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Calpain-8 (EC 3.4.22.53) (New calpain 2) (nCL-2) (Stomach-specific M-type calpain)

 CAN8_MOUSE              Reviewed;         703 AA.
Q91VA3; Q059W1; Q91UZ9; Q920R7;
02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-OCT-2017, entry version 126.
RecName: Full=Calpain-8;
EC=3.4.22.53;
AltName: Full=New calpain 2;
Short=nCL-2;
AltName: Full=Stomach-specific M-type calpain;
Name=Capn8; Synonyms=Ncl2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND
TISSUE SPECIFICITY.
PubMed=11523006; DOI=10.1007/s002390010209;
Hata S., Nishi K., Kawamoto T., Lee H.-J., Kawahara H., Maeda T.,
Shintani Y., Sorimachi H., Suzuki K.;
"Both the conserved and the unique gene structure of stomach-specific
calpains reveal processes of calpain gene evolution.";
J. Mol. Evol. 53:191-203(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION, INTERACTION WITH COPS1; COPB1; EYA2; NME2; NME4 AND TOMM70,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16476741; DOI=10.1074/jbc.M509244200;
Hata S., Koyama S., Kawahara H., Doi N., Maeda T.,
Toyama-Sorimachi N., Abe K., Suzuki K., Sorimachi H.;
"Stomach-specific calpain, nCL-2, localizes in mucus cells and
proteolyzes the beta-subunit of coatomer complex, beta-COP.";
J. Biol. Chem. 281:11214-11224(2006).
[4]
SUBUNIT, ENZYME REGULATION, DOMAIN, BIOPHYSICOCHEMICAL PROPERTIES,
PTM, AND MUTAGENESIS OF CYS-105.
PubMed=17646163; DOI=10.1074/jbc.M703168200;
Hata S., Doi N., Kitamura F., Sorimachi H.;
"Stomach-specific calpain, nCL-2/calpain 8, is active without calpain
regulatory subunit and oligomerizes through C2-like domains.";
J. Biol. Chem. 282:27847-27856(2007).
-!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease (By
similarity). Involved in membrane trafficking in the gastric
surface mucus cells (pit cells) and may involve the membrane
trafficking of mucus cells via interactions with coat protein.
Proteolytically cleaves the beta-subunit of coatomer complex.
{ECO:0000250, ECO:0000269|PubMed:16476741}.
-!- CATALYTIC ACTIVITY: Broad endopeptidase specificity.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
Note=Binds 2 calcium ions. {ECO:0000305};
-!- ENZYME REGULATION: The concentration of calcium for half-maximal
activity is 0.3 mM. Inhibited by calpastatin and calpeptin.
{ECO:0000269|PubMed:17646163}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 6. {ECO:0000269|PubMed:17646163};
Temperature dependence:
Optimum temperature is 20 degrees Celsius.
{ECO:0000269|PubMed:17646163};
-!- SUBUNIT: Monomer and homooligomer. Interacts with COPS1/GPS1,
COPB1, EYA2, NME2, NME4 and TOMM70. {ECO:0000269|PubMed:16476741,
ECO:0000269|PubMed:17646163}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus
{ECO:0000269|PubMed:16476741}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=nCL-2;
IsoId=Q91VA3-1; Sequence=Displayed;
Name=2; Synonyms=Calpain 8b, nCL-2';
IsoId=Q91VA3-2; Sequence=VSP_035306, VSP_035307;
-!- TISSUE SPECIFICITY: Predominantly expressed in the stomach.
Localizes strictly to the surface mucus cells in the gastric
epithelium and the mucus-secreting goblet cells in the duodenum.
{ECO:0000269|PubMed:11523006, ECO:0000269|PubMed:16476741}.
-!- DOMAIN: The domain III mediates oligomerization.
{ECO:0000269|PubMed:17646163}.
-!- PTM: Undergoes autolytic cleavage between Ala-5 and Ala-6 which
gives rise to fragments extending from Ala-6 to the C-terminus,
Ala-6 to the EF-hand 2 domain and from Ala-6 to the beginning of
domain III.
-!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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EMBL; AB050201; BAB70479.1; -; Genomic_DNA.
EMBL; AB050202; BAB70480.1; -; mRNA.
EMBL; AB050203; BAB70481.1; -; mRNA.
EMBL; AB061518; BAB55000.1; -; mRNA.
EMBL; AB061519; BAB55001.1; -; mRNA.
EMBL; BC125504; AAI25505.1; -; mRNA.
EMBL; BC125508; AAI25509.1; -; mRNA.
CCDS; CCDS35814.1; -. [Q91VA3-1]
CCDS; CCDS48477.1; -. [Q91VA3-2]
RefSeq; NP_001139278.1; NM_001145806.1. [Q91VA3-2]
RefSeq; NP_570960.2; NM_130890.2.
UniGene; Mm.189201; -.
ProteinModelPortal; Q91VA3; -.
SMR; Q91VA3; -.
CORUM; Q91VA3; -.
STRING; 10090.ENSMUSP00000047164; -.
MEROPS; C02.007; -.
PhosphoSitePlus; Q91VA3; -.
EPD; Q91VA3; -.
PaxDb; Q91VA3; -.
PeptideAtlas; Q91VA3; -.
PRIDE; Q91VA3; -.
Ensembl; ENSMUST00000168514; ENSMUSP00000129549; ENSMUSG00000038599. [Q91VA3-2]
GeneID; 170725; -.
KEGG; mmu:170725; -.
UCSC; uc007dyh.2; mouse. [Q91VA3-2]
UCSC; uc007dyi.2; mouse. [Q91VA3-1]
CTD; 388743; -.
MGI; MGI:2181366; Capn8.
eggNOG; KOG0045; Eukaryota.
eggNOG; ENOG410XP0B; LUCA.
GeneTree; ENSGT00760000118971; -.
HOGENOM; HOG000232035; -.
HOVERGEN; HBG012645; -.
InParanoid; Q91VA3; -.
KO; K08577; -.
PhylomeDB; Q91VA3; -.
TreeFam; TF314748; -.
BRENDA; 3.4.22.B28; 3474.
PRO; PR:Q91VA3; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000038599; -.
CleanEx; MM_CAPN8; -.
ExpressionAtlas; Q91VA3; baseline and differential.
Genevisible; Q91VA3; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0007586; P:digestion; IEA:InterPro.
GO; GO:0006508; P:proteolysis; IBA:GO_Central.
CDD; cd00214; Calpain_III; 1.
CDD; cd00044; CysPc; 1.
InterPro; IPR033883; C2_III.
InterPro; IPR022684; Calpain_cysteine_protease.
InterPro; IPR022682; Calpain_domain_III.
InterPro; IPR022683; Calpain_III.
InterPro; IPR036213; Calpain_III_sf.
InterPro; IPR029543; CAPN8.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR001300; Peptidase_C2_calpain_cat.
PANTHER; PTHR10183:SF374; PTHR10183:SF374; 1.
Pfam; PF01067; Calpain_III; 1.
Pfam; PF00648; Peptidase_C2; 1.
PRINTS; PR00704; CALPAIN.
SMART; SM00720; calpain_III; 1.
SMART; SM00230; CysPc; 1.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF49758; SSF49758; 1.
PROSITE; PS50203; CALPAIN_CAT; 1.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
1: Evidence at protein level;
Alternative splicing; Autocatalytic cleavage; Calcium;
Complete proteome; Cytoplasm; Golgi apparatus; Hydrolase;
Metal-binding; Protease; Reference proteome; Repeat; Thiol protease.
CHAIN 1 703 Calpain-8.
/FTId=PRO_0000349281.
DOMAIN 45 344 Calpain catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00239}.
DOMAIN 531 566 EF-hand 1.
DOMAIN 575 610 EF-hand 2.
DOMAIN 605 640 EF-hand 3.
DOMAIN 670 703 EF-hand 4.
CA_BIND 588 599 1. {ECO:0000255}.
CA_BIND 618 629 2. {ECO:0000255}.
REGION 355 512 Domain III.
REGION 513 531 Linker. {ECO:0000250}.
REGION 532 703 Domain IV. {ECO:0000250}.
ACT_SITE 105 105 {ECO:0000250}.
ACT_SITE 262 262 {ECO:0000250}.
ACT_SITE 286 286 {ECO:0000250}.
VAR_SEQ 379 381 ATY -> GSF (in isoform 2).
{ECO:0000303|PubMed:11523006}.
/FTId=VSP_035306.
VAR_SEQ 382 703 Missing (in isoform 2).
{ECO:0000303|PubMed:11523006}.
/FTId=VSP_035307.
MUTAGEN 105 105 C->S: Loss of activity.
{ECO:0000269|PubMed:17646163}.
CONFLICT 354 354 H -> Q (in Ref. 1; BAB70479).
{ECO:0000305}.
CONFLICT 519 519 P -> A (in Ref. 2; AAI25505/AAI25509).
{ECO:0000305}.
CONFLICT 700 700 R -> C (in Ref. 2; AAI25505/AAI25509).
{ECO:0000305}.
SEQUENCE 703 AA; 79335 MW; 50F2F9CCF2192FB6 CRC64;
MAALAAGISK QRAAAQGLGS NQNAVKYLGQ DFETLRKQCL NSGVLFKDPE FPACPSALGY
RDLGPGSAET QGIIWKRPTE LCSNPQFIVG GATRTDIRQG GLGDCWLLAA IASLTLNEKL
LYRVVPRDQS FQKNYAGIFH FQFWQYGEWV EVVIDDRLPT KNGQLLFLHS EEGNEFWSAL
LEKAYAKLNG SYEALAGGST IEGFEDFTGG ISEFYDLRKP PGNLYYTIQK ALRKGSLLGC
SIDVSNAAEA EATTRQKLVK GHAYSVTGVE EVDFRGLPEK LIRLRNPWGE VEWTGAWSDS
APEWNYIDPQ KKGELDKRAE DGEFWMSFSD FLKQFSRLEI CNLSPDSLSS EEIHKWNLVL
FNGRWTRGST AGGCQNYPAT YWTNPQFKIH LDEVDEDQEE GTSEPCCTVL LGLMQKNRRR
QRRIGQGMLS IGYAVYQIPK ELENHTDEHL GRDFFQGRQP STCSSTYMNL REVSSRVQLP
PGQYLVVPST FEPFKDGDFC LRVFSEKKAQ ALEIGDAVPG DPHEPHPRDM DGEDEHFWSL
SEEFADKDSE ISAHQLKRVL NGLLSKRTDM KFDGFNINTC REMISLLDGD GTGSLRPVEF
KTLWLKICKY LEIYQEMDHS RAGTIDAHEM RTALKKAGFT LNNQVQQTIA TRYACSKLGV
DFDGFVACMI RLEILFKLFR LLDKDQNGIV QLSLAEWLCR ALV


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