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Protein S100-A12 (CGRP) (Calcium-binding protein in amniotic fluid 1) (CAAF1) (Calgranulin-C) (CAGC) (Extracellular newly identified RAGE-binding protein) (EN-RAGE) (Migration inhibitory factor-related protein 6) (MRP-6) (p6) (Neutrophil S100 protein) (S100 calcium-binding protein A12) [Cleaved into: Calcitermin]

 S10AC_HUMAN             Reviewed;          92 AA.
P80511; P83219; Q5SY66; Q7M4R1;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 170.
RecName: Full=Protein S100-A12;
AltName: Full=CGRP;
AltName: Full=Calcium-binding protein in amniotic fluid 1;
Short=CAAF1;
AltName: Full=Calgranulin-C;
Short=CAGC;
AltName: Full=Extracellular newly identified RAGE-binding protein;
Short=EN-RAGE;
AltName: Full=Migration inhibitory factor-related protein 6;
Short=MRP-6;
Short=p6;
AltName: Full=Neutrophil S100 protein;
AltName: Full=S100 calcium-binding protein A12;
Contains:
RecName: Full=Calcitermin;
Name=S100A12;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=8619860; DOI=10.1006/bbrc.1996.0600;
Yamamura T., Hitomi J., Nagasaki K., Suzuki M., Takahashi E.,
Saito S., Tsukada T., Yamaguchi K.;
"Human CAAF1 gene -- molecular cloning, gene structure, and chromosome
mapping.";
Biochem. Biophys. Res. Commun. 221:356-360(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=8985590; DOI=10.1016/S0143-4160(96)90087-1;
Wicki R., Marenholz I., Mischke D., Schaefer B.W., Heizmann C.W.;
"Characterization of the human S100A12 (calgranulin C, p6, CAAF1,
CGRP) gene, a new member of the S100 gene cluster on chromosome
1q21.";
Cell Calcium 20:459-464(1996).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Blood;
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).
[5]
PROTEIN SEQUENCE OF 2-92.
PubMed=8619876; DOI=10.1006/bbrc.1996.0616;
Marti T., Erttmann K.D., Gallin M.Y.;
"Host-parasite interaction in human onchocerciasis: identification and
sequence analysis of a novel human calgranulin.";
Biochem. Biophys. Res. Commun. 221:454-458(1996).
[6]
PROTEIN SEQUENCE OF 2-92.
TISSUE=Neutrophil;
PubMed=8769108; DOI=10.1006/bbrc.1996.1144;
Ilg E.C., Troxler H., Buergisser D.M., Kuster T., Markert M.,
Guignard F., Hunziker P., Birchler N., Heizmann C.W.;
"Amino acid sequence determination of human S100A12 (P6, calgranulin
C, CGRP, CAAF1) by tandem mass spectrometry.";
Biochem. Biophys. Res. Commun. 225:146-150(1996).
[7]
PROTEIN SEQUENCE OF 2-21.
PubMed=7626002; DOI=10.1042/bj3090395;
Guignard F., Mauel J., Markert M.;
"Identification and characterization of a novel human neutrophil
protein related to the S100 family.";
Biochem. J. 309:395-401(1995).
[8]
PROTEIN SEQUENCE OF 2-16.
PubMed=1860454; DOI=10.3109/01902149109062865;
Singh G., Katyal S.L., Brown W.E., Kennedy A.L., Wong-Chong M.-L.,
Gottron S.A.;
"Identification, isolation, and partial characterization of a 7.5-kDa
surfactant-associated protein.";
Exp. Lung Res. 17:559-567(1991).
[9]
PROTEIN SEQUENCE OF 78-92, FUNCTION AS AN ANTIMICROBIAL PROTEIN, AND
MASS SPECTROMETRY.
TISSUE=Nasal mucus;
PubMed=11522286; DOI=10.1016/S0014-5793(01)02731-4;
Cole A.M., Kim Y.-H., Tahk S., Hong T., Weis P., Waring A.J., Ganz T.;
"Calcitermin, a novel antimicrobial peptide isolated from human airway
secretions.";
FEBS Lett. 504:5-10(2001).
[10]
INTERACTION WITH CACYBP.
PubMed=12042313; DOI=10.1074/jbc.M203602200;
Filipek A., Jastrzebska B., Nowotny M., Kuznicki J.;
"CacyBP/SIP, a calcyclin and Siah-1-interacting protein, binds EF-hand
proteins of the S100 family.";
J. Biol. Chem. 277:28848-28852(2002).
[11]
REVIEW.
PubMed=12645006; DOI=10.1002/jemt.10300;
Moroz O.V., Dodson G.G., Wilson K.S., Lukanidin E., Bronstein I.B.;
"Multiple structural states of S100A12: A key to its functional
diversity.";
Microsc. Res. Tech. 60:581-592(2003).
[12]
FUNCTION.
PubMed=17208591; DOI=10.1016/j.jaci.2006.08.021;
Yang Z., Yan W.X., Cai H., Tedla N., Armishaw C., Di Girolamo N.,
Wang H.W., Hampartzoumian T., Simpson J.L., Gibson P.G., Hunt J.,
Hart P., Hughes J.M., Perry M.A., Alewood P.F., Geczy C.L.;
"S100A12 provokes mast cell activation: a potential amplification
pathway in asthma and innate immunity.";
J. Allergy Clin. Immunol. 119:106-114(2007).
[13]
FUNCTION, AND DOMAIN HINGE.
PubMed=18292089; DOI=10.1074/jbc.M710388200;
Yan W.X., Armishaw C., Goyette J., Yang Z., Cai H., Alewood P.,
Geczy C.L.;
"Mast cell and monocyte recruitment by S100A12 and its hinge domain.";
J. Biol. Chem. 283:13035-13043(2008).
[14]
REVIEW.
PubMed=18443896; DOI=10.1007/s00726-008-0097-7;
Pietzsch J., Hoppmann S.;
"Human S100A12: a novel key player in inflammation?";
Amino Acids 36:381-389(2009).
[15]
REVIEW.
PubMed=20523765; DOI=10.2174/187152309789838975;
Hsu K., Champaiboon C., Guenther B.D., Sorenson B.S., Khammanivong A.,
Ross K.F., Geczy C.L., Herzberg M.C.;
"Anti-infective protective properties of S100 calgranulins.";
Antiinflamm. Antiallergy Agents Med. Chem. 8:290-305(2009).
[16]
FUNCTION, SUBUNIT, AND INTERACTION WITH AGER.
PubMed=19386136; DOI=10.1186/1471-2091-10-11;
Moroz O.V., Burkitt W., Wittkowski H., He W., Ianoul A.,
Novitskaya V., Xie J., Polyakova O., Lednev I.K., Shekhtman A.,
Derrick P.J., Bjoerk P., Foell D., Bronstein I.B.;
"Both Ca2+ and Zn2+ are essential for S100A12 protein oligomerization
and function.";
BMC Biochem. 10:11-11(2009).
[17]
REVIEW.
PubMed=19935766; DOI=10.1038/icb.2009.88;
Perera C., McNeil H.P., Geczy C.L.;
"S100 Calgranulins in inflammatory arthritis.";
Immunol. Cell Biol. 88:41-49(2010).
[18]
REVIEW.
PubMed=20213444; DOI=10.1007/s00726-010-0528-0;
Goyette J., Geczy C.L.;
"Inflammation-associated S100 proteins: new mechanisms that regulate
function.";
Amino Acids 41:821-842(2011).
[19]
REVIEW, AND SUBCELLULAR LOCATION.
PubMed=22811950; DOI=10.1155/2012/907078;
Meijer B., Gearry R.B., Day A.S.;
"The role of S100A12 as a systemic marker of inflammation.";
Int. J. Inflamm. 2012:907078-907078(2012).
[20]
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).
[21]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
PubMed=11134923; DOI=10.1107/S090744490001458X;
Moroz O.V., Antson A.A., Murshudov G.N., Maitland N.J., Dodson G.G.,
Wilson K.S., Skibshoj I., Lukanidin E.M., Bronstein I.B.;
"The three-dimensional structure of human S100A12.";
Acta Crystallogr. D 57:20-29(2001).
[22]
X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS), AND COPPER-BINDING.
PubMed=12777802; DOI=10.1107/S0907444903004700;
Moroz O.V., Antson A.A., Grist S.J., Maitland N.J., Dodson G.G.,
Wilson K.S., Lukanidin E., Bronstein I.B.;
"Structure of the human S100A12-copper complex: implications for host-
parasite defence.";
Acta Crystallogr. D 59:859-867(2003).
[23]
X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 2-92, AND ZINC-BINDING.
PubMed=19501594; DOI=10.1016/j.jmb.2009.06.004;
Moroz O.V., Blagova E.V., Wilkinson A.J., Wilson K.S., Bronstein I.B.;
"The crystal structures of human S100A12 in apo form and in complex
with zinc: new insights into S100A12 oligomerisation.";
J. Mol. Biol. 391:536-551(2009).
-!- FUNCTION: S100A12 is a calcium-, zinc- and copper-binding protein
which plays a prominent role in the regulation of inflammatory
processes and immune response. Its proinflammatory activity
involves recruitment of leukocytes, promotion of cytokine and
chemokine production, and regulation of leukocyte adhesion and
migration. Acts as an alarmin or a danger associated molecular
pattern (DAMP) molecule and stimulates innate immune cells via
binding to receptor for advanced glycation endproducts (AGER).
Binding to AGER activates the MAP-kinase and NF-kappa-B signaling
pathways leading to production of proinflammatory cytokines and
up-regulation of cell adhesion molecules ICAM1 and VCAM1. Acts as
a monocyte and mast cell chemoattractant. Can stimulate mast cell
degranulation and activation which generates chemokines, histamine
and cytokines inducing further leukocyte recruitment to the sites
of inflammation. Can inhibit the activity of matrix
metalloproteinases; MMP2, MMP3 and MMP9 by chelating Zn(2+) from
their active sites. Possesses filariacidal and filariastatic
activity. Calcitermin possesses antifungal activity against
C.albicans and is also active against E.coli and P.aeruginosa but
not L.monocytogenes and S.aureus. {ECO:0000269|PubMed:11522286,
ECO:0000269|PubMed:17208591, ECO:0000269|PubMed:18292089,
ECO:0000269|PubMed:19386136}.
-!- SUBUNIT: Homodimer. Homooligomer (tetramer or hexamer) in the
presence of calcium, zinc and copper ions. Interacts with AGER and
both calcium and zinc are essential for the interaction. Interacts
with CACYBP in a calcium-dependent manner.
{ECO:0000269|PubMed:12042313, ECO:0000269|PubMed:19386136}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22811950}.
Cytoplasm {ECO:0000269|PubMed:22811950}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:22811950}. Cell membrane
{ECO:0000269|PubMed:22811950}; Peripheral membrane protein
{ECO:0000269|PubMed:22811950}. Note=Predominantly localized in the
cytoplasm. Upon elevation of the intracellular calcium level,
translocated from the cytoplasm to the cytoskeleton and the cell
membrane. Upon neutrophil activation is secreted via a
microtubule-mediated, alternative pathway.
-!- TISSUE SPECIFICITY: Predominantly expressed by neutrophils,
monocytes and activated macrophages. Expressed by eosinophils and
macrophages in asthmatic airways in regions where mast cells
accumulate. Found in high concentrations in the serum of patients
suffering from various inflammatory disorders, such as rheumatoid
arthritis, psoriatic arthritis, Crohn's disease, ulcerative
colitis, and Kawasaki disease.
-!- DOMAIN: The hinge domain contributes significantly to its
chemotactic properties. {ECO:0000269|PubMed:18292089}.
-!- MASS SPECTROMETRY: Mass=10444; Method=Electrospray; Range=2-92;
Evidence={ECO:0000269|PubMed:11522286};
-!- MASS SPECTROMETRY: Mass=1688.9; Method=MALDI; Range=78-92;
Evidence={ECO:0000269|PubMed:11522286};
-!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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EMBL; D49549; BAA08497.1; -; mRNA.
EMBL; D83657; BAA12030.1; -; Genomic_DNA.
EMBL; D83664; BAA12036.1; -; mRNA.
EMBL; X97859; CAA66453.1; -; mRNA.
EMBL; X98289; CAB94792.1; -; Genomic_DNA.
EMBL; X98290; CAB94792.1; JOINED; Genomic_DNA.
EMBL; AL591704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC070294; AAH70294.1; -; mRNA.
CCDS; CCDS1037.1; -.
PIR; A61522; A61522.
PIR; JC4712; JC4712.
RefSeq; NP_005612.1; NM_005621.1.
UniGene; Hs.19413; -.
PDB; 1E8A; X-ray; 1.95 A; A/B=2-92.
PDB; 1GQM; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=2-92.
PDB; 1ODB; X-ray; 2.19 A; A/B/C/D/E/F=2-92.
PDB; 2M9G; NMR; -; A/B=1-92.
PDB; 2WC8; X-ray; 1.88 A; A/B/C/D=2-92.
PDB; 2WCB; X-ray; 1.73 A; A/B=2-92.
PDB; 2WCE; X-ray; 1.77 A; A/B=2-92.
PDB; 2WCF; X-ray; 2.78 A; A/B/C/D/E/F=2-92.
PDBsum; 1E8A; -.
PDBsum; 1GQM; -.
PDBsum; 1ODB; -.
PDBsum; 2M9G; -.
PDBsum; 2WC8; -.
PDBsum; 2WCB; -.
PDBsum; 2WCE; -.
PDBsum; 2WCF; -.
ProteinModelPortal; P80511; -.
SMR; P80511; -.
BioGrid; 112191; 1.
IntAct; P80511; 1.
MINT; MINT-239108; -.
STRING; 9606.ENSP00000357726; -.
DrugBank; DB01025; Amlexanox.
DrugBank; DB00768; Olopatadine.
iPTMnet; P80511; -.
PhosphoSitePlus; P80511; -.
BioMuta; S100A12; -.
DMDM; 2507565; -.
PaxDb; P80511; -.
PeptideAtlas; P80511; -.
PRIDE; P80511; -.
TopDownProteomics; P80511; -.
DNASU; 6283; -.
Ensembl; ENST00000368737; ENSP00000357726; ENSG00000163221.
GeneID; 6283; -.
KEGG; hsa:6283; -.
UCSC; uc001fbr.2; human.
CTD; 6283; -.
DisGeNET; 6283; -.
EuPathDB; HostDB:ENSG00000163221.8; -.
GeneCards; S100A12; -.
HGNC; HGNC:10489; S100A12.
HPA; CAB025872; -.
HPA; HPA002881; -.
MIM; 603112; gene.
neXtProt; NX_P80511; -.
OpenTargets; ENSG00000163221; -.
PharmGKB; PA34901; -.
eggNOG; ENOG410JDIE; Eukaryota.
eggNOG; ENOG411177M; LUCA.
GeneTree; ENSGT00900000141006; -.
HOGENOM; HOG000246968; -.
HOVERGEN; HBG001479; -.
InParanoid; P80511; -.
OMA; NTKDQAT; -.
OrthoDB; EOG091G12NB; -.
PhylomeDB; P80511; -.
TreeFam; TF332727; -.
Reactome; R-HSA-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-HSA-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
Reactome; R-HSA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-879415; Advanced glycosylation endproduct receptor signaling.
Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
EvolutionaryTrace; P80511; -.
GeneWiki; S100A12; -.
GenomeRNAi; 6283; -.
PRO; PR:P80511; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000163221; -.
CleanEx; HS_S100A12; -.
Genevisible; P80511; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0005509; F:calcium ion binding; TAS:UniProtKB.
GO; GO:0005507; F:copper ion binding; TAS:UniProtKB.
GO; GO:0050786; F:RAGE receptor binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; TAS:UniProtKB.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
GO; GO:0050663; P:cytokine secretion; TAS:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; TAS:UniProtKB.
GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
GO; GO:0031640; P:killing of cells of other organism; IDA:UniProtKB.
GO; GO:0045576; P:mast cell activation; TAS:UniProtKB.
GO; GO:0002548; P:monocyte chemotaxis; TAS:UniProtKB.
GO; GO:0030593; P:neutrophil chemotaxis; TAS:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0050729; P:positive regulation of inflammatory response; TAS:UniProtKB.
GO; GO:0043406; P:positive regulation of MAP kinase activity; TAS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; TAS:UniProtKB.
GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR001751; S100/CaBP-9k_CS.
InterPro; IPR013787; S100_Ca-bd_sub.
Pfam; PF01023; S_100; 1.
SMART; SM01394; S_100; 1.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS50222; EF_HAND_2; 1.
PROSITE; PS00303; S100_CABP; 1.
1: Evidence at protein level;
3D-structure; Antibiotic; Antimicrobial; Calcium; Cell membrane;
Complete proteome; Copper; Cytoplasm; Cytoskeleton;
Direct protein sequencing; Fungicide; Immunity; Inflammatory response;
Innate immunity; Membrane; Metal-binding; Reference proteome; Repeat;
Secreted; Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1860454,
ECO:0000269|PubMed:7626002,
ECO:0000269|PubMed:8619876,
ECO:0000269|PubMed:8769108}.
CHAIN 2 92 Protein S100-A12.
/FTId=PRO_0000045383.
PEPTIDE 78 92 Calcitermin.
/FTId=PRO_0000004774.
DOMAIN 13 48 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 49 84 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 19 32 1; low affinity. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 62 73 2; high affinity. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
REGION 38 53 Hinge domain.
METAL 16 16 Zinc or copper.
METAL 26 26 Zinc or copper.
METAL 86 86 Zinc or copper.
METAL 90 90 Zinc or copper.
CONFLICT 7 7 H -> V (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 12 13 VN -> YS (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 16 16 H -> F (in Ref. 8; AA sequence).
{ECO:0000305}.
HELIX 3 19 {ECO:0000244|PDB:2WCB}.
STRAND 21 24 {ECO:0000244|PDB:2WCB}.
STRAND 27 29 {ECO:0000244|PDB:2WCB}.
HELIX 30 40 {ECO:0000244|PDB:2WCB}.
HELIX 42 47 {ECO:0000244|PDB:2WCB}.
HELIX 51 58 {ECO:0000244|PDB:2WCB}.
STRAND 61 64 {ECO:0000244|PDB:2WCB}.
STRAND 67 70 {ECO:0000244|PDB:2WCB}.
HELIX 71 89 {ECO:0000244|PDB:2WCB}.
SEQUENCE 92 AA; 10575 MW; 52AF75A31BDC222A CRC64;
MTKLEEHLEG IVNIFHQYSV RKGHFDTLSK GELKQLLTKE LANTIKNIKD KAVIDEIFQG
LDANQDEQVD FQEFISLVAI ALKAAHYHTH KE


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