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Database: UniProt
Entry: A0A1D5RLJ4_MOUSE
LinkDB: A0A1D5RLJ4_MOUSE
Original site: A0A1D5RLJ4_MOUSE 
ID   A0A1D5RLJ4_MOUSE        Unreviewed;       955 AA.
AC   A0A1D5RLJ4;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Calpain 15 {ECO:0000313|Ensembl:ENSMUSP00000148393.2};
GN   Name=Capn15 {ECO:0000313|Ensembl:ENSMUSP00000148393.2,
GN   ECO:0000313|MGI:MGI:1355075};
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 {ECO:0000313|Ensembl:ENSMUSP00000148393.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000148393.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000148393.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0000313|Ensembl:ENSMUSP00000148393.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000148393.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family.
CC       {ECO:0000256|ARBA:ARBA00007623}.
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DR   AlphaFoldDB; A0A1D5RLJ4; -.
DR   SMR; A0A1D5RLJ4; -.
DR   ProteomicsDB; 346769; -.
DR   Antibodypedia; 22715; 88 antibodies from 16 providers.
DR   Ensembl; ENSMUST00000212789.2; ENSMUSP00000148393.2; ENSMUSG00000037326.11.
DR   AGR; MGI:1355075; -.
DR   MGI; MGI:1355075; Capn15.
DR   VEuPathDB; HostDB:ENSMUSG00000037326; -.
DR   GeneTree; ENSGT00940000158312; -.
DR   ChiTaRS; Capn15; mouse.
DR   Proteomes; UP000000589; Chromosome 17.
DR   Bgee; ENSMUSG00000037326; Expressed in motor neuron and 252 other cell types or tissues.
DR   ExpressionAtlas; A0A1D5RLJ4; baseline and differential.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00044; CysPc; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 3.
DR   Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR   InterPro; IPR022684; Calpain_cysteine_protease.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   PANTHER; PTHR10183; CALPAIN; 1.
DR   PANTHER; PTHR10183:SF382; CALPAIN-15; 1.
DR   Pfam; PF00648; Peptidase_C2; 1.
DR   Pfam; PF00641; zf-RanBP; 4.
DR   PRINTS; PR00704; CALPAIN.
DR   SMART; SM00230; CysPc; 1.
DR   SMART; SM00547; ZnF_RBZ; 5.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 4.
DR   PROSITE; PS50203; CALPAIN_CAT; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 5.
DR   PROSITE; PS50199; ZF_RANBP2_2; 4.
PE   1: Evidence at protein level;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00239}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU00239};
KW   Proteomics identification {ECO:0007829|EPD:A0A1D5RLJ4,
KW   ECO:0007829|ProteomicsDB:A0A1D5RLJ4};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW   ProRule:PRU00239}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT   DOMAIN          3..32
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          148..178
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          348..379
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          422..451
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
FT   DOMAIN          497..803
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50203"
FT   REGION          96..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..283
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        562
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        727
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        747
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
SQ   SEQUENCE   955 AA;  103407 MW;  CDF71CB1F6FF4149 CRC64;
     MATVGEWSCA RCTFLNPAGQ RQCSICEAPR HKPDLDQILR LSVEEQKWPC ARCTFRNFLG
     KEACEVCGFT PEPVPGAPLL PIINGVLPKP PTILVEPKGS GKEEAGPVRT AGLVATEPAR
     GRPEGEEERE ERGEEEEKEQ EGEGERAEPG SGWACQRCTL HNTPVASSCS ACGGPRKLSL
     PRIPPEALVV PEVVAPTGFH VVPAPSQPVL PGEGAEADSP STSQGPTSTD QEPPRVPLFS
     PFSPTLQNNP VPRSRREVPP QLQPPVPEAV QSSASTSSKG PQQGPGRAAA GASRLAELLS
     GKELLPGKRL SVLEEEVPES SPARCESCSD VIDLAGDIVR YTPASPSSPD FTTWSCARCT
     LRNPTTAPRC SVCGGSKLHG FQEHSEPPTH CPDCGANKPG PCVGSCGRAP SAHKAVRLLP
     DRPGQWACPA CTLINTPRAK HCAACHTPQL LVTQCRGATP LRRRESMHVE KRRQTDEGEA
     KALWENIVAF CRENSVNFVD DSFPPGPASV GFPVGDSVQQ RVKQWLRPHE INCSVFRDHG
     TPWSVFHTLR PSDILQGLLG NCWFLSALAV LAERPDLVER VMVTRSLCAE GAYQVRLCKD
     GTWTTVLVDD MLPCDEAGFL LFSQAQRKQL WVALIEKALA KLHGSYFALQ AGRAIEGLAT
     LTGAPCESLA LQVSSTNPRE EPVDTDLIWA KMLSSKEAGF LMGASCGGGN MKVDDAAYES
     LGLRPRHAYS VLDVRDVQGS RLLRLRNPWG RFSWNGSWSD EWPHWPGHLR AELMPHGSSE
     GVFWMEYSDF IRYFDSVDIC KVHSDWQEAR VQGCFPSTAG GPVGVTALTV LERASLEFAL
     FQEGSRRSDS VDSHLLDLCI LVFRATFGTG GRLSLGRLLA HSKRAVKKFV NCDVMLEPGE
     YAVVCCAFNH WNPAPPGPPA QGSRGHDLLL PDSWLGGTHR GSGEPAPQVL PACAM
//
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