HEMTM_THETS
ID HEMTM_THETS Reviewed; 120 AA.
AC Q9GYZ9;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Myohemerythrin;
DE Short=MHr;
OS Theromyzon tessulatum (Duck leech).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Hirudinea; Rhynchobdellida; Glossiphoniidae; Theromyzon.
OX NCBI_TaxID=13286;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11311941; DOI=10.1016/s0167-4781(00)00312-2;
RA Coutte L., Slomianny M.-C., Malecha J., Baert J.-L.;
RT "Cloning and expression analysis of a cDNA that encodes a leech
RT hemerythrin.";
RL Biochim. Biophys. Acta 1518:282-286(2001).
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:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the hemerythrin family. {ECO:0000305}.
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DR EMBL; AF279333; AAG01808.1; -; mRNA.
DR AlphaFoldDB; Q9GYZ9; -.
DR SMR; Q9GYZ9; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript level;
KW Cytoplasm; Iron; Metal-binding; Oxygen transport; Transport.
FT CHAIN 1..120
FT /note="Myohemerythrin"
FT /id="PRO_0000191840"
FT BINDING 26
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 56
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 60
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 60
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; 14119 MW; A86D6ECC98ECAEEA CRC64;
MVFEIPEPYQ WDETFEVFYE KLDEEHKGLF KGIKDLSDSP ACSETLEKLV KLIEDHFTDE
EEMMKSKSYE DLDSHKKIHS DFVETLKGVK APVSEENIKM AKEWLVNHIK GTDFKYKGKL
