HEMT2_PHAGO
ID HEMT2_PHAGO Reviewed; 31 AA.
AC P27687;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Myohemerythrin-2;
DE Short=MHr-2;
DE Flags: Fragment;
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; PS0350; PS0350.
DR AlphaFoldDB; P27687; -.
DR SMR; P27687; -.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR InterPro; IPR002063; Haemerythrin.
DR InterPro; IPR035938; Hemerythrin-like_sf.
DR PRINTS; PR00186; HEMERYTHRIN.
DR SUPFAM; SSF47188; SSF47188; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Iron; Metal-binding; Muscle protein;
KW Oxygen transport; Transport.
FT CHAIN 1..>31
FT /note="Myohemerythrin-2"
FT /id="PRO_0000191836"
FT BINDING 25
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02244"
FT NON_TER 31
SQ SEQUENCE 31 AA; 3735 MW; DA740CEE0FD9FDA1 CRC64;
GFDIPEPYVW DESFRVFYDL LDDEHKGLFQ G