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Calpain-8 (EC 3.4.22.53) (Calpain large subunit 4) (New calpain 2) (nCL-2) (Stomach-specific M-type calpain)

 CAN8_RAT                Reviewed;         703 AA.
Q78EJ9; Q64698; Q78EJ8; Q8K407;
02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
30-AUG-2017, entry version 111.
RecName: Full=Calpain-8;
EC=3.4.22.53;
AltName: Full=Calpain large subunit 4;
AltName: Full=New calpain 2;
Short=nCL-2;
AltName: Full=Stomach-specific M-type calpain;
Name=Capn8; Synonyms=Cls4, Ncl2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
AND TISSUE SPECIFICITY.
TISSUE=Gastric mucosa;
PubMed=7690035;
Sorimachi H., Ishiura S., Suzuki K.;
"A novel tissue-specific calpain species expressed predominantly in
the stomach comprises two alternative splicing products with and
without Ca(2+)-binding domain.";
J. Biol. Chem. 268:19476-19482(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17, AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley;
PubMed=12150941; DOI=10.1016/S0006-291X(02)00655-1;
Duan W.R., Ito M., Lee E.J., Chien P.-Y., Jameson J.L.;
"Estrogen regulates a tissue-specific calpain in the anterior
pituitary.";
Biochem. Biophys. Res. Commun. 295:261-266(2002).
-!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease. 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 (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Broad endopeptidase specificity.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
Note=Binds 2 calcium ions. {ECO:0000305};
-!- SUBUNIT: Monomer and homooligomer. Interacts with COPS1/GPS1,
COPB1, EYA2, NME2, NME4 and TOMM70 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7690035}.
Golgi apparatus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=nCL-2;
IsoId=Q78EJ9-1; Sequence=Displayed;
Name=2; Synonyms=Calpain 8b, nCL-2';
IsoId=Q78EJ9-2; Sequence=VSP_035308, VSP_035309;
-!- 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.
Detected in the pituitary after estrogen stimulation.
{ECO:0000269|PubMed:12150941, ECO:0000269|PubMed:7690035}.
-!- DOMAIN: The domain III mediates oligomerization. {ECO:0000250}.
-!- 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. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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EMBL; D14478; BAA03369.1; -; Transcribed_RNA.
EMBL; D14479; BAA03370.1; -; mRNA.
EMBL; D14480; BAA03371.1; -; mRNA.
EMBL; AF514419; AAM94284.1; -; Genomic_DNA.
PIR; A48764; A48764.
RefSeq; NP_579843.2; NM_133309.2. [Q78EJ9-1]
UniGene; Rn.80837; -.
ProteinModelPortal; Q78EJ9; -.
SMR; Q78EJ9; -.
STRING; 10116.ENSRNOP00000062898; -.
MEROPS; C02.007; -.
iPTMnet; Q78EJ9; -.
PhosphoSitePlus; Q78EJ9; -.
PaxDb; Q78EJ9; -.
PRIDE; Q78EJ9; -.
Ensembl; ENSRNOT00000004649; ENSRNOP00000004649; ENSRNOG00000003468. [Q78EJ9-2]
Ensembl; ENSRNOT00000067005; ENSRNOP00000062898; ENSRNOG00000003468. [Q78EJ9-1]
GeneID; 170808; -.
KEGG; rno:170808; -.
UCSC; RGD:620085; rat. [Q78EJ9-1]
CTD; 388743; -.
RGD; 620085; Capn8.
eggNOG; KOG0045; Eukaryota.
eggNOG; ENOG410XP0B; LUCA.
GeneTree; ENSGT00760000118971; -.
HOGENOM; HOG000232035; -.
HOVERGEN; HBG012645; -.
InParanoid; Q78EJ9; -.
KO; K08577; -.
OMA; DGEFCLR; -.
OrthoDB; EOG091G049E; -.
PhylomeDB; Q78EJ9; -.
TreeFam; TF314748; -.
PRO; PR:Q78EJ9; -.
Proteomes; UP000002494; Chromosome 13.
Bgee; ENSRNOG00000003468; -.
Genevisible; Q78EJ9; RN.
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; IPR029543; CAPN8.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR001300; Peptidase_C2_calpain_cat.
PANTHER; PTHR10183:SF350; PTHR10183:SF350; 1.
Pfam; PF01067; Calpain_III; 1.
Pfam; PF00648; Peptidase_C2; 1.
PRINTS; PR00704; CALPAIN.
SMART; SM00720; calpain_III; 1.
SMART; SM00230; CysPc; 1.
SMART; SM00054; EFh; 2.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF49758; SSF49758; 1.
PROSITE; PS50203; CALPAIN_CAT; 1.
PROSITE; PS00018; EF_HAND_1; 1.
PROSITE; PS50222; EF_HAND_2; 4.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
2: Evidence at transcript 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_0000349282.
DOMAIN 45 344 Calpain catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00239}.
DOMAIN 532 566 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 575 608 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 605 640 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 670 703 EF-hand 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 588 599 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 618 629 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
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 380 381 TY -> SS (in isoform 2).
{ECO:0000303|PubMed:7690035}.
/FTId=VSP_035308.
VAR_SEQ 382 703 Missing (in isoform 2).
{ECO:0000303|PubMed:7690035}.
/FTId=VSP_035309.
CONFLICT 103 103 G -> V (in Ref. 1; BAA03369).
{ECO:0000305}.
SEQUENCE 703 AA; 79555 MW; C0688B055FC0D6EC CRC64;
MAALAAGVSK QRAVAEGLGS NQNAVKYLGQ DFETLRKQCL NSGVLFKDPE FPACPSALGY
KDLGPGSPDT QGIVWKRPTE LCPNPQFIVG GATRTDIRQG GLGDCWLLAA IASLTLNEKL
LYRVLPRDQS FQKDYAGIFH FQFWQYGEWV EVVIDDRLPT KNGQLLFLHS EEGNEFWSAL
LEKAYAKLNG SYEALVGGST IEGFEDFTGG ISEFYDLKKP PENLYYIIQK ALRKGSLLGC
SIDVSTAAEA EATTRQKLVK GHAYSVTGVE EVNFHGRPEK LIRLRNPWGE VEWSGAWSDN
APEWNYIDPR RKEELDKKAE DGEFWMSFSD FLKQYSRLEI CNLSPDSLSS EEIHKWNLVL
FNGRWTRGST AGGCLNYPGT YWTNPQFKIH LDEVDEDQEE GTSEPCCTVL LGLMQKNRRR
QKRIGQGMLS IGYAVYQIPK ELESHTDAHL GRDFFLGRQP STCSSTYMNL REVSSRVRLP
PGQYLVVPST FEPFKDGDFC LRVFSEKKAK ALEIGDTVSG HPHEPHPRDM DEEDEHVRSL
FEEFVGKDSE ISANQLKRVL NEVLSKRTDM KFDGFNINTC REMISLLDSD GTGSLGPMEF
KTLWLKIRTY LEIFQEMDHN HVGTIEAHEM RTALKKAGFT LNNQVQQTIA MRYACSKLGV
DFNGFVACMI RLETLFKLFR LLDKDQNGIV QLSLAEWLCC VLV


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