MTA_STRPU
ID MTA_STRPU Reviewed; 64 AA.
AC P04734;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Metallothionein-A;
DE Short=MTA;
GN Name=MTA;
OS Strongylocentrotus purpuratus (Purple sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC Strongylocentrotus.
OX NCBI_TaxID=7668;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2586524; DOI=10.1128/mcb.9.12.5445-5455.1989;
RA Harlow P., Watkins E., Thornton R.D., Nemer M.;
RT "Structure of an ectodermally expressed sea urchin metallothionein gene and
RT characterization of its metal-responsive region.";
RL Mol. Cell. Biol. 9:5445-5455(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3860837; DOI=10.1073/pnas.82.15.4992;
RA Nemer M., Wilkinson D.G., Travaglini E.C., Sternberg E.J., Butt T.R.;
RT "Sea urchin metallothionein sequence: key to an evolutionary diversity.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:4992-4994(1985).
RN [3]
RP STRUCTURE BY NMR.
RX PubMed=10438629; DOI=10.1006/jmbi.1999.2967;
RA Riek R., Precheur B., Wang Y., Mackay E.A., Wider G., Guntert P., Liu A.,
RA Kaegi J.H.R., Wuethrich K.;
RT "NMR structure of the sea urchin (Strongylocentrotus purpuratus)
RT metallothionein MTA.";
RL J. Mol. Biol. 291:417-428(1999).
CC -!- FUNCTION: Metallothioneins have a high content of cysteine residues
CC that bind various heavy metals.
CC -!- INDUCTION: By heavy metals.
CC -!- SIMILARITY: Belongs to the metallothionein superfamily. Type 4 family.
CC {ECO:0000305}.
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DR EMBL; M30606; AAA30067.1; -; Genomic_DNA.
DR EMBL; K02464; AAA30061.1; -; mRNA.
DR PIR; A25775; A25775.
DR PIR; A33825; A33825.
DR RefSeq; NP_999742.1; NM_214577.1.
DR PDB; 1QJK; NMR; -; A=2-37.
DR PDB; 1QJL; NMR; -; A=37-64.
DR PDBsum; 1QJK; -.
DR PDBsum; 1QJL; -.
DR AlphaFoldDB; P04734; -.
DR SMR; P04734; -.
DR EnsemblMetazoa; XM_030990197; XP_030846057; LOC115926005.
DR EnsemblMetazoa; XM_030990198; XP_030846058; LOC115926005.
DR GeneID; 373380; -.
DR KEGG; spu:373380; -.
DR CTD; 373380; -.
DR HOGENOM; CLU_2834403_0_0_1; -.
DR EvolutionaryTrace; P04734; -.
DR Proteomes; UP000007110; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR017980; Metalthion_4_echinoid/annelid.
DR InterPro; IPR001396; Metalthion_4_echinoidea.
DR InterPro; IPR017854; Metalthion_dom_sf.
DR Pfam; PF05522; Metallothio_6; 1.
DR PRINTS; PR00873; MTECHINOIDEA.
DR SUPFAM; SSF57868; SSF57868; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Metal-thiolate cluster; Reference proteome.
FT CHAIN 1..64
FT /note="Metallothionein-A"
FT /id="PRO_0000197347"
FT CONFLICT 10
FT /note="K -> T (in Ref. 2; AAA30061)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="K -> V (in Ref. 2; AAA30061)"
FT /evidence="ECO:0000305"
FT HELIX 7..11
FT /evidence="ECO:0007829|PDB:1QJK"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:1QJK"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:1QJK"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:1QJK"
SQ SEQUENCE 64 AA; 6445 MW; 66F0AA7A4991E3E6 CRC64;
MPDVKCVCCK EGKECACFGQ DCCKTGECCK DGTCCGICTN AACKCANGCK CGSGCSCTEG
NCAC