HEMT_PHAGO
ID HEMT_PHAGO Reviewed; 114 AA.
AC P02244; Q9U3V2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Hemerythrin;
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 NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF LEU-99.
RX PubMed=10748012; DOI=10.1074/jbc.m001289200;
RA Farmer C.S., Kurtz D.M. Jr., Phillips R.S., Ai J., Sanders-Loehr J.;
RT "A leucine residue 'Gates' solvent but not O2 access to the binding pocket
RT of Phascolopsis gouldii hemerythrin.";
RL J. Biol. Chem. 275:17043-17050(2000).
RN [2]
RP PROTEIN SEQUENCE OF 2-114.
RX PubMed=5722254; DOI=10.1021/bi00851a012;
RA Klippenstein G.L., Holleman J.W., Klotz I.M.;
RT "The primary structure of Golfingia gouldii hemerythrin. Oder of peptides
RT in fragments produced by tryptic digestion of succinylated hemerythrin.
RT Complete amino acid sequence.";
RL Biochemistry 7:3868-3878(1968).
RN [3]
RP SEQUENCE REVISION TO 11-12.
RX PubMed=11945609; DOI=10.1016/0014-5793(71)80005-4;
RA Ferrell R.E., Kitto G.B.;
RT "The amino-terminal sequence of Dendrostomum pyroides hemerythrin.";
RL FEBS Lett. 12:322-324(1971).
RN [4]
RP SEQUENCE REVISION TO 59-60.
RX PubMed=743303; DOI=10.1016/0006-291x(78)91153-1;
RA Gormley P.M., Loehr J.S., Brimhall B., Hermodson M.A.;
RT "New evidence for glutamic acid as an iron ligand in hemerythrin.";
RL Biochem. Biophys. Res. Commun. 85:1360-1366(1978).
RN [5]
RP VARIANTS.
RX PubMed=5059118; DOI=10.1021/bi00753a011;
RA Klippenstein G.L.;
RT "Molecular variants of Golfingia gouldii hemerythrin. The primary structure
RT of the variants arising from five amino acid interchanges.";
RL Biochemistry 11:372-379(1972).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (5.50 ANGSTROMS) OF 2-114.
RX PubMed=5; DOI=10.1016/0006-291x(75)90508-2;
RA Hendrickson W.A., Ward K.B.;
RT "Atomic models for the polypeptide backbones of myohemerythrin and
RT hemerythrin.";
RL Biochem. Biophys. Res. Commun. 66:1349-1356(1975).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH IRON, AND SUBUNIT.
RX PubMed=11372200; DOI=10.1007/s007750100218;
RA Farmer C.S., Kurtz D.M. Jr., Liu Z.J., Wang B.C., Rose J., Ai J.,
RA Sanders-Loehr J.;
RT "The crystal structures of Phascolopsis gouldii wild type and L98Y
RT methemerythrins: structural and functional alterations of the O2 binding
RT pocket.";
RL J. Biol. Inorg. Chem. 6:418-429(2001).
CC -!- FUNCTION: Hemerythrin is a respiratory protein in blood cells of
CC certain marine worms. The oxygen-binding site in each chain contains
CC two iron atoms.
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:11372200}.
CC -!- MISCELLANEOUS: The sequence from one of the four major component
CC variants is shown.
CC -!- SIMILARITY: Belongs to the hemerythrin family. {ECO:0000305}.
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DR EMBL; AF220529; AAF25482.1; -; mRNA.
DR PIR; A90553; HRGG.
DR PDB; 1HRB; X-ray; 5.50 A; A/B=2-114.
DR PDB; 1I4Y; X-ray; 1.80 A; A/B/C/D/E/F/G/H=1-114.
DR PDB; 1I4Z; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1-114.
DR PDBsum; 1HRB; -.
DR PDBsum; 1I4Y; -.
DR PDBsum; 1I4Z; -.
DR AlphaFoldDB; P02244; -.
DR SMR; P02244; -.
DR EvolutionaryTrace; P02244; -.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.50; -; 1.
DR InterPro; IPR002063; Haemerythrin.
DR InterPro; IPR016131; Haemerythrin_Fe_BS.
DR InterPro; IPR035938; Hemerythrin-like_sf.
DR InterPro; IPR012827; Hemerythrin_metal-bd.
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 Oxygen transport; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:5722254"
FT CHAIN 2..114
FT /note="Hemerythrin"
FT /id="PRO_0000191837"
FT BINDING 26
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11372200,
FT ECO:0007744|PDB:1I4Y, ECO:0007744|PDB:1I4Z"
FT BINDING 55
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11372200,
FT ECO:0007744|PDB:1I4Y, ECO:0007744|PDB:1I4Z"
FT BINDING 59
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11372200,
FT ECO:0007744|PDB:1I4Y, ECO:0007744|PDB:1I4Z"
FT BINDING 59
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11372200,
FT ECO:0007744|PDB:1I4Y, ECO:0007744|PDB:1I4Z"
FT BINDING 74
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11372200,
FT ECO:0007744|PDB:1I4Y, ECO:0007744|PDB:1I4Z"
FT BINDING 78
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11372200,
FT ECO:0007744|PDB:1I4Y, ECO:0007744|PDB:1I4Z"
FT BINDING 102
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11372200,
FT ECO:0007744|PDB:1I4Y, ECO:0007744|PDB:1I4Z"
FT BINDING 107
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11372200,
FT ECO:0007744|PDB:1I4Y, ECO:0007744|PDB:1I4Z"
FT BINDING 107
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11372200,
FT ECO:0007744|PDB:1I4Y, ECO:0007744|PDB:1I4Z"
FT VARIANT 64
FT /note="Q -> E (in minor component)"
FT VARIANT 79
FT /note="E -> D (in minor component)"
FT VARIANT 80
FT /note="T -> G"
FT VARIANT 83
FT /note="H -> N (in minor component)"
FT VARIANT 97
FT /note="S -> A (in minor and major variants)"
FT MUTAGEN 99
FT /note="L->X: Increased auto-oxidation rate (when X
FT different from Tyr)."
FT /evidence="ECO:0000269|PubMed:10748012"
FT MUTAGEN 99
FT /note="L->Y: Decreased auto-oxidation rate."
FT /evidence="ECO:0000269|PubMed:10748012"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:1I4Y"
FT HELIX 20..38
FT /evidence="ECO:0007829|PDB:1I4Y"
FT HELIX 42..65
FT /evidence="ECO:0007829|PDB:1I4Y"
FT HELIX 71..86
FT /evidence="ECO:0007829|PDB:1I4Y"
FT HELIX 92..105
FT /evidence="ECO:0007829|PDB:1I4Y"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:1I4Y"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1I4Y"
SQ SEQUENCE 114 AA; 13605 MW; BF730C540D0769FC CRC64;
MGFPIPDPYV WDPSFRTFYS IIDDEHKTLF NGIFHLAIDD NADNLGELRR CTGKHFLNEQ
VLMQASQYQF YDEHKKEHET FIHALDNWKG DVKWAKSWLV NHIKTIDFKY KGKI
