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Calpain-9 (EC 3.4.22.-) (Digestive tract-specific calpain) (New calpain 4) (nCL-4) (Protein CG36)

 CAN9_HUMAN              Reviewed;         690 AA.
O14815; B1APS1; B1AQI0; Q9NS74;
16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 156.
RecName: Full=Calpain-9;
EC=3.4.22.-;
AltName: Full=Digestive tract-specific calpain;
AltName: Full=New calpain 4;
Short=nCL-4;
AltName: Full=Protein CG36;
Name=CAPN9; Synonyms=NCL4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Stomach;
PubMed=9524069; DOI=10.1515/bchm.1998.379.2.175;
Lee H.-J., Sorimachi H., Jeong S.-Y., Ishiura S., Suzuki K.;
"Molecular cloning and characterization of a novel tissue-specific
calpain predominantly expressed in the digestive tract.";
Biol. Chem. 379:175-183(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=10835488; DOI=10.1111/j.1349-7006.2000.tb00967.x;
Yoshikawa Y., Mukai H., Hino F., Asada K., Kato I.;
"Isolation of two novel genes, down-regulated in gastric cancer.";
Jpn. J. Cancer Res. 91:459-463(2000).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-102; ARG-122;
ASN-164; THR-234; THR-239; TRP-277; GLN-322; GLN-327; LYS-342;
TRP-458; TRP-522 AND ILE-611.
NIEHS SNPs program;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[4]
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).
[5]
X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 28-347, ACTIVE SITE, AND
CALCIUM-BINDING SITES.
PubMed=17157313; DOI=10.1016/j.jmb.2006.11.037;
Davis T.L., Walker J.R., Finerty P.J. Jr., Mackenzie F., Newman E.M.,
Dhe-Paganon S.;
"The crystal structures of human calpains 1 and 9 imply diverse
mechanisms of action and auto-inhibition.";
J. Mol. Biol. 366:216-229(2007).
-!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease.
-!- CATALYTIC ACTIVITY: Broad endopeptidase specificity.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O14815-1; Sequence=Displayed;
Name=2; Synonyms=CG36;
IsoId=O14815-2; Sequence=VSP_007553;
-!- TISSUE SPECIFICITY: Expressed predominantly in stomach.
-!- INDUCTION: Down-regulated in gastric cancer tissue and in gastric
cell lines of differentiated and poorly differentiated types.
-!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/capn9/";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AF022799; AAB80762.1; -; mRNA.
EMBL; AB038463; BAA92137.1; -; mRNA.
EMBL; AY874864; AAW49735.1; -; Genomic_DNA.
EMBL; AL512328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; FO393421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS1586.1; -. [O14815-1]
CCDS; CCDS31053.1; -. [O14815-2]
RefSeq; NP_001306605.1; NM_001319676.1.
RefSeq; NP_006606.1; NM_006615.2. [O14815-1]
RefSeq; NP_057536.1; NM_016452.2. [O14815-2]
UniGene; Hs.498021; -.
PDB; 1ZIV; X-ray; 2.31 A; A=28-347.
PDB; 2P0R; X-ray; 2.50 A; A/B=10-340.
PDBsum; 1ZIV; -.
PDBsum; 2P0R; -.
ProteinModelPortal; O14815; -.
SMR; O14815; -.
BioGrid; 115976; 2.
STRING; 9606.ENSP00000271971; -.
MEROPS; C02.006; -.
iPTMnet; O14815; -.
PhosphoSitePlus; O14815; -.
BioMuta; CAPN9; -.
PaxDb; O14815; -.
PeptideAtlas; O14815; -.
PRIDE; O14815; -.
Ensembl; ENST00000271971; ENSP00000271971; ENSG00000135773. [O14815-1]
Ensembl; ENST00000354537; ENSP00000346538; ENSG00000135773. [O14815-2]
GeneID; 10753; -.
KEGG; hsa:10753; -.
UCSC; uc001htz.2; human. [O14815-1]
CTD; 10753; -.
DisGeNET; 10753; -.
EuPathDB; HostDB:ENSG00000135773.12; -.
GeneCards; CAPN9; -.
HGNC; HGNC:1486; CAPN9.
HPA; CAB033483; -.
HPA; HPA020398; -.
MIM; 606401; gene.
neXtProt; NX_O14815; -.
OpenTargets; ENSG00000135773; -.
PharmGKB; PA26066; -.
eggNOG; KOG0045; Eukaryota.
eggNOG; ENOG410XP0B; LUCA.
GeneTree; ENSGT00760000118971; -.
HOGENOM; HOG000232035; -.
HOVERGEN; HBG012645; -.
InParanoid; O14815; -.
KO; K08578; -.
OMA; MSSYELR; -.
OrthoDB; EOG091G049E; -.
PhylomeDB; O14815; -.
TreeFam; TF314748; -.
BRENDA; 3.4.22.B29; 2681.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
EvolutionaryTrace; O14815; -.
GeneWiki; CAPN9; -.
GenomeRNAi; 10753; -.
PRO; PR:O14815; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000135773; -.
CleanEx; HS_CAPN9; -.
ExpressionAtlas; O14815; baseline and differential.
Genevisible; O14815; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IBA:GO_Central.
GO; GO:0007586; P:digestion; TAS:ProtInc.
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; IPR029542; CAPN9.
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:SF385; PTHR10183:SF385; 1.
Pfam; PF01067; Calpain_III; 1.
Pfam; PF13833; EF-hand_8; 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; 2.
PROSITE; PS50222; EF_HAND_2; 3.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Complete proteome;
Hydrolase; Metal-binding; Polymorphism; Protease; Reference proteome;
Repeat; Thiol protease.
CHAIN 1 690 Calpain-9.
/FTId=PRO_0000207722.
DOMAIN 42 337 Calpain catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00239}.
DOMAIN 518 552 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 561 594 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 591 626 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 574 585 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 604 615 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
REGION 338 521 Domain III.
REGION 522 690 Domain IV.
ACT_SITE 97 97 {ECO:0000269|PubMed:17157313}.
ACT_SITE 254 254 {ECO:0000269|PubMed:17157313}.
ACT_SITE 278 278 {ECO:0000269|PubMed:17157313}.
METAL 81 81 Calcium 1; via carbonyl oxygen.
METAL 83 83 Calcium 1; via carbonyl oxygen.
METAL 88 88 Calcium 1.
METAL 167 167 Calcium 1.
METAL 284 284 Calcium 2.
METAL 291 291 Calcium 2.
METAL 312 312 Calcium 2; via carbonyl oxygen.
METAL 314 314 Calcium 2.
METAL 316 316 Calcium 2; via carbonyl oxygen.
VAR_SEQ 292 318 SSPEWRSVGPAEQKRLCHTALDDGEFW -> R (in
isoform 2).
{ECO:0000303|PubMed:10835488}.
/FTId=VSP_007553.
VARIANT 102 102 A -> V (in dbSNP:rs12562749).
{ECO:0000269|Ref.3}.
/FTId=VAR_022188.
VARIANT 122 122 S -> R (in dbSNP:rs28359608).
{ECO:0000269|Ref.3}.
/FTId=VAR_022189.
VARIANT 164 164 D -> N (in dbSNP:rs28359632).
{ECO:0000269|Ref.3}.
/FTId=VAR_022190.
VARIANT 234 234 I -> T (in dbSNP:rs28359644).
{ECO:0000269|Ref.3}.
/FTId=VAR_022191.
VARIANT 239 239 A -> T (in dbSNP:rs28359647).
{ECO:0000269|Ref.3}.
/FTId=VAR_022192.
VARIANT 277 277 R -> W (in dbSNP:rs28359655).
{ECO:0000269|Ref.3}.
/FTId=VAR_022193.
VARIANT 322 322 K -> Q (in dbSNP:rs1933631).
{ECO:0000269|Ref.3}.
/FTId=VAR_022194.
VARIANT 327 327 H -> Q (in dbSNP:rs28359684).
{ECO:0000269|Ref.3}.
/FTId=VAR_022195.
VARIANT 342 342 E -> K (in dbSNP:rs16852652).
{ECO:0000269|Ref.3}.
/FTId=VAR_022196.
VARIANT 458 458 R -> W (in dbSNP:rs28359688).
{ECO:0000269|Ref.3}.
/FTId=VAR_022197.
VARIANT 522 522 R -> W (in dbSNP:rs12731961).
{ECO:0000269|Ref.3}.
/FTId=VAR_022198.
VARIANT 611 611 M -> I (in dbSNP:rs16852683).
{ECO:0000269|Ref.3}.
/FTId=VAR_022199.
HELIX 29 38 {ECO:0000244|PDB:1ZIV}.
STRAND 46 48 {ECO:0000244|PDB:1ZIV}.
HELIX 52 54 {ECO:0000244|PDB:1ZIV}.
STRAND 57 59 {ECO:0000244|PDB:2P0R}.
STRAND 66 68 {ECO:0000244|PDB:1ZIV}.
HELIX 70 72 {ECO:0000244|PDB:1ZIV}.
STRAND 74 76 {ECO:0000244|PDB:1ZIV}.
STRAND 78 80 {ECO:0000244|PDB:1ZIV}.
HELIX 86 88 {ECO:0000244|PDB:1ZIV}.
STRAND 93 95 {ECO:0000244|PDB:2P0R}.
HELIX 98 107 {ECO:0000244|PDB:1ZIV}.
HELIX 110 116 {ECO:0000244|PDB:1ZIV}.
STRAND 129 136 {ECO:0000244|PDB:1ZIV}.
STRAND 138 147 {ECO:0000244|PDB:1ZIV}.
STRAND 150 161 {ECO:0000244|PDB:1ZIV}.
HELIX 169 181 {ECO:0000244|PDB:1ZIV}.
HELIX 185 187 {ECO:0000244|PDB:1ZIV}.
STRAND 188 190 {ECO:0000244|PDB:2P0R}.
HELIX 192 200 {ECO:0000244|PDB:1ZIV}.
STRAND 205 208 {ECO:0000244|PDB:1ZIV}.
HELIX 209 211 {ECO:0000244|PDB:1ZIV}.
HELIX 216 226 {ECO:0000244|PDB:1ZIV}.
STRAND 229 233 {ECO:0000244|PDB:1ZIV}.
HELIX 239 241 {ECO:0000244|PDB:1ZIV}.
STRAND 256 266 {ECO:0000244|PDB:1ZIV}.
STRAND 269 277 {ECO:0000244|PDB:1ZIV}.
HELIX 294 298 {ECO:0000244|PDB:1ZIV}.
HELIX 301 306 {ECO:0000244|PDB:1ZIV}.
STRAND 313 320 {ECO:0000244|PDB:1ZIV}.
HELIX 321 327 {ECO:0000244|PDB:1ZIV}.
STRAND 330 334 {ECO:0000244|PDB:1ZIV}.
SEQUENCE 690 AA; 79097 MW; 02176C04BE1E5C23 CRC64;
MPYLYRAPGP QAHPVPKDAR ITHSSGQSFE QMRQECLQRG TLFEDADFPA SNSSLFYSER
PQIPFVWKRP GEIVKNPEFI LGGATRTDIC QGELGDCWLL AAIASLTLNQ KALARVIPQD
QSFGPGYAGI FHFQFWQHSE WLDVVIDDRL PTFRDRLVFL HSADHNEFWS ALLEKAYAKL
NGSYEALKGG SAIEAMEDFT GGVAETFQTK EAPENFYEIL EKALKRGSLL GCFIDTRSAA
ESEARTPFGL IKGHAYSVTG IDQVSFRGQR IELIRIRNPW GQVEWNGSWS DSSPEWRSVG
PAEQKRLCHT ALDDGEFWMA FKDFKAHFDK VEICNLTPDA LEEDAIHKWE VTVHQGSWVR
GSTAGGCRNF LDTFWTNPQI KLSLTEKDEG QEECSFLVAL MQKDRRKLKR FGANVLTIGY
AIYECPDKDE HLNKDFFRYH ASRARSKTFI NLREVSDRFK LPPGEYILIP STFEPHQEAD
FCLRIFSEKK AITRDMDGNV DIDLPEPPKP TPPDQETEEE QRFRALFEQV AGEDMEVTAE
ELEYVLNAVL QKKKDIKFKK LSLISCKNII SLMDTSGNGK LEFDEFKVFW DKLKQWINLF
LRFDADKSGT MSTYELRTAL KAAGFQLSSH LLQLIVLRYA DEELQLDFDD FLNCLVRLEN
ASRVFQALST KNKEFIHLNI NEFIHLTMNI


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