HEMTM_HEDDI
ID HEMTM_HEDDI Reviewed; 120 AA.
AC P22761;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Myohemerythrin;
DE Short=MHr;
OS Hediste diversicolor (Sandworm) (Nereis diversicolor).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Errantia; Phyllodocida; Nereididae; Hediste;
OC Hediste diversicolor species group.
OX NCBI_TaxID=126592;
RN [1]
RP PROTEIN SEQUENCE, AND TISSUE SPECIFICITY.
RC TISSUE=Muscle;
RX PubMed=2065779; DOI=10.1016/0014-5793(91)80716-g;
RA Takagi T., Cox J.A.;
RT "Primary structure of myohemerythrin from the annelid Nereis
RT diversicolor.";
RL FEBS Lett. 285:25-27(1991).
CC -!- FUNCTION: Myohemerythrin is an oxygen-binding protein found in the
CC retractor muscles of certain worms. The oxygen-binding site contains
CC two iron atoms (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Muscle. {ECO:0000269|PubMed:2065779}.
CC -!- SIMILARITY: Belongs to the hemerythrin family. {ECO:0000305}.
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DR PIR; S16190; S16190.
DR AlphaFoldDB; P22761; -.
DR SMR; P22761; -.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProt.
DR CDD; cd12107; Hemerythrin; 1.
DR Gene3D; 1.20.120.50; -; 1.
DR InterPro; IPR002063; Haemerythrin.
DR InterPro; IPR016131; Haemerythrin_Fe_BS.
DR InterPro; IPR012312; Hemerythrin-like.
DR InterPro; IPR035938; Hemerythrin-like_sf.
DR InterPro; IPR012827; Hemerythrin_metal-bd.
DR Pfam; PF01814; Hemerythrin; 1.
DR PIRSF; PIRSF002033; Hemerythrin; 1.
DR PRINTS; PR00186; HEMERYTHRIN.
DR SUPFAM; SSF47188; SSF47188; 1.
DR TIGRFAMs; TIGR02481; hemeryth_dom; 1.
DR TIGRFAMs; TIGR00058; Hemerythrin; 1.
DR PROSITE; PS00550; HEMERYTHRINS; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Iron; Metal-binding; Muscle protein;
KW Oxygen transport; Transport.
FT CHAIN 1..120
FT /note="Myohemerythrin"
FT /id="PRO_0000191833"
FT BINDING 25
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 54
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 75
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 79
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 108
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 113
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 113
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
SQ SEQUENCE 120 AA; 13641 MW; A793589D582E8B97 CRC64;
GFEVPEPFKW DESFQVFYDK LDEEHKQIFN AIFALGGGNN ADNLKKMIDV TANHFADEEA
MMLASAAYKS EHPGHKKKHE DFLAVIRGLS APVPNDKLLY AKDWLVNHIK GTDFTYKGKL