HEMT1_PHAGO
ID HEMT1_PHAGO Reviewed; 119 AA.
AC P27686;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Myohemerythrin-1;
DE Short=MHr-1;
OS Phascolopsis gouldii (Peanut worm) (Golfingia gouldii).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Sipuncula; Sipunculidea;
OC Golfingiida; Sipunculidae; Phascolopsis.
OX NCBI_TaxID=6442;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Muscle;
RX PubMed=1322702; DOI=10.1016/0167-4838(92)90315-5;
RA Long R.C., Zhang J.-H., Kurtz D.M. Jr., Negri A., Tedeschi G., Bonomi F.;
RT "Myohemerythrin from the sipunculid, Phascolopsis gouldii: purification,
RT properties and amino acid sequence.";
RL Biochim. Biophys. Acta 1122:136-142(1992).
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. {ECO:0000269|PubMed:1322702}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1322702}.
CC -!- TISSUE SPECIFICITY: Muscle. {ECO:0000269|PubMed:1322702}.
CC -!- SIMILARITY: Belongs to the hemerythrin family. {ECO:0000305}.
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DR PIR; S23922; S23922.
DR AlphaFoldDB; P27686; -.
DR SMR; P27686; -.
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..119
FT /note="Myohemerythrin-1"
FT /id="PRO_0000191835"
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 55
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"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 59
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 74
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 78
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 107
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 112
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT BINDING 112
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02244"
SQ SEQUENCE 119 AA; 13710 MW; BB25A9A2617BAE39 CRC64;
PFDIPEPYVW DESFRVFYDN LDDEHKGLFK GVFNCAADMS SAGNLKHLID VTTTHFRNEE
AMMDAAKYEN VVPHKQMHKD FLAKLGGLKA PLDQGTIDYA KDWLVQHIKT TDFKYKGKL
