MT3_HUMAN
ID MT3_HUMAN Reviewed; 68 AA.
AC P25713; Q2V574;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Metallothionein-3;
DE Short=MT-3;
DE AltName: Full=GIFB;
DE Short=GIF;
DE AltName: Full=Growth inhibitory factor;
DE AltName: Full=Metallothionein-III;
DE Short=MT-III;
GN Name=MT3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RC TISSUE=Brain;
RX PubMed=1873033; DOI=10.1016/0896-6273(91)90272-2;
RA Uchida Y., Takio K., Titani K., Ihara Y., Tomonaga M.;
RT "The growth inhibitory factor that is deficient in the Alzheimer's disease
RT brain is a 68 amino acid metallothionein-like protein.";
RL Neuron 7:337-347(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=1631128; DOI=10.1073/pnas.89.14.6333;
RA Palmiter R.D., Findley S.D., Whitmore T.E., Durnam D.M.;
RT "MT-III, a brain-specific member of the metallothionein gene family.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:6333-6337(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1464312; DOI=10.1002/j.1460-2075.1992.tb05590.x;
RA Tsuji S., Kobayashi H., Uchida Y., Ihara Y., Miyatake T.;
RT "Molecular cloning of human growth inhibitory factor cDNA and its down-
RT regulation in Alzheimer's disease.";
RL EMBO J. 11:4843-4850(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8039715; DOI=10.1016/0378-1119(94)90391-3;
RA Naruse S., Igarashi S., Furuya T., Kobayashi H., Miyatake T., Tsuji S.;
RT "Structures of the human and mouse growth inhibitory factor-encoding
RT genes.";
RL Gene 144:283-287(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7677777; DOI=10.1006/bbrc.1995.2334;
RA Amoureux M.C., Wurch T., Pauwels P.J.;
RT "Modulation of metallothionein-III mRNA content and growth rate of rat C6-
RT glial cells by transfection with human 5-HT1D receptor genes.";
RL Biochem. Biophys. Res. Commun. 214:639-645(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9] {ECO:0007744|PDB:2FJ4, ECO:0007744|PDB:2FJ5}
RP STRUCTURE BY NMR OF 32-68.
RA Wu H., Zhang Q.;
RT "Solution structure of a-domain of HUMAN Metallothionein-3 (MT-3).";
RL Submitted (DEC-2005) to the PDB data bank.
RN [10] {ECO:0007744|PDB:2F5H}
RP STRUCTURE BY NMR OF 32-68 IN COMPLEX WITH CADMIUM IONS.
RX PubMed=16413543; DOI=10.1016/j.febslet.2005.12.099;
RA Wang H., Zhang Q., Cai B., Li H., Sze K.H., Huang Z.X., Wu H.M., Sun H.;
RT "Solution structure and dynamics of human metallothionein-3 (MT-3).";
RL FEBS Lett. 580:795-800(2006).
CC -!- FUNCTION: Binds heavy metals. Contains three zinc and three copper
CC atoms per polypeptide chain and only a negligible amount of cadmium.
CC Inhibits survival and neurite formation of cortical neurons in vitro.
CC -!- INTERACTION:
CC P25713; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-8084264, EBI-750109;
CC P25713; P02766: TTR; NbExp=3; IntAct=EBI-8084264, EBI-711909;
CC -!- TISSUE SPECIFICITY: Abundant in a subset of astrocytes in the normal
CC human brain, but greatly reduced in the Alzheimer disease (AD) brain.
CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 1 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/mt3/";
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DR EMBL; M93311; AAA36214.1; -; Genomic_DNA.
DR EMBL; D13365; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; S72043; AAB31396.1; -; Genomic_DNA.
DR EMBL; X89604; CAA61763.1; -; mRNA.
DR EMBL; BT007030; AAP35677.1; -; mRNA.
DR EMBL; DQ297144; ABB84467.1; -; Genomic_DNA.
DR EMBL; BC013081; AAH13081.1; -; mRNA.
DR CCDS; CCDS10762.1; -.
DR PIR; B46034; B46034.
DR RefSeq; NP_005945.1; NM_005954.2.
DR PDB; 2F5H; NMR; -; A=32-68.
DR PDB; 2FJ4; NMR; -; A=32-68.
DR PDB; 2FJ5; NMR; -; A=32-68.
DR PDBsum; 2F5H; -.
DR PDBsum; 2FJ4; -.
DR PDBsum; 2FJ5; -.
DR AlphaFoldDB; P25713; -.
DR SMR; P25713; -.
DR BioGRID; 110610; 2.
DR IntAct; P25713; 2.
DR MINT; P25713; -.
DR STRING; 9606.ENSP00000200691; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB12965; Silver.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR iPTMnet; P25713; -.
DR PhosphoSitePlus; P25713; -.
DR BioMuta; MT3; -.
DR DMDM; 127404; -.
DR MassIVE; P25713; -.
DR PaxDb; P25713; -.
DR PeptideAtlas; P25713; -.
DR PRIDE; P25713; -.
DR ProteomicsDB; 54284; -.
DR Antibodypedia; 1293; 164 antibodies from 19 providers.
DR DNASU; 4504; -.
DR Ensembl; ENST00000200691.5; ENSP00000200691.5; ENSG00000087250.9.
DR GeneID; 4504; -.
DR KEGG; hsa:4504; -.
DR MANE-Select; ENST00000200691.5; ENSP00000200691.5; NM_005954.4; NP_005945.1.
DR UCSC; uc002ejf.4; human.
DR CTD; 4504; -.
DR DisGeNET; 4504; -.
DR GeneCards; MT3; -.
DR HGNC; HGNC:7408; MT3.
DR HPA; ENSG00000087250; Group enriched (brain, choroid plexus).
DR MIM; 139255; gene.
DR neXtProt; NX_P25713; -.
DR OpenTargets; ENSG00000087250; -.
DR PharmGKB; PA31216; -.
DR VEuPathDB; HostDB:ENSG00000087250; -.
DR eggNOG; KOG4738; Eukaryota.
DR GeneTree; ENSGT00950000182967; -.
DR HOGENOM; CLU_171204_2_0_1; -.
DR InParanoid; P25713; -.
DR OMA; ECAKSEY; -.
DR PhylomeDB; P25713; -.
DR PathwayCommons; P25713; -.
DR Reactome; R-HSA-5661231; Metallothioneins bind metals.
DR SignaLink; P25713; -.
DR BioGRID-ORCS; 4504; 11 hits in 1065 CRISPR screens.
DR ChiTaRS; MT3; human.
DR EvolutionaryTrace; P25713; -.
DR GeneWiki; MT3; -.
DR GenomeRNAi; 4504; -.
DR Pharos; P25713; Tbio.
DR PRO; PR:P25713; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P25713; protein.
DR Bgee; ENSG00000087250; Expressed in nucleus accumbens and 108 other tissues.
DR ExpressionAtlas; P25713; baseline and differential.
DR GO; GO:0097450; C:astrocyte end-foot; IEA:Ensembl.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0016234; C:inclusion body; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:Ensembl.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0005840; C:ribosome; IEA:Ensembl.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0016209; F:antioxidant activity; NAS:UniProtKB.
DR GO; GO:0046870; F:cadmium ion binding; IDA:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR GO; GO:0030295; F:protein kinase activator activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0032148; P:activation of protein kinase B activity; IDA:UniProtKB.
DR GO; GO:0014002; P:astrocyte development; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0055073; P:cadmium ion homeostasis; IDA:UniProtKB.
DR GO; GO:0044242; P:cellular lipid catabolic process; ISS:UniProtKB.
DR GO; GO:0006875; P:cellular metal ion homeostasis; TAS:UniProtKB.
DR GO; GO:0071276; P:cellular response to cadmium ion; IDA:UniProtKB.
DR GO; GO:0071280; P:cellular response to copper ion; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:UniProtKB.
DR GO; GO:0071732; P:cellular response to nitric oxide; IDA:UniProtKB.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEP:UniProtKB.
DR GO; GO:0071294; P:cellular response to zinc ion; IBA:GO_Central.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; ISS:UniProtKB.
DR GO; GO:0006707; P:cholesterol catabolic process; ISS:UniProtKB.
DR GO; GO:0010273; P:detoxification of copper ion; IBA:GO_Central.
DR GO; GO:0006112; P:energy reserve metabolic process; ISS:UniProtKB.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0016570; P:histone modification; IMP:UniProtKB.
DR GO; GO:0033210; P:leptin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0030517; P:negative regulation of axon extension; IDA:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:2000296; P:negative regulation of hydrogen peroxide catabolic process; IEA:Ensembl.
DR GO; GO:0060547; P:negative regulation of necrotic cell death; IDA:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; TAS:GO_Central.
DR GO; GO:0051354; P:negative regulation of oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISS:UniProtKB.
DR GO; GO:0010942; P:positive regulation of cell death; IDA:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0097214; P:positive regulation of lysosomal membrane permeability; ISS:UniProtKB.
DR GO; GO:0010940; P:positive regulation of necrotic cell death; IDA:UniProtKB.
DR GO; GO:2000376; P:positive regulation of oxygen metabolic process; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0036091; P:positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0043491; P:protein kinase B signaling; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR GO; GO:0060049; P:regulation of protein glycosylation; ISS:UniProtKB.
DR GO; GO:0032095; P:regulation of response to food; ISS:UniProtKB.
DR GO; GO:0019430; P:removal of superoxide radicals; IDA:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB.
DR GO; GO:0055069; P:zinc ion homeostasis; IDA:UniProtKB.
DR GO; GO:0006829; P:zinc ion transport; ISS:UniProtKB.
DR Gene3D; 4.10.10.10; -; 1.
DR InterPro; IPR003019; Metalthion.
DR InterPro; IPR017854; Metalthion_dom_sf.
DR InterPro; IPR023587; Metalthion_dom_sf_vert.
DR InterPro; IPR000006; Metalthion_vert.
DR InterPro; IPR018064; Metalthion_vert_metal_BS.
DR PANTHER; PTHR23299; PTHR23299; 1.
DR Pfam; PF00131; Metallothio; 1.
DR PRINTS; PR00860; MTVERTEBRATE.
DR SUPFAM; SSF57868; SSF57868; 1.
DR PROSITE; PS00203; METALLOTHIONEIN_VRT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Copper; Direct protein sequencing;
KW Metal-binding; Metal-thiolate cluster; Phosphoprotein; Reference proteome;
KW Zinc.
FT CHAIN 1..68
FT /note="Metallothionein-3"
FT /id="PRO_0000197250"
FT REGION 1..30
FT /note="Beta"
FT REGION 31..68
FT /note="Alpha"
FT BINDING 6
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000250|UniProtKB:P02795"
FT BINDING 8
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000250|UniProtKB:P02795"
FT BINDING 8
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000250|UniProtKB:P02795"
FT BINDING 14
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000250|UniProtKB:P02795"
FT BINDING 16
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000250|UniProtKB:P02795"
FT BINDING 16
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000250|UniProtKB:P02795"
FT BINDING 20
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000250|UniProtKB:P02795"
FT BINDING 22
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000250|UniProtKB:P02795"
FT BINDING 25
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000250|UniProtKB:P02795"
FT BINDING 25
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000250|UniProtKB:P02795"
FT BINDING 27
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000250|UniProtKB:P02795"
FT BINDING 30
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="3"
FT /ligand_note="in cluster B"
FT /evidence="ECO:0000250|UniProtKB:P02795"
FT BINDING 34
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="4"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:16413543,
FT ECO:0007744|PDB:2F5H"
FT BINDING 35
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="4"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:16413543,
FT ECO:0007744|PDB:2F5H"
FT BINDING 35
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="5"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:16413543,
FT ECO:0007744|PDB:2F5H"
FT BINDING 37
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="5"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:16413543,
FT ECO:0007744|PDB:2F5H"
FT BINDING 38
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="5"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:16413543,
FT ECO:0007744|PDB:2F5H"
FT BINDING 38
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="6"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:16413543,
FT ECO:0007744|PDB:2F5H"
FT BINDING 42
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="6"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:16413543,
FT ECO:0007744|PDB:2F5H"
FT BINDING 45
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="4"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:16413543,
FT ECO:0007744|PDB:2F5H"
FT BINDING 45
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="6"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:16413543,
FT ECO:0007744|PDB:2F5H"
FT BINDING 49
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="4"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:16413543,
FT ECO:0007744|PDB:2F5H"
FT BINDING 51
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="5"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:16413543,
FT ECO:0007744|PDB:2F5H"
FT BINDING 51
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="7"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:16413543,
FT ECO:0007744|PDB:2F5H"
FT BINDING 64
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="7"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:16413543,
FT ECO:0007744|PDB:2F5H"
FT BINDING 66
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="7"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:16413543,
FT ECO:0007744|PDB:2F5H"
FT BINDING 67
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="6"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:16413543,
FT ECO:0007744|PDB:2F5H"
FT BINDING 67
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="7"
FT /ligand_note="in cluster A"
FT /evidence="ECO:0000269|PubMed:16413543,
FT ECO:0007744|PDB:2F5H"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:1873033"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28184"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:2F5H"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:2F5H"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:2FJ4"
FT TURN 55..59
FT /evidence="ECO:0007829|PDB:2FJ4"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2FJ4"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:2FJ4"
SQ SEQUENCE 68 AA; 6927 MW; 59801ECF5BC8A406 CRC64;
MDPETCPCPS GGSCTCADSC KCEGCKCTSC KKSCCSCCPA ECEKCAKDCV CKGGEAAEAE
AEKCSCCQ
