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Calpain-2 catalytic subunit (EC 3.4.22.53) (Calcium-activated neutral proteinase 2) (CANP 2) (Calpain M-type) (Calpain large polypeptide L2) (Calpain-2 large subunit) (Millimolar-calpain) (M-calpain)

 CAN2_HUMAN              Reviewed;         700 AA.
P17655; A6NDG7; B7ZA96; E7ES58; Q16738; Q6PJT3; Q8WU26; Q9HBB1;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 6.
30-AUG-2017, entry version 210.
RecName: Full=Calpain-2 catalytic subunit;
EC=3.4.22.53;
AltName: Full=Calcium-activated neutral proteinase 2;
Short=CANP 2;
AltName: Full=Calpain M-type;
AltName: Full=Calpain large polypeptide L2;
AltName: Full=Calpain-2 large subunit;
AltName: Full=Millimolar-calpain;
Short=M-calpain;
Flags: Precursor;
Name=CAPN2; Synonyms=CANPL2;
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), AND VARIANT GLU-22.
PubMed=2852952; DOI=10.1021/bi00421a022;
Imajoh S., Aoki K., Ohno S., Emori Y., Kawasaki H., Sugihara H.,
Suzuki K.;
"Molecular cloning of the cDNA for the large subunit of the high-Ca2+-
requiring form of human Ca2+-activated neutral protease.";
Biochemistry 27:8122-8128(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLU-22.
TISSUE=Astrocytoma;
PubMed=10944468; DOI=10.1006/bbrc.2000.3282;
Ye Z., Connor J.R.;
"cDNA cloning by amplification of circularized first strand cDNAs
reveals non-IRE-regulated iron-responsive mRNAs.";
Biochem. Biophys. Res. Commun. 275:223-227(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-22; GLY-68;
ARG-476; GLN-521; GLN-568 AND GLN-677.
NIEHS SNPs program;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
GLU-22.
TISSUE=Pancreas, Placenta, and Skin;
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-79, AND VARIANTS GLU-22 AND
GLY-68.
TISSUE=Lymph node;
PubMed=2539381;
Hata A., Ohno S., Akita Y., Suzuki K.;
"Tandemly reiterated negative enhancer-like elements regulate
transcription of a human gene for the large subunit of calcium-
dependent protease.";
J. Biol. Chem. 264:6404-6411(1989).
[8]
PROTEIN SEQUENCE OF 2-12.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[9]
FUNCTION.
PubMed=17650508; DOI=10.1074/jbc.M609608200;
Sanchez-Sanchez F., Martinez-Redondo F., Aroca-Aguilar J.D.,
Coca-Prados M., Escribano J.;
"Characterization of the intracellular proteolytic cleavage of
myocilin and identification of calpain II as a myocilin-processing
protease.";
J. Biol. Chem. 282:27810-27824(2007).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=10639123; DOI=10.1073/pnas.97.2.588;
Strobl S., Fernandez-Catalan C., Braun M., Huber R., Masumoto H.,
Nakagawa K., Irie A., Sorimachi H., Bourenkow G., Bartunik H.,
Suzuki K., Bode W.;
"The crystal structure of calcium-free human m-calpain suggests an
electrostatic switch mechanism for activation by calcium.";
Proc. Natl. Acad. Sci. U.S.A. 97:588-592(2000).
[13]
VARIANT [LARGE SCALE ANALYSIS] GLU-22, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
-!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease which
catalyzes limited proteolysis of substrates involved in
cytoskeletal remodeling and signal transduction. Proteolytically
cleaves MYOC at 'Arg-226' (PubMed:17650508). Proteolytically
cleaves CPEB3 following neuronal stimulation which abolishes CPEB3
translational repressor activity, leading to translation of CPEB3
target mRNAs (By similarity). {ECO:0000250|UniProtKB:O08529,
ECO:0000269|PubMed:17650508}.
-!- CATALYTIC ACTIVITY: Broad endopeptidase specificity.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 7 Ca(2+) ions. {ECO:0000250};
-!- ENZYME REGULATION: Activated by 200-1000 micromolar concentrations
of calcium and inhibited by calpastatin.
-!- SUBUNIT: Forms a heterodimer with a small (regulatory) subunit
(CAPNS1). Interacts with CPEB3; this leads to cleavage of CPEB3.
{ECO:0000250|UniProtKB:O08529, ECO:0000250|UniProtKB:Q07009}.
-!- INTERACTION:
P04632:CAPNS1; NbExp=3; IntAct=EBI-1028956, EBI-711828;
Q8IUH5:ZDHHC17; NbExp=2; IntAct=EBI-1028956, EBI-524753;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Translocates
to the plasma membrane upon Ca(2+) binding.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P17655-1; Sequence=Displayed;
Name=2;
IsoId=P17655-2; Sequence=VSP_043027, VSP_043028;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH07686.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH11828.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/capn2/";
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EMBL; M23254; AAA35645.1; -; mRNA.
EMBL; AF261089; AAF99682.1; -; mRNA.
EMBL; AK316211; BAH14582.1; -; mRNA.
EMBL; AY835586; AAV80421.1; -; Genomic_DNA.
EMBL; AC096542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC099065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC007686; AAH07686.1; ALT_SEQ; mRNA.
EMBL; BC011828; AAH11828.1; ALT_SEQ; mRNA.
EMBL; BC021303; AAH21303.1; -; mRNA.
EMBL; J04700; AAA52760.1; -; Genomic_DNA.
CCDS; CCDS31035.1; -. [P17655-1]
CCDS; CCDS53478.1; -. [P17655-2]
PIR; S10590; CIHUH2.
RefSeq; NP_001139540.1; NM_001146068.1. [P17655-2]
RefSeq; NP_001739.2; NM_001748.4.
UniGene; Hs.350899; -.
PDB; 1KFU; X-ray; 2.50 A; L=2-700.
PDB; 1KFX; X-ray; 3.15 A; L=2-700.
PDB; 2NQA; X-ray; 2.20 A; A/B=48-346.
PDBsum; 1KFU; -.
PDBsum; 1KFX; -.
PDBsum; 2NQA; -.
ProteinModelPortal; P17655; -.
SMR; P17655; -.
BioGrid; 107274; 53.
IntAct; P17655; 13.
MINT; MINT-120195; -.
STRING; 9606.ENSP00000295006; -.
BindingDB; P17655; -.
ChEMBL; CHEMBL2382; -.
GuidetoPHARMACOLOGY; 2337; -.
MEROPS; C02.002; -.
iPTMnet; P17655; -.
PhosphoSitePlus; P17655; -.
SwissPalm; P17655; -.
BioMuta; CAPN2; -.
DMDM; 317373596; -.
EPD; P17655; -.
MaxQB; P17655; -.
PaxDb; P17655; -.
PeptideAtlas; P17655; -.
PRIDE; P17655; -.
DNASU; 824; -.
Ensembl; ENST00000295006; ENSP00000295006; ENSG00000162909. [P17655-1]
Ensembl; ENST00000433674; ENSP00000413158; ENSG00000162909. [P17655-2]
GeneID; 824; -.
KEGG; hsa:824; -.
UCSC; uc001hob.5; human. [P17655-1]
CTD; 824; -.
DisGeNET; 824; -.
GeneCards; CAPN2; -.
HGNC; HGNC:1479; CAPN2.
HPA; HPA024470; -.
MIM; 114230; gene.
neXtProt; NX_P17655; -.
OpenTargets; ENSG00000162909; -.
PharmGKB; PA26060; -.
eggNOG; KOG0045; Eukaryota.
eggNOG; ENOG410XP0B; LUCA.
GeneTree; ENSGT00760000118971; -.
HOVERGEN; HBG012645; -.
InParanoid; P17655; -.
KO; K03853; -.
OMA; DTYKKWK; -.
OrthoDB; EOG091G049E; -.
PhylomeDB; P17655; -.
TreeFam; TF314748; -.
BRENDA; 3.4.22.53; 2681.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
SIGNOR; P17655; -.
ChiTaRS; CAPN2; human.
EvolutionaryTrace; P17655; -.
GeneWiki; CAPN2; -.
GenomeRNAi; 824; -.
PRO; PR:P17655; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000162909; -.
CleanEx; HS_CAPN2; -.
ExpressionAtlas; P17655; baseline and differential.
Genevisible; P17655; HS.
GO; GO:0000785; C:chromatin; IEA:Ensembl.
GO; GO:0030864; C:cortical actin cytoskeleton; TAS:BHF-UCL.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
GO; GO:0005764; C:lysosome; IEA:Ensembl.
GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0031143; C:pseudopodium; IDA:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IDA:BHF-UCL.
GO; GO:0008234; F:cysteine-type peptidase activity; TAS:ProtInc.
GO; GO:0008092; F:cytoskeletal protein binding; NAS:BHF-UCL.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0001824; P:blastocyst development; IEA:Ensembl.
GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0007520; P:myoblast fusion; IEA:Ensembl.
GO; GO:0016540; P:protein autoprocessing; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IDA:BHF-UCL.
GO; GO:0051493; P:regulation of cytoskeleton organization; TAS:BHF-UCL.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
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; IPR029539; CAPN2.
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:SF340; PTHR10183:SF340; 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.
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; Acetylation; Alternative splicing; Calcium;
Cell membrane; Complete proteome; Cytoplasm;
Direct protein sequencing; Hydrolase; Membrane; Metal-binding;
Polymorphism; Protease; Reference proteome; Repeat; Thiol protease.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:12665801}.
PROPEP 2 19 Anchors to the small subunit.
{ECO:0000255}.
/FTId=PRO_0000026487.
CHAIN 20 700 Calpain-2 catalytic subunit.
/FTId=PRO_0000026488.
DOMAIN 45 344 Calpain catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00239}.
DOMAIN 572 605 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 602 637 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 667 700 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 585 596 1.
CA_BIND 615 626 2.
REGION 345 514 Domain III.
REGION 515 529 Linker.
REGION 530 700 Domain IV.
ACT_SITE 105 105 {ECO:0000250}.
ACT_SITE 262 262 {ECO:0000250}.
ACT_SITE 286 286 {ECO:0000250}.
METAL 89 89 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 91 91 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 96 96 Calcium 3. {ECO:0000250}.
METAL 175 175 Calcium 3. {ECO:0000250}.
METAL 229 229 Calcium 2. {ECO:0000250}.
METAL 230 230 Calcium 2. {ECO:0000250}.
METAL 292 292 Calcium 4. {ECO:0000250}.
METAL 299 299 Calcium 4. {ECO:0000250}.
METAL 323 323 Calcium 4; via carbonyl oxygen.
{ECO:0000250}.
METAL 542 542 Calcium 5; via carbonyl oxygen.
{ECO:0000250}.
METAL 545 545 Calcium 5. {ECO:0000250}.
METAL 547 547 Calcium 5; via carbonyl oxygen.
{ECO:0000250}.
METAL 552 552 Calcium 5. {ECO:0000250}.
METAL 585 585 Calcium 6. {ECO:0000250}.
METAL 587 587 Calcium 6. {ECO:0000250}.
METAL 589 589 Calcium 6; via carbonyl oxygen.
{ECO:0000250}.
METAL 591 591 Calcium 6; via carbonyl oxygen.
{ECO:0000250}.
METAL 596 596 Calcium 6. {ECO:0000250}.
METAL 615 615 Calcium 7. {ECO:0000250}.
METAL 617 617 Calcium 7. {ECO:0000250}.
METAL 619 619 Calcium 7; via carbonyl oxygen.
{ECO:0000250}.
METAL 621 621 Calcium 7; via carbonyl oxygen.
{ECO:0000250}.
METAL 626 626 Calcium 7. {ECO:0000250}.
METAL 658 658 Calcium 1. {ECO:0000250}.
METAL 661 661 Calcium 1. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378}.
VAR_SEQ 1 78 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043027.
VAR_SEQ 79 79 T -> M (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043028.
VARIANT 22 22 D -> E (in dbSNP:rs25655).
{ECO:0000244|PubMed:21269460,
ECO:0000269|PubMed:10944468,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2539381,
ECO:0000269|PubMed:2852952,
ECO:0000269|Ref.4}.
/FTId=VAR_014435.
VARIANT 68 68 S -> G (in dbSNP:rs2230083).
{ECO:0000269|PubMed:2539381,
ECO:0000269|Ref.4}.
/FTId=VAR_021404.
VARIANT 476 476 K -> R (in dbSNP:rs9804140).
{ECO:0000269|Ref.4}.
/FTId=VAR_021405.
VARIANT 521 521 E -> Q (in dbSNP:rs28370127).
{ECO:0000269|Ref.4}.
/FTId=VAR_021406.
VARIANT 568 568 K -> Q (in dbSNP:rs17599).
{ECO:0000269|Ref.4}.
/FTId=VAR_014436.
VARIANT 677 677 K -> Q (in dbSNP:rs2230082).
{ECO:0000269|Ref.4}.
/FTId=VAR_021407.
CONFLICT 73 74 IE -> MR (in Ref. 1; AAA35645).
{ECO:0000305}.
CONFLICT 256 256 Q -> K (in Ref. 2; AAF99682).
{ECO:0000305}.
CONFLICT 300 300 N -> S (in Ref. 2; AAF99682).
{ECO:0000305}.
CONFLICT 534 534 F -> V (in Ref. 1; AAA35645 and 2;
AAF99682). {ECO:0000305}.
HELIX 4 16 {ECO:0000244|PDB:1KFU}.
TURN 17 19 {ECO:0000244|PDB:1KFU}.
HELIX 27 29 {ECO:0000244|PDB:1KFU}.
HELIX 32 42 {ECO:0000244|PDB:1KFU}.
STRAND 49 51 {ECO:0000244|PDB:1KFU}.
HELIX 55 58 {ECO:0000244|PDB:2NQA}.
STRAND 60 68 {ECO:0000244|PDB:1KFU}.
STRAND 74 76 {ECO:0000244|PDB:2NQA}.
HELIX 78 81 {ECO:0000244|PDB:2NQA}.
STRAND 82 84 {ECO:0000244|PDB:1KFX}.
HELIX 94 96 {ECO:0000244|PDB:2NQA}.
STRAND 97 99 {ECO:0000244|PDB:1KFX}.
HELIX 105 115 {ECO:0000244|PDB:2NQA}.
HELIX 118 124 {ECO:0000244|PDB:2NQA}.
STRAND 131 134 {ECO:0000244|PDB:1KFU}.
STRAND 136 144 {ECO:0000244|PDB:2NQA}.
STRAND 146 155 {ECO:0000244|PDB:2NQA}.
STRAND 158 161 {ECO:0000244|PDB:2NQA}.
STRAND 164 167 {ECO:0000244|PDB:2NQA}.
STRAND 169 175 {ECO:0000244|PDB:1KFU}.
HELIX 177 189 {ECO:0000244|PDB:2NQA}.
STRAND 190 192 {ECO:0000244|PDB:2NQA}.
HELIX 193 195 {ECO:0000244|PDB:2NQA}.
STRAND 196 199 {ECO:0000244|PDB:2NQA}.
TURN 204 206 {ECO:0000244|PDB:2NQA}.
HELIX 207 209 {ECO:0000244|PDB:2NQA}.
STRAND 212 216 {ECO:0000244|PDB:2NQA}.
HELIX 224 233 {ECO:0000244|PDB:2NQA}.
STRAND 237 241 {ECO:0000244|PDB:2NQA}.
HELIX 247 249 {ECO:0000244|PDB:2NQA}.
STRAND 259 261 {ECO:0000244|PDB:2NQA}.
STRAND 264 274 {ECO:0000244|PDB:2NQA}.
STRAND 277 285 {ECO:0000244|PDB:2NQA}.
STRAND 294 297 {ECO:0000244|PDB:1KFU}.
STRAND 299 301 {ECO:0000244|PDB:1KFU}.
HELIX 302 306 {ECO:0000244|PDB:2NQA}.
HELIX 309 315 {ECO:0000244|PDB:2NQA}.
STRAND 321 327 {ECO:0000244|PDB:2NQA}.
HELIX 328 334 {ECO:0000244|PDB:2NQA}.
STRAND 336 341 {ECO:0000244|PDB:2NQA}.
HELIX 344 346 {ECO:0000244|PDB:1KFU}.
STRAND 347 349 {ECO:0000244|PDB:1KFU}.
STRAND 363 365 {ECO:0000244|PDB:1KFU}.
TURN 367 370 {ECO:0000244|PDB:1KFU}.
TURN 378 380 {ECO:0000244|PDB:1KFU}.
HELIX 381 383 {ECO:0000244|PDB:1KFU}.
STRAND 388 390 {ECO:0000244|PDB:1KFU}.
STRAND 400 402 {ECO:0000244|PDB:1KFU}.
STRAND 406 413 {ECO:0000244|PDB:1KFU}.
STRAND 420 425 {ECO:0000244|PDB:1KFU}.
STRAND 429 435 {ECO:0000244|PDB:1KFU}.
TURN 442 444 {ECO:0000244|PDB:1KFU}.
HELIX 450 455 {ECO:0000244|PDB:1KFU}.
STRAND 459 461 {ECO:0000244|PDB:1KFX}.
STRAND 466 471 {ECO:0000244|PDB:1KFU}.
STRAND 474 476 {ECO:0000244|PDB:1KFU}.
STRAND 479 492 {ECO:0000244|PDB:1KFU}.
STRAND 495 505 {ECO:0000244|PDB:1KFU}.
STRAND 507 509 {ECO:0000244|PDB:1KFX}.
STRAND 527 530 {ECO:0000244|PDB:1KFU}.
HELIX 533 541 {ECO:0000244|PDB:1KFU}.
STRAND 542 546 {ECO:0000244|PDB:1KFU}.
HELIX 550 560 {ECO:0000244|PDB:1KFU}.
TURN 561 564 {ECO:0000244|PDB:1KFU}.
HELIX 574 582 {ECO:0000244|PDB:1KFU}.
STRAND 586 588 {ECO:0000244|PDB:1KFU}.
STRAND 590 592 {ECO:0000244|PDB:1KFU}.
HELIX 595 612 {ECO:0000244|PDB:1KFU}.
STRAND 622 624 {ECO:0000244|PDB:1KFU}.
HELIX 627 630 {ECO:0000244|PDB:1KFU}.
TURN 631 635 {ECO:0000244|PDB:1KFU}.
HELIX 640 650 {ECO:0000244|PDB:1KFU}.
STRAND 655 657 {ECO:0000244|PDB:1KFU}.
HELIX 659 679 {ECO:0000244|PDB:1KFU}.
STRAND 687 690 {ECO:0000244|PDB:1KFU}.
HELIX 691 698 {ECO:0000244|PDB:1KFU}.
SEQUENCE 700 AA; 79995 MW; 8CF8294351A024E3 CRC64;
MAGIAAKLAK DREAAEGLGS HDRAIKYLNQ DYEALRNECL EAGTLFQDPS FPAIPSALGF
KELGPYSSKT RGIEWKRPTE ICADPQFIIG GATRTDICQG ALGDCWLLAA IASLTLNEEI
LARVVPLNQS FQENYAGIFH FQFWQYGEWV EVVVDDRLPT KDGELLFVHS AEGSEFWSAL
LEKAYAKING CYEALSGGAT TEGFEDFTGG IAEWYELKKP PPNLFKIIQK ALQKGSLLGC
SIDITSAADS EAITFQKLVK GHAYSVTGAE EVESNGSLQK LIRIRNPWGE VEWTGRWNDN
CPSWNTIDPE ERERLTRRHE DGEFWMSFSD FLRHYSRLEI CNLTPDTLTS DTYKKWKLTK
MDGNWRRGST AGGCRNYPNT FWMNPQYLIK LEEEDEDEED GESGCTFLVG LIQKHRRRQR
KMGEDMHTIG FGIYEVPEEL SGQTNIHLSK NFFLTNRARE RSDTFINLRE VLNRFKLPPG
EYILVPSTFE PNKDGDFCIR VFSEKKADYQ AVDDEIEANL EEFDISEDDI DDGFRRLFAQ
LAGEDAEISA FELQTILRRV LAKRQDIKSD GFSIETCKIM VDMLDSDGSG KLGLKEFYIL
WTKIQKYQKI YREIDVDRSG TMNSYEMRKA LEEAGFKMPC QLHQVIVARF ADDQLIIDFD
NFVRCLVRLE TLFKIFKQLD PENTGTIELD LISWLCFSVL


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