HEMTM_THEHE
ID HEMTM_THEHE Reviewed; 118 AA.
AC P02247;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Myohemerythrin;
DE Short=MHr;
OS Themiste hennahi (Peanut worm) (Themiste zostericola).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Sipuncula; Sipunculidea;
OC Golfingiida; Themistidae; Themiste.
OX NCBI_TaxID=360549;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=1252432; DOI=10.1021/bi00650a027;
RA Klippenstein G.L., Cote J.L., Ludlam S.E.;
RT "The primary structure of myohemerythrin.";
RL Biochemistry 15:1128-1136(1976).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS).
RX PubMed=1056020; DOI=10.1073/pnas.72.6.2160;
RA Hendrickson W.A., Klippenstein G.L., Ward K.B.;
RT "Tertiary structure of myohemerythrin at low resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 72:2160-2164(1975).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (5.0 ANGSTROMS).
RX PubMed=856811; DOI=10.1016/s0021-9258(17)40465-0;
RA Hendrickson W.A., Ward K.B.;
RT "Pseudosymmetry in the structure of myohemerythrin.";
RL J. Biol. Chem. 252:3012-3018(1977).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH IRON, AND SEQUENCE
RP REVISION TO 34-35.
RX PubMed=3681996; DOI=10.1016/0022-2836(87)90124-0;
RA Sheriff S., Hendrickson W.A., Smith J.L.;
RT "Structure of myohemerythrin in the azidomet state at 1.7/1.3-A
RT resolution.";
RL J. Mol. Biol. 197:273-296(1987).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=9188702; DOI=10.1021/bi9630422;
RA Martins L.J., Hill C.P., Ellis W.R. Jr.;
RT "Structures of wild-type chloromet and L103N hydroxomet Themiste
RT zostericola myohemerythrins at 1.8-A resolution.";
RL Biochemistry 36:7044-7049(1997).
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.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q60AX2}.
CC -!- TISSUE SPECIFICITY: Muscle.
CC -!- SIMILARITY: Belongs to the hemerythrin family. {ECO:0000305}.
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DR PIR; A37369; HRTHM.
DR PDB; 1A7D; X-ray; 1.80 A; A=1-118.
DR PDB; 1A7E; X-ray; 1.80 A; A=1-118.
DR PDB; 2IGF; X-ray; 2.80 A; P=69-87.
DR PDB; 2MHR; X-ray; 1.30 A; A=1-118.
DR PDBsum; 1A7D; -.
DR PDBsum; 1A7E; -.
DR PDBsum; 2IGF; -.
DR PDBsum; 2MHR; -.
DR AlphaFoldDB; P02247; -.
DR SMR; P02247; -.
DR ABCD; P02247; 1 sequenced antibody.
DR EvolutionaryTrace; P02247; -.
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 3D-structure; Direct protein sequencing; Iron; Metal-binding;
KW Muscle protein; Oxygen transport; Transport.
FT CHAIN 1..118
FT /note="Myohemerythrin"
FT /id="PRO_0000191842"
FT BINDING 25
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:3681996,
FT ECO:0007744|PDB:2MHR"
FT BINDING 54
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:3681996,
FT ECO:0007744|PDB:2MHR"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:3681996,
FT ECO:0007744|PDB:2MHR"
FT BINDING 58
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:3681996,
FT ECO:0007744|PDB:2MHR"
FT BINDING 73
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:3681996,
FT ECO:0007744|PDB:2MHR"
FT BINDING 77
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:3681996,
FT ECO:0007744|PDB:2MHR"
FT BINDING 106
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:3681996,
FT ECO:0007744|PDB:2MHR"
FT BINDING 111
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:3681996,
FT ECO:0007744|PDB:2MHR"
FT BINDING 111
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:3681996,
FT ECO:0007744|PDB:2MHR"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:2MHR"
FT HELIX 19..37
FT /evidence="ECO:0007829|PDB:2MHR"
FT HELIX 41..64
FT /evidence="ECO:0007829|PDB:2MHR"
FT HELIX 70..85
FT /evidence="ECO:0007829|PDB:2MHR"
FT HELIX 93..109
FT /evidence="ECO:0007829|PDB:2MHR"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:2MHR"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:2MHR"
SQ SEQUENCE 118 AA; 13778 MW; 3591FEEC56EE90B4 CRC64;
GWEIPEPYVW DESFRVFYEQ LDEEHKKIFK GIFDCIRDNS APNLATLVKV TTNHFTHEEA
MMDAAKYSEV VPHKKMHKDF LEKIGGLSAP VDAKNVDYCK EWLVNHIKGT DFKYKGKL
