(data stored in ACNUC9543 zone)

SWISSPROT: 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   08-MAY-2019, entry version 155.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   domain: 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
RT   they are 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
RT   project: 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
RT   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}.
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   STRING; 10090.ENSMUSP00000048183; -.
DR   MEROPS; C02.011; -.
DR   iPTMnet; O08688; -.
DR   PhosphoSitePlus; O08688; -.
DR   SwissPalm; O08688; -.
DR   EPD; O08688; -.
DR   PaxDb; O08688; -.
DR   PeptideAtlas; O08688; -.
DR   PRIDE; O08688; -.
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   eggNOG; KOG0045; Eukaryota.
DR   eggNOG; ENOG410XP0B; LUCA.
DR   GeneTree; ENSGT00940000156536; -.
DR   HOGENOM; HOG000232036; -.
DR   InParanoid; O08688; -.
DR   KO; K08574; -.
DR   OMA; GMCGYPQ; -.
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   ChiTaRS; Capn5; mouse.
DR   PRO; PR:O08688; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000035547; Expressed in 211 organ(s), highest expression level in urinary bladder urothelium.
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; ISO: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; SSF49758; SSF49758; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS50203; CALPAIN_CAT; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE   1: Evidence at protein level;
DR   PRODOM; O08688.
DR   SWISS-2DPAGE; O08688.
KW   Complete proteome; Hydrolase; Polymorphism; Protease;
KW   Reference proteome; Thiol protease.
FT   CHAIN         1    640       Calpain-5.
FT                                /FTId=PRO_0000207714.
FT   DOMAIN       26    343       Calpain catalytic. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00239}.
FT   DOMAIN      518    619       C2.
FT   REGION      344    496       Domain III.
FT   ACT_SITE     81     81       {ECO:0000250}.
FT   ACT_SITE    252    252       {ECO:0000250}.
FT   ACT_SITE    284    284       {ECO:0000250}.
FT   VARIANT     427    427       D -> N. {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
//

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