ID   CAN13_RAT               Reviewed;         668 AA.
AC   Q5BK10;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
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;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
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; BC091250; AAH91250.1; -; mRNA.
DR   RefSeq; NP_001020304.1; NM_001025133.1.
DR   RefSeq; XP_006239839.1; XM_006239777.3.
DR   RefSeq; XP_006239840.1; XM_006239778.3.
DR   AlphaFoldDB; Q5BK10; -.
DR   SMR; Q5BK10; -.
DR   STRING; 10116.ENSRNOP00000039021; -.
DR   MEROPS; C02.020; -.
DR   PaxDb; Q5BK10; -.
DR   PRIDE; Q5BK10; -.
DR   Ensembl; ENSRNOT00000047853; ENSRNOP00000039021; ENSRNOG00000032375.
DR   GeneID; 362701; -.
DR   KEGG; rno:362701; -.
DR   UCSC; RGD:1562682; rat.
DR   CTD; 92291; -.
DR   RGD; 1562682; Capn13.
DR   eggNOG; KOG0037; Eukaryota.
DR   eggNOG; KOG0045; Eukaryota.
DR   GeneTree; ENSGT00940000160921; -.
DR   HOGENOM; CLU_010982_0_3_1; -.
DR   InParanoid; Q5BK10; -.
DR   OMA; SQHAYTV; -.
DR   OrthoDB; 704215at2759; -.
DR   PhylomeDB; Q5BK10; -.
DR   TreeFam; TF314748; -.
DR   Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
DR   PRO; PR:Q5BK10; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000032375; Expressed in stomach and 12 other tissues.
DR   Genevisible; Q5BK10; RN.
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; IPR022683; Calpain_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; SM00720; calpain_III; 1.
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..668
FT                   /note="Calpain-13"
FT                   /id="PRO_0000259584"
FT   DOMAIN          34..331
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   DOMAIN          537..572
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          635..668
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   ACT_SITE        93
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        249
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        273
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   668 AA;  76939 MW;  654F7BDEA9D3C6F2 CRC64;
     MAHDTEALEE TSVVKFKNQD FRFLRDRCLS RGQLFIDDTF PAEASSIGQK LLMGKRLPKL
     EWKRPQDLSF GPPHFILEGA SRFDIQQGRA GDCWFLAALG SLTQNPQCLQ KILMNQSFSY
     QYAGIFHFRF WQCGQWVEVV IDDRLPVVGN NFCFVHPRRG NQEFWPCLME KAYAKLLGSY
     SQLHYGYLPD ALVDLTGGVV TRINLHSSPS DLLMVVKTAV QTGSMVACAT PKWLTEESEV
     MENGLVSQHA YTVTGAEKIQ YRRGWEEIIR LWNPWGNTEW RGRWGDGSQE WWETHGSRKS
     QLYENKDDGE FWMSCRDFHE NFSCLYICSQ FPITMDPGVT PNESWRQMRF KNQVISGNTA
     GGDGRDIQYL FDVQEPMDGN NVIVAFTVMP QSLKTEEWPF PLQFQVFKVD SQFQKFQKRL
     PPAFFSQFRD AAQGIDYVTK RNFTKSFHLS PGTYVVVASA HGKEVEFLLR IFLKMPHKDR
     NPNSSFNLKA LKGSLSENES PKSSFHRYMD QGLDIDASQL QSLLNQEYLT GPPGDTFSLD
     QCQSIMALMD LKVNGRLDRE EFARLQSRLI HCQHVFQHIQ RSQGVLRSSD LWEVIESTDF
     LSGVLLSKEL LSLMTLRYSD SSGRLSFPSL VCFLIRLETM SKAFRNLSKD GKSIYLTEME
     WMKLVMYS