ID L5M1A3_MYODS Unreviewed; 354 AA.
AC L5M1A3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Calpain-8 {ECO:0000313|EMBL:ELK32146.1};
GN ORFNames=MDA_GLEAN10022843 {ECO:0000313|EMBL:ELK32146.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK32146.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00239}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KB105638; ELK32146.1; -; Genomic_DNA.
DR AlphaFoldDB; L5M1A3; -.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00044; CysPc; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 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 PANTHER; PTHR10183; CALPAIN; 1.
DR PANTHER; PTHR10183:SF374; CALPAIN-8; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00230; CysPc; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 2.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT DOMAIN 45..307
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 334..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 105
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1"
SQ SEQUENCE 354 AA; 39235 MW; 05B5BCADC739268A CRC64;
MAAPAAQVSR QRAAAGRLGS NQKVVKYLGQ DFETLRQQCL DSGVLFKDPE FPACPSALGY
KDLGPRSPET QGVVWKRPPE LCPSPQFIAG GATRADICQG GLGDCWLLAA IASLTLNEEL
LHRVVPRDQS FQESYAGIFR FQFWQRGEWV QVVVDDRLPT RDGQLLFLRS GEGSEFWSAL
LEKAYAKLLG SYEALAGGST VEGFEDFTGG ISEFFDLKKP PTGLFQIIRK ALRAGSLLAC
SIDFWQRGEW VQVVVDDRLP TRDGQLLFLR SGEGSEFWSA LLEKAYAKMS FAEFLRQFSR
LEICRWSPDS LSSEEAHKWD LVLSNGLWAR GSTAKGCQNP PGEHGPRASW ACPS
//
