MT2A_RABIT
ID MT2A_RABIT Reviewed; 62 AA.
AC P18055;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Metallothionein-2A;
DE Short=MT-2A;
DE AltName: Full=Metallothionein-IIA;
DE Short=MT-IIA;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=New Zealand white; TISSUE=Kidney, and Liver;
RX PubMed=1779803; DOI=10.1016/0076-6879(91)05125-f;
RA Hunziker P.E.;
RT "Amino acid sequence determination.";
RL Methods Enzymol. 205:421-426(1991).
RN [2]
RP PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RC STRAIN=New Zealand white; TISSUE=Kidney, and Liver;
RX PubMed=7864820; DOI=10.1042/bj3060265;
RA Hunziker P.E., Kaur P., Wan M., Kaenzig A.;
RT "Primary structures of seven metallothioneins from rabbit tissue.";
RL Biochem. J. 306:265-270(1995).
RN [3]
RP STRUCTURE BY NMR, AND PROTEIN SEQUENCE.
RX PubMed=3709538; DOI=10.1111/j.1432-1033.1986.tb09666.x;
RA Wagner G., Neuhaus D., Worgotter E., Vasak M., Kaegi J.H.R., Wuethrich K.;
RT "Sequence-specific 1H-NMR assignments in rabbit-liver metallothionein-2.";
RL Eur. J. Biochem. 157:275-289(1986).
RN [4]
RP STRUCTURE BY NMR.
RX PubMed=3959079; DOI=10.1016/0022-2836(86)90413-4;
RA Wagner G., Neuhaus D., Worgotter E., Vasak M., Kaegi J.H.R., Wuethrich K.;
RT "Nuclear magnetic resonance identification of 'half-turn' and 3(10)-helix
RT secondary structure in rabbit liver metallothionein-2.";
RL J. Mol. Biol. 187:131-135(1986).
RN [5] {ECO:0007744|PDB:1MRB, ECO:0007744|PDB:2MRB}
RP STRUCTURE BY NMR IN COMPLEX WITH CADMIUM IONS, AND DOMAIN.
RX PubMed=3418714; DOI=10.1016/0022-2836(88)90644-4;
RA Arseniev A., Schultze P., Worgotter E., Braun W., Wagner G., Vasak M.,
RA Kaegi J.H.R., Wuethrich K.;
RT "Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in
RT aqueous solution determined by nuclear magnetic resonance.";
RL J. Mol. Biol. 201:637-657(1988).
CC -!- FUNCTION: Metallothioneins have a high content of cysteine residues
CC that bind various heavy metals; these proteins are transcriptionally
CC regulated by both heavy metals and glucocorticoids.
CC -!- SUBUNIT: Monomer.
CC -!- DOMAIN: Class I metallothioneins contain 2 metal-binding domains: four
CC divalent ions are chelated within cluster A of the alpha domain and are
CC coordinated via cysteinyl thiolate bridges to 11 cysteine ligands.
CC Cluster B, the corresponding region within the beta domain, can ligate
CC three divalent ions to 9 cysteines. {ECO:0000269|PubMed:3418714}.
CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 1 family.
CC {ECO:0000305}.
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DR PIR; A37425; A37425.
DR PIR; S54336; S54336.
DR RefSeq; XP_017197722.1; XM_017342233.1.
DR PDB; 1MRB; NMR; -; A=32-62.
DR PDB; 2MRB; NMR; -; A=1-31.
DR PDBsum; 1MRB; -.
DR PDBsum; 2MRB; -.
DR AlphaFoldDB; P18055; -.
DR BMRB; P18055; -.
DR SMR; P18055; -.
DR STRING; 9986.ENSOCUP00000018875; -.
DR iPTMnet; P18055; -.
DR GeneID; 100343299; -.
DR KEGG; ocu:100343299; -.
DR eggNOG; KOG4738; Eukaryota.
DR HOGENOM; CLU_171204_2_0_1; -.
DR InParanoid; P18055; -.
DR OMA; CKQCRCA; -.
DR TreeFam; TF336054; -.
DR EvolutionaryTrace; P18055; -.
DR Proteomes; UP000001811; Unplaced.
DR ExpressionAtlas; P18055; baseline.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0071294; P:cellular response to zinc ion; ISS:UniProtKB.
DR GO; GO:0045926; P:negative regulation of growth; 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; Cadmium; Copper; Direct protein sequencing;
KW Metal-binding; Metal-thiolate cluster; Phosphoprotein; Reference proteome;
KW Zinc.
FT CHAIN 1..62
FT /note="Metallothionein-2A"
FT /id="PRO_0000197216"
FT REGION 1..30
FT /note="Beta"
FT REGION 31..62
FT /note="Alpha"
FT BINDING 5
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:0000269|PubMed:3418714,
FT ECO:0007744|PDB:2MRB"
FT BINDING 7
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:0000269|PubMed:3418714,
FT ECO:0007744|PDB:2MRB"
FT BINDING 7
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:0000269|PubMed:3418714,
FT ECO:0007744|PDB:2MRB"
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:0000269|PubMed:3418714,
FT ECO:0007744|PDB:2MRB"
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:0000269|PubMed:3418714,
FT ECO:0007744|PDB:2MRB"
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:0000269|PubMed:3418714,
FT ECO:0007744|PDB:2MRB"
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:0000269|PubMed:3418714,
FT ECO:0007744|PDB:2MRB"
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:0000269|PubMed:3418714,
FT ECO:0007744|PDB:2MRB"
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:0000269|PubMed:3418714,
FT ECO:0007744|PDB:2MRB"
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:0000269|PubMed:3418714,
FT ECO:0007744|PDB:2MRB"
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:0000269|PubMed:3418714,
FT ECO:0007744|PDB:2MRB"
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:0000269|PubMed:3418714,
FT ECO:0007744|PDB:2MRB"
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:3418714,
FT ECO:0007744|PDB:1MRB"
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:3418714,
FT ECO:0007744|PDB:1MRB"
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:3418714,
FT ECO:0007744|PDB:1MRB"
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:3418714,
FT ECO:0007744|PDB:1MRB"
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:3418714,
FT ECO:0007744|PDB:1MRB"
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:3418714,
FT ECO:0007744|PDB:1MRB"
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:3418714,
FT ECO:0007744|PDB:1MRB"
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:3418714,
FT ECO:0007744|PDB:1MRB"
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:3418714,
FT ECO:0007744|PDB:1MRB"
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:3418714,
FT ECO:0007744|PDB:1MRB"
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:3418714,
FT ECO:0007744|PDB:1MRB"
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:3418714,
FT ECO:0007744|PDB:1MRB"
FT BINDING 58
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:3418714,
FT ECO:0007744|PDB:1MRB"
FT BINDING 60
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:3418714,
FT ECO:0007744|PDB:1MRB"
FT BINDING 61
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:3418714,
FT ECO:0007744|PDB:1MRB"
FT BINDING 61
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:3418714,
FT ECO:0007744|PDB:1MRB"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:7864820"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02795"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:2MRB"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1MRB"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1MRB"
SQ SEQUENCE 62 AA; 6083 MW; C3FEA7B701081B3E CRC64;
MDPNCSCAAA GDSCTCANSC TCKACKCTSC KKSCCSCCPP GCAKCAQGCI CKGASDKCSC
CA
