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

 CAN8_HUMAN              Reviewed;         703 AA.
A6NHC0; B2RXL2;
02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
10-AUG-2010, sequence version 3.
25-OCT-2017, entry version 92.
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;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Leukocyte;
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 GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
-!- 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:0000250}. Golgi apparatus
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Stomach.
-!- 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; AC099065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR628412; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR848842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC157893; AAI57894.1; -; mRNA.
CCDS; CCDS73038.1; -.
RefSeq; NP_001137434.1; NM_001143962.1.
UniGene; Hs.291487; -.
ProteinModelPortal; A6NHC0; -.
SMR; A6NHC0; -.
BioGrid; 132835; 4.
MEROPS; C02.007; -.
iPTMnet; A6NHC0; -.
PhosphoSitePlus; A6NHC0; -.
BioMuta; CAPN8; -.
MaxQB; A6NHC0; -.
PRIDE; A6NHC0; -.
Ensembl; ENST00000366872; ENSP00000355837; ENSG00000203697.
GeneID; 388743; -.
KEGG; hsa:388743; -.
UCSC; uc031vow.1; human.
CTD; 388743; -.
EuPathDB; HostDB:ENSG00000203697.11; -.
GeneCards; CAPN8; -.
HGNC; HGNC:1485; CAPN8.
HPA; HPA073939; -.
neXtProt; NX_A6NHC0; -.
OpenTargets; ENSG00000203697; -.
GeneTree; ENSGT00760000118971; -.
HOGENOM; HOG000232035; -.
HOVERGEN; HBG012645; -.
InParanoid; A6NHC0; -.
KO; K08577; -.
OMA; DGEFCLR; -.
OrthoDB; EOG091G049E; -.
PhylomeDB; A6NHC0; -.
TreeFam; TF314748; -.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
ChiTaRS; CAPN8; human.
GenomeRNAi; 388743; -.
PRO; PR:A6NHC0; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000203697; -.
CleanEx; HS_CAPN8; -.
ExpressionAtlas; A6NHC0; baseline and differential.
Genevisible; A6NHC0; HS.
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; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
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; PS00018; EF_HAND_1; 2.
PROSITE; PS50222; EF_HAND_2; 3.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
2: Evidence at transcript level;
Autocatalytic cleavage; Calcium; Complete proteome; Cytoplasm;
Golgi apparatus; Hydrolase; Metal-binding; Protease;
Reference proteome; Repeat; Thiol protease.
CHAIN 1 703 Calpain-8.
/FTId=PRO_0000349280.
DOMAIN 45 344 Calpain catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00239}.
DOMAIN 575 610 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 605 640 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 670 703 EF-hand 3. {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 356 379 Domain III.
ACT_SITE 105 105 {ECO:0000250}.
ACT_SITE 262 262 {ECO:0000250}.
ACT_SITE 286 286 {ECO:0000250}.
CONFLICT 245 245 S -> Y (in Ref. 3; AAI57894).
{ECO:0000305}.
CONFLICT 592 592 T -> M (in Ref. 3; AAI57894).
{ECO:0000305}.
SEQUENCE 703 AA; 79144 MW; 2A6DFFC0814894A8 CRC64;
MAAQAAGVSR QRAATQGLGS NQNALKYLGQ DFKTLRQQCL DSGVLFKDPE FPACPSALGY
KDLGPGSPQT QGIIWKRPTE LCPSPQFIVG GATRTDICQG GLGDCWLLAA IASLTLNEEL
LYRVVPRDQD FQENYAGIFH FQFWQYGEWV EVVIDDRLPT KNGQLLFLHS EQGNEFWSAL
LEKAYAKLNG CYEALAGGST VEGFEDFTGG ISEFYDLKKP PANLYQIIRK ALCAGSLLGC
SIDVSSAAEA EAITSQKLVK SHAYSVTGVE EVNFQGHPEK LIRLRNPWGE VEWSGAWSDD
APEWNHIDPR RKEELDKKVE DGEFWMSLSD FVRQFSRLEI CNLSPDSLSS EEVHKWNLVL
FNGHWTRGST AGGCQNYPAT YWTNPQFKIR LDEVDEDQEE SIGEPCCTVL LGLMQKNRRW
RKRIGQGMLS IGYAVYQVPK ELESHTDAHL GRDFFLAYQP SARTSTYVNL REVSGRARLP
PGEYLVVPST FEPFKDGEFC LRVFSEKKAQ ALEIGDVVAG NPYEPHPSEV DQEDDQFRRL
FEKLAGKDSE ITANALKILL NEAFSKRTDI KFDGFNINTC REMISLLDSN GTGTLGAVEF
KTLWLKIQKY LEIYWETDYN HSGTIDAHEM RTALRKAGFT LNSQVQQTIA LRYACSKLGI
NFDSFVACMI RLETLFKLFS LLDEDKDGMV QLSLAEWLCC VLV


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