CAN7_MOUSE
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 03-AUG-2022, entry version 162.
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; Q9R1S8; -.
DR PRIDE; Q9R1S8; -.
DR ProteomicsDB; 281766; -.
DR Antibodypedia; 11065; 103 antibodies from 23 providers.
DR DNASU; 12339; -.
DR Ensembl; ENSMUST00000022451; ENSMUSP00000022451; ENSMUSG00000021893.
DR GeneID; 12339; -.
DR KEGG; mmu:12339; -.
DR UCSC; uc007sxm.1; mouse.
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; CSTFAPD; -.
DR OrthoDB; 343870at2759; -.
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 74 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 265 other tissues.
DR ExpressionAtlas; Q9R1S8; baseline and differential.
DR Genevisible; Q9R1S8; MM.
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 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 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; SSF116846; SSF116846; 2.
DR SUPFAM; SSF49758; SSF49758; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
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
