CAN5_MOUSE
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 03-AUG-2022, entry version 171.
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; O08688; -.
DR PeptideAtlas; O08688; -.
DR PRIDE; O08688; -.
DR ProteomicsDB; 273908; -.
DR Antibodypedia; 31220; 261 antibodies from 29 providers.
DR DNASU; 12337; -.
DR Ensembl; ENSMUST00000040971; ENSMUSP00000048183; ENSMUSG00000035547.
DR Ensembl; ENSMUST00000107112; ENSMUSP00000102729; ENSMUSG00000035547.
DR GeneID; 12337; -.
DR KEGG; mmu:12337; -.
DR UCSC; uc009ikc.2; mouse.
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; RWKRPKY; -.
DR OrthoDB; 704215at2759; -.
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 76 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 184 other tissues.
DR ExpressionAtlas; O08688; baseline and differential.
DR Genevisible; O08688; MM.
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; 2.60.40.150; -; 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 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; SSF49562; 1.
DR SUPFAM; SSF49758; SSF49758; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
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
