Gene3D; 2.60.120.380; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   InterPro; IPR033884; C2_Calpain.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
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; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR   PANTHER; PTHR10183; CALPAIN; 1.
DR   PANTHER; PTHR10183:SF402; CALPAIN-5; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF01067; Calpain_III; 1.
DR   Pfam; PF00648; Peptidase_C2; 1.
DR   PRINTS; PR00704; CALPAIN.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00720; calpain_III; 1.
DR   SMART; SM00230; CysPc; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF49758; Calpain large subunit, middle domain (domain III); 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50203; CALPAIN_CAT; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   Genevisible; O08688; MM.
PE   1: Evidence at protein level;
KW   Hydrolase; Protease; Reference proteome; Thiol protease.
FT   CHAIN           1..640
FT                   /note="Calpain-5"
FT                   /id="PRO_0000207714"
FT   DOMAIN          26..343
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   DOMAIN          499..617
FT                   /note="C2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          344..496
FT                   /note="Domain III"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        252
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        284
FT                   /evidence="ECO:0000250"
FT   VARIANT         427
FT                   /note="D -> N"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:9503024"
SQ   SEQUENCE   640 AA;  72955 MW;  7F1DA3E299FEC02D CRC64;
     MFSCAKAYED QNYSALKRAC LRKKVLFEDP LFPATDDSLY YKGTPGPTVR WKRPKDICDD
     PRLFVDGISS HDLHQGQVGN CWFVAACSSL ASRESLWQKV IPDWKEQEWN PEKPDSYAGI
     FHFNFWRFGE WVDVIVDDRL PTVNNQLIYC HSNSKNEFWC ALVEKAYAKL AGCYQALDGG
     NTADALVDFT GGVSEPIDLT EGDLATDEAK RNQLFERVLK VHSRGGLISA SIKAVTAADM
     EARLACGLVK GHAYAVTDVR KVRLGHGLLA FFKSEKLDMI RLRNPWGERE WTGPWSDTSE
     EWQKVSKSER EKMGVTVQDD GEFWMTFEDM CRYFTDIIKC RLINTSYLSI HKTWEEARLH
     GAWTRHEDPQ QNRSGGCINH KDTFFQNPQY VFEVKKPEDE VLISIQQRPK RSTRREGKGE
     NLAIGFDIYK VEENRQYRMH SLQHKAASSI YINSRSVFLR TELPEGRYVI IPTTFEPGHT
     GEFLLRVFTD VPSNCRELRL DEPPRTCWSS LCGYPQQVAQ VHVLGAAGLK DSPTGANSYV
     IIKCEGEKVR SAVQRGTSTP EYNVKGIFYR KKLAQPITVQ VWNHRVLKDE FLGQVHLKTA
     PDDLQDLHTL HLQDRSSRQP SDLPGIVAVR VLCSASLTAV
//