CAN12_MOUSE
ID CAN12_MOUSE Reviewed; 720 AA.
AC Q9ER56; Q9ER53; Q9ER54; Q9ER55;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Calpain-12;
DE EC=3.4.22.-;
DE AltName: Full=Calcium-activated neutral proteinase 12;
DE Short=CANP 12;
GN Name=Capn12;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3 AND 4).
RX PubMed=10964513; DOI=10.1006/geno.2000.6289;
RA Dear T.N., Meier N.T., Hunn M., Boehm T.;
RT "Gene structure, chromosomal localization and expression pattern of Capn12,
RT a new member of the calpain large subunit gene family.";
RL Genomics 68:152-160(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Mammary gland;
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: Calcium-regulated non-lysosomal thiol-protease.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9ER56-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ER56-2; Sequence=VSP_007807, VSP_007808;
CC Name=3; Synonyms=variant 3;
CC IsoId=Q9ER56-3; Sequence=VSP_007809, VSP_007810;
CC Name=4; Synonyms=variant 2;
CC IsoId=Q9ER56-4; Sequence=VSP_007811, VSP_007812;
CC -!- TISSUE SPECIFICITY: Expression localized to the cortex of the hair
CC follicle during the anagen phase of hair cycle.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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DR EMBL; AJ289241; CAC10066.1; -; Genomic_DNA.
DR EMBL; AJ289241; CAC10067.1; -; Genomic_DNA.
DR EMBL; AJ289241; CAC10068.1; -; Genomic_DNA.
DR EMBL; AJ289243; CAC10070.1; -; mRNA.
DR EMBL; BC028751; AAH28751.1; -; mRNA.
DR CCDS; CCDS52166.1; -. [Q9ER56-1]
DR RefSeq; XP_006540316.1; XM_006540253.3. [Q9ER56-4]
DR AlphaFoldDB; Q9ER56; -.
DR SMR; Q9ER56; -.
DR BioGRID; 208623; 6.
DR STRING; 10090.ENSMUSP00000069055; -.
DR MEROPS; C02.017; -.
DR PhosphoSitePlus; Q9ER56; -.
DR PaxDb; Q9ER56; -.
DR PRIDE; Q9ER56; -.
DR ProteomicsDB; 265427; -. [Q9ER56-1]
DR ProteomicsDB; 265428; -. [Q9ER56-2]
DR ProteomicsDB; 265429; -. [Q9ER56-3]
DR ProteomicsDB; 265430; -. [Q9ER56-4]
DR DNASU; 60594; -.
DR GeneID; 60594; -.
DR CTD; 147968; -.
DR MGI; MGI:1891369; Capn12.
DR eggNOG; KOG0045; Eukaryota.
DR InParanoid; Q9ER56; -.
DR PhylomeDB; Q9ER56; -.
DR BRENDA; 3.4.22.B32; 3474.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR BioGRID-ORCS; 60594; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Capn12; mouse.
DR PRO; PR:Q9ER56; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9ER56; protein.
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:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00214; Calpain_III; 1.
DR CDD; cd00044; CysPc; 1.
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; IPR029545; CAPN12.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
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:SF280; PTHR10183:SF280; 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; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Thiol protease.
FT CHAIN 1..720
FT /note="Calpain-12"
FT /id="PRO_0000207731"
FT DOMAIN 45..341
FT /note="Calpain catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT DOMAIN 621..656
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 342..541
FT /note="Domain III"
FT REGION 393..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..720
FT /note="Domain IV"
FT ACT_SITE 105
FT /evidence="ECO:0000250"
FT ACT_SITE 259
FT /evidence="ECO:0000250"
FT ACT_SITE 283
FT /evidence="ECO:0000250"
FT BINDING 634
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 636
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 638
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 640
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 645
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VAR_SEQ 341..448
FT /note="SPEVLGPSPAGGGWHIHIFQGRWVRGFNSGGSQPSAENFWTNPQFRLTLLEP
FT DEEEDDDDEEGPWGGWGAAGARGPARGGRVPKCTVLLSLIQRNRRCLRAKGLTYLT ->
FT LPTPGWRRGGRLPDPQTVVGGGYLLIGLKLREVTLLPDSLSQRWWLCNPGRPHKCWDYE
FT LEPSQTELPPFLLKPLHVSPCLERGTTPTQALGWWALPAPWGMNRDAGRR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:10964513,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007807"
FT VAR_SEQ 449..720
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10964513,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007808"
FT VAR_SEQ 460..502
FT /note="LLDLWDSPRSRALLPGLLRADRSVFCARRDVSRRCRLPPGHYL -> PRALA
FT GTAARRPLGFLRPPRREPSLSPAAWPLPGGTQRLARRR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10964513"
FT /id="VSP_007811"
FT VAR_SEQ 460..462
FT /note="LLD -> GDR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10964513"
FT /id="VSP_007809"
FT VAR_SEQ 463..720
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10964513"
FT /id="VSP_007810"
FT VAR_SEQ 503..720
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10964513"
FT /id="VSP_007812"
SQ SEQUENCE 720 AA; 80588 MW; 37C07BDF0145B531 CRC64;
MASGNRKVTI QLVDDGAGTG AGGPQLFKGQ NYEAIRRACL DSGILFRDPC FPAGPDALGY
DKLGPDSEKA KGVEWKRPHE FCAEPQFICE DMSRTDVCQG SLGNCWLLAA AASLTLYPRL
LYRVVPPGQG FQDGYAGVFH FQLWQFGRWV DVVVDDKLPV REGKLMFVRS EQRNEFWAPL
LEKAYAKLHG SYEVMRGGHM NEAFVDFTGG VGEVLYLRQN TPGVFAALRH ALAKESLVGA
TALSDRGEIR TDEGLVKGHA YSVTGTHKMS LGFTKVRLLR LRNPWGRVEW SGPWSDSCPR
WDMLPSEWRD ALLVKKEDGE FWMELQDFLT HFNTVQICSL SPEVLGPSPA GGGWHIHIFQ
GRWVRGFNSG GSQPSAENFW TNPQFRLTLL EPDEEEDDDD EEGPWGGWGA AGARGPARGG
RVPKCTVLLS LIQRNRRCLR AKGLTYLTVG FHVFQIPEEL LDLWDSPRSR ALLPGLLRAD
RSVFCARRDV SRRCRLPPGH YLVVPSASRV GDEADFTLRI FSERSHTAVE IDDVISADLD
ALQAPYKPLE LELAQLFLEL AGEEEELNAL QLQTLISIAL EPARANTRTP GEIGLRTCEQ
LVQCFGRGQR LSLHHFQELW GHLMSWQATF DKFDEDASGT MNSCELRLAL TAAGFHLNNQ
LTQSLTSRYR DSRLRVDFER FVGCAARLTC IFRHCCQHLD GGEGVVCLTH KQWSEVATFS
