ID   CAN10_MACFA             Reviewed;         653 AA.
AC   Q95LP4; Q4R3M7;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Calpain-10;
DE            EC=3.4.22.-;
DE   AltName: Full=Calcium-activated neutral proteinase 10;
DE            Short=CANP 10;
GN   Name=CAPN10; ORFNames=QtsA-15844;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA   Terao K., Sugano S., Hashimoto K.;
RT   "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT   the human genome sequence.";
RL   BMC Genomics 3:36-36(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease which
CC       catalyzes limited proteolysis of substrates involved in cytoskeletal
CC       remodeling and signal transduction. May play a role in insulin-
CC       stimulated glucose uptake (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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DR   EMBL; AB072744; BAB69713.1; -; mRNA.
DR   EMBL; AB179239; BAE02290.1; -; mRNA.
DR   RefSeq; NP_001270318.1; NM_001283389.1.
DR   AlphaFoldDB; Q95LP4; -.
DR   SMR; Q95LP4; -.
DR   STRING; 9541.XP_005574878.1; -.
DR   MEROPS; C02.018; -.
DR   GeneID; 101866540; -.
DR   CTD; 11132; -.
DR   eggNOG; KOG0045; Eukaryota.
DR   OrthoDB; 704215at2759; -.
DR   BRENDA; 3.4.22.B30; 1793.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00214; Calpain_III; 2.
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; IPR028791; CAPN10.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR   PANTHER; PTHR10183:SF30; PTHR10183:SF30; 1.
DR   Pfam; PF01067; Calpain_III; 2.
DR   Pfam; PF00648; Peptidase_C2; 1.
DR   PRINTS; PR00704; CALPAIN.
DR   SMART; SM00720; calpain_III; 2.
DR   SMART; SM00230; CysPc; 1.
DR   SUPFAM; SSF49758; SSF49758; 2.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS50203; CALPAIN_CAT; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Protease; Reference proteome; Repeat; Thiol protease.
FT   CHAIN           1..653
FT                   /note="Calpain-10"
FT                   /id="PRO_0000207726"
FT   DOMAIN          13..321
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT   REGION          322..494
FT                   /note="Domain III 1"
FT   REGION          513..653
FT                   /note="Domain III 2"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        238
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        263
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   653 AA;  72998 MW;  47812497BB315971 CRC64;
     MRAGRGATPA RELFRDAAFP AADSSLFCDL STPLAQFRED ITWRRPQEIC AMPRLFPDDP
     QEGQVKQGLL GDCWFLCACA ALQKSRHLLE QVIPPGQPSW ADQEYQGSFT CRIWQFGRWV
     EVTTDDRLPC LAGRLCFSRC QREDVFWLPL LEKVYAKVHG SYEHLWAGQV ADALVDLTGG
     LAERWSLKGV AGSGGQQDRL GRWEHRTCRQ LLRLKDQSLI SCSVLSPRAG ARELGEFHAF
     IVSDLRELQD QAGQSILLLR IQNPWGRRCW QGLWREGGEG WSQVDAAVTS ELLSQLQEGE
     FWVEEEEFLR EFDEITIGYP ITEAGHLQSL YTEKLLCHTR ALPGAWVKGQ SAGGCRNNSG
     FPSNPKFWLR VSEPSEVYIA VLQRSRLRAV DWAGRARALV GDSHTSWSPA SIPGKHYQAV
     GLHLWKVEKR RVNLPRVLST PPVAGTACHA YDREVHLRCE LSPGYYLAVP STFLKDAPGE
     FLLRVFSTGR VSLSAIRAVA KNASPRAALP AGEWGTVQLR GSWRAGQTAG GSRNFASYPT
     NPCFPFSVPE GPGPRCVRIT LHQHCQPRDT EFHPIGFHIF QVPEGGRSQD APPLLLQEPL
     LSCVPHRYAQ EVSQLCLLPP GTYRVVPSTY LPDTEGAFTV TIATRIDRSP SWQ