ID MT_ESOLU STANDARD; PRT; 60 AA. AC P25127; DT 01-MAY-1992 (REL. 22, CREATED) DT 01-MAY-1992 (REL. 22, LAST SEQUENCE UPDATE) DT 01-FEB-1994 (REL. 28, LAST ANNOTATION UPDATE) DE METALLOTHIONEIN (MT). OS ESOX LUCIUS (NORTHERN PIKE). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA; OC OSTEICHTHYES; ACTINOPTERYGII; SALMONIFORMES. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LIVER; RM 91316146 RA KILLE P., STEPHENS P.E., KAY J.; RL BIOCHIM. BIOPHYS. ACTA 1089:407-410(1991). RN [2] RP SEQUENCE FROM N.A. RM 94032489 RA KILLE P., KAY J., SWEENEY G.E.; RL BIOCHIM. BIOPHYS. ACTA 1216:55-64(1993). CC -!- FUNCTION: METALLOTHIONEINS HAVE A HIGH CONTENT OF CYSTEINE CC RESIDUES THAT BIND VARIOUS HEAVY METALS; THESE PROTEINS ARE CC TRANSCRIPTIONALLY REGULATED BY BOTH HEAVY METALS AND CC GLUCOCORTICOIDS. CC -!- CLASS I METALLOTHIONEINS CONTAIN 2 METAL-BINDING DOMAINS: FOUR CC DIVALENT IONS ARE CHELATED WITHIN CLUSTER A OF THE ALPHA DOMAIN CC AND ARE COORDINATED VIA CYSTEINYL THIOLATE BRIDGES TO 11 CYSTEINE CC LIGANDS. CLUSTER B, THE CORRESPONDING REGION WITHIN THE BETA CC DOMAIN, CAN LIGATE THREE DIVALENT IONS TO 9 CYSTEINES. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X59392; ELMETA. DR EMBL; X70042; ELMETL. DR PIR; S17175; S17175. DR PIR; S15503; S15503. DR PROSITE; PS00203; METALLOTHIONEIN_CL1. KW METAL-BINDING; METAL-THIOLATE CLUSTER; CHELATION. FT DOMAIN 1 28 BETA. FT DOMAIN 29 60 ALPHA. FT METAL 4 4 CLUSTER B. FT METAL 6 6 CLUSTER B. FT METAL 12 12 CLUSTER B. FT METAL 14 14 CLUSTER B. FT METAL 18 18 CLUSTER B. FT METAL 20 20 CLUSTER B. FT METAL 23 23 CLUSTER B. FT METAL 25 25 CLUSTER B. FT METAL 28 28 CLUSTER B. FT METAL 32 32 CLUSTER A. FT METAL 33 33 CLUSTER A. FT METAL 35 35 CLUSTER A. FT METAL 36 36 CLUSTER A. FT METAL 40 40 CLUSTER A. FT METAL 43 43 CLUSTER A. FT METAL 47 47 CLUSTER A. FT METAL 49 49 CLUSTER A. FT METAL 54 54 CLUSTER A. FT METAL 58 58 CLUSTER A. FT METAL 59 59 CLUSTER A. SQ SEQUENCE 60 AA; 5979 MW; 16957 CN; MDPCECSKTG SCNCGGSCKC SNCACTSCKK SCCSCCPSGC SKCASGCICK GKTCDTSCCQ //