ID   CAN7_MOUSE              Reviewed;         813 AA.
AC   Q9R1S8; Q9Z0P9;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 170.
DE   RecName: Full=Calpain-7;
DE            EC=3.4.22.-;
DE   AltName: Full=PalB homolog;
DE            Short=PalBH;
GN   Name=Capn7; Synonyms=Palbh;
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].
RX   PubMed=11342116; DOI=10.1016/s0167-4781(00)00256-6;
RA   Futai E., Kubo T., Sorimachi H., Suzuki K., Maeda T.;
RT   "Molecular cloning of PalBH, a mammalian homologue of the Aspergillus
RT   atypical calpain PalB.";
RL   Biochim. Biophys. Acta 1517:316-319(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 11-813.
RX   PubMed=10051333; DOI=10.1007/s003359900995;
RA   Franz T., Vingron M., Boehm T., Dear T.N.;
RT   "Capn7: a highly divergent vertebrate calpain with a novel C-terminal
RT   domain.";
RL   Mamm. Genome 10:318-321(1999).
CC   -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB39203.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB028640; BAA78731.1; -; mRNA.
DR   EMBL; AJ012475; CAB39203.1; ALT_INIT; mRNA.
DR   CCDS; CCDS26911.1; -.
DR   RefSeq; NP_033926.1; NM_009796.2.
DR   RefSeq; XP_017171318.1; XM_017315829.1.
DR   AlphaFoldDB; Q9R1S8; -.
DR   SMR; Q9R1S8; -.
DR   BioGRID; 198476; 3.
DR   STRING; 10090.ENSMUSP00000022451; -.
DR   MEROPS; C02.029; -.
DR   iPTMnet; Q9R1S8; -.
DR   PhosphoSitePlus; Q9R1S8; -.
DR   EPD; Q9R1S8; -.
DR   MaxQB; Q9R1S8; -.
DR   PaxDb; 10090-ENSMUSP00000022451; -.
DR   ProteomicsDB; 281766; -.
DR   Pumba; Q9R1S8; -.
DR   Antibodypedia; 11065; 116 antibodies from 23 providers.
DR   DNASU; 12339; -.
DR   Ensembl; ENSMUST00000022451.14; ENSMUSP00000022451.8; ENSMUSG00000021893.15.
DR   GeneID; 12339; -.
DR   KEGG; mmu:12339; -.
DR   UCSC; uc007sxm.1; mouse.
DR   AGR; MGI:1338030; -.
DR   CTD; 23473; -.
DR   MGI; MGI:1338030; Capn7.
DR   VEuPathDB; HostDB:ENSMUSG00000021893; -.
DR   eggNOG; KOG0045; Eukaryota.
DR   GeneTree; ENSGT00940000155892; -.
DR   HOGENOM; CLU_006770_2_0_1; -.
DR   InParanoid; Q9R1S8; -.
DR   OMA; GDYRRGC; -.
DR   OrthoDB; 230045at2759; -.
DR   PhylomeDB; Q9R1S8; -.
DR   TreeFam; TF322245; -.
DR   BRENDA; 3.4.22.B27; 3474.
DR   Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR   BioGRID-ORCS; 12339; 1 hit in 79 CRISPR screens.
DR   ChiTaRS; Capn7; mouse.
DR   PRO; PR:Q9R1S8; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q9R1S8; Protein.
DR   Bgee; ENSMUSG00000021893; Expressed in metanephric cortical collecting duct and 269 other cell types or tissues.
DR   ExpressionAtlas; Q9R1S8; baseline and differential.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR   GO; GO:0090541; F:MIT domain binding; ISO:MGI.
DR   GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
DR   GO; GO:0006508; P:proteolysis; IMP:CACAO.
DR   GO; GO:0097264; P:self proteolysis; ISO:MGI.
DR   CDD; cd00044; CysPc; 1.
DR   CDD; cd02681; MIT_calpain7_1; 1.
DR   Gene3D; 2.60.120.380; -; 2.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 2.
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; IPR007330; MIT_dom.
DR   InterPro; IPR036181; MIT_dom_sf.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR   PANTHER; PTHR46143; CALPAIN-7; 1.
DR   PANTHER; PTHR46143:SF1; CALPAIN-7; 1.
DR   Pfam; PF01067; Calpain_III; 1.
DR   Pfam; PF04212; MIT; 2.
DR   Pfam; PF00648; Peptidase_C2; 1.
DR   PRINTS; PR00704; CALPAIN.
DR   SMART; SM00720; calpain_III; 1.
DR   SMART; SM00230; CysPc; 1.
DR   SMART; SM00745; MIT; 2.
DR   SUPFAM; SSF49758; Calpain large subunit, middle domain (domain III); 2.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF116846; MIT domain; 2.
DR   PROSITE; PS50203; CALPAIN_CAT; 1.
DR   Genevisible; Q9R1S8; MM.
PE   2: Evidence at transcript level;
KW   Acetylation; Hydrolase; Nucleus; Phosphoprotein; Protease;
KW   Reference proteome; Repeat; Thiol protease.
FT   CHAIN           1..813
FT                   /note="Calpain-7"
FT                   /id="PRO_0000207721"
FT   DOMAIN          232..540
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   REGION          541..701
FT                   /note="Domain III"
FT   REGION          702..813
FT                   /note="Domain N"
FT   ACT_SITE        290
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        458
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        478
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6W3"
FT   MOD_RES         95
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6W3"
SQ   SEQUENCE   813 AA;  92564 MW;  81EB508DF7357655 CRC64;
     MDASALERDA VQFARLAVQR DHEGRYSEAV FYYKEAAQAL IYAEMAGSSL ERIQEKINEY
     LERVQALHSA VQSKSTDPLK SKHQLDLERA HFLVTQAFDE DEKGNVEDAI ELYTEAVELC
     LKTSSETADK TLQNKLKQLA RQALDRAEAL SEPLTKPFCK LKSANMKTKT PPVRTHFPLG
     PNPFVEKPQA FISPQSCDAQ GQKYTAEEIE VLRTTSKING VEYVPFMSVD LRERFAYPMP
     FCDRLGKLPL SPKQKTTFSK WVRPEDLTNN PTMIYTVSSF SIKQTIVSDC SFVASLAISA
     AYERRFNKKL ITSIIYPQNK DGEPEYNPCG KYMVKLHLNG VPRKVIIDDQ LPVDHKGELL
     CSYSNNKSEL WVSLIEKAYM KVMGGYDFPG SNSNIDLHAL TGWIPERIAM HSDSQTFSKD
     NSFRMLYQRF HKGDVLITAS TGVMTEAEGE KWGLVPTHAY AVLDIREFKG LRFIQLKNPW
     SHLRWKGRYS ENDVKNWTPE LQKYLNFDPR TAQKIDNGIF WISWDDLCQY YDVVYLSWNP
     ALFKESTCIH STWDAKQGPV KDAYSLANNP QYKLEVQCPQ GGAAVWVLLS RHITDKDDFA
     NNREFITMVV YKTDGKKVYY PADPPPYIDG IRINSPHYLT KIKLTTPGTH TFTLVVSQYE
     KQNTIHYTVR VYSACSFTFS KIPSPYTLSK RINGKWSGQS AGGCGNFQET HKNNPIYQFH
     IDKTGPLLIE LRGPRQYSVG FEVVAVSIMG DPGPHGFQRK SSGDYRCGFC YLELENIPAG
     IFNIIPSTFL PKQEGPFFLD FNSTVPIKTT QLQ
//