MT2_CANLF
ID MT2_CANLF Reviewed; 61 AA.
AC Q9XST5;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Metallothionein-2;
DE Short=MT-2;
DE AltName: Full=Metallothionein-II;
DE Short=MT-II;
GN Name=MT2A; Synonyms=MT2; ORFNames=B28;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=4062298; DOI=10.1016/0003-9861(85)90778-7;
RA Lerch K., Johnson G.F., Grushoff P.S., Sternlieb I.;
RT "Canine hepatic lysosomal copper protein: identification as
RT metallothionein.";
RL Arch. Biochem. Biophys. 243:108-114(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Beagle; TISSUE=Kidney;
RA Kobayashi K., Morita T., Shimada A.;
RT "Molecular cloning and expression of canine metallothionein-II.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thyroid;
RX PubMed=10964405; DOI=10.1006/abio.2000.4674;
RA Pichon B., Mercan D., Pouillon V., Christophe-Hobertus C., Christophe D.;
RT "A method for the large-scale cloning of nuclear proteins and nuclear
RT targeting sequences on a functional basis.";
RL Anal. Biochem. 284:231-239(2000).
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: Interacts with EOLA1. {ECO:0000250|UniProtKB:P02795}.
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.
CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 1 family.
CC {ECO:0000305}.
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DR EMBL; AB028042; BAA87327.1; -; mRNA.
DR EMBL; AJ388530; CAB46832.1; -; mRNA.
DR RefSeq; NP_001003149.1; NM_001003149.1.
DR AlphaFoldDB; Q9XST5; -.
DR SMR; Q9XST5; -.
DR STRING; 9615.ENSCAFP00000013399; -.
DR PaxDb; Q9XST5; -.
DR Ensembl; ENSCAFT00000014487; ENSCAFP00000013399; ENSCAFG00000023759.
DR Ensembl; ENSCAFT00030007812; ENSCAFP00030006852; ENSCAFG00030004211.
DR Ensembl; ENSCAFT00040025591; ENSCAFP00040022249; ENSCAFG00040013818.
DR Ensembl; ENSCAFT00845006916; ENSCAFP00845005508; ENSCAFG00845003852.
DR GeneID; 403768; -.
DR KEGG; cfa:403768; -.
DR CTD; 4502; -.
DR VEuPathDB; HostDB:ENSCAFG00845003852; -.
DR eggNOG; KOG4738; Eukaryota.
DR GeneTree; ENSGT00950000182967; -.
DR HOGENOM; CLU_171204_2_0_1; -.
DR InParanoid; Q9XST5; -.
DR OMA; CKECKCA; -.
DR TreeFam; TF336054; -.
DR Reactome; R-CFA-5661231; Metallothioneins bind metals.
DR Proteomes; UP000002254; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0071276; P:cellular response to cadmium ion; IBA:GO_Central.
DR GO; GO:0071280; P:cellular response to copper ion; IBA:GO_Central.
DR GO; GO:0071294; P:cellular response to zinc ion; ISS:UniProtKB.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IBA:GO_Central.
DR GO; GO:0010273; P:detoxification of copper ion; IBA:GO_Central.
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 Acetylation; Direct protein sequencing; Metal-binding;
KW Metal-thiolate cluster; Phosphoprotein; Reference proteome.
FT CHAIN 1..61
FT /note="Metallothionein-2"
FT /id="PRO_0000197199"
FT REGION 1..29
FT /note="Beta"
FT REGION 30..61
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
FT BINDING 13
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 15
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 15
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 19
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 21
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 24
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 24
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 26
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 29
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 33
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: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:0000250|UniProtKB:P02795"
FT BINDING 34
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:0000250|UniProtKB:P02795"
FT BINDING 36
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
FT BINDING 37
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:0000250|UniProtKB:P02795"
FT BINDING 41
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:0000250|UniProtKB:P02795"
FT BINDING 44
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:0000250|UniProtKB:P02795"
FT BINDING 44
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:0000250|UniProtKB:P02795"
FT BINDING 48
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:0000250|UniProtKB:P02795"
FT BINDING 50
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:0000250|UniProtKB:P02795"
FT BINDING 50
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:0000250|UniProtKB:P02795"
FT BINDING 57
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:0000250|UniProtKB:P02795"
FT BINDING 59
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:0000250|UniProtKB:P02795"
FT BINDING 60
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:0000250|UniProtKB:P02795"
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:0000250|UniProtKB:P02795"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P68301"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02795"
SQ SEQUENCE 61 AA; 6012 MW; 7B0A7C54E272C448 CRC64;
MDPNCSCAAG GSCTCAGSCK CKECRCTSCK KSCCSCCPVG CAKCAQGCIC KGASDKCSCC
A
