GLB3_CHITH
ID GLB3_CHITH Reviewed; 151 AA.
AC P02229;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Globin CTT-III;
DE AltName: Full=Erythrocruorin III;
DE Flags: Precursor;
GN Name=A;
GN and
GN Name=A';
GN and
GN Name=B;
GN and
GN Name=B';
OS Chironomus thummi thummi (Midge).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Chironominae; Chironomus.
OX NCBI_TaxID=7155;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3678833; DOI=10.1016/0378-1119(87)90156-9;
RA Antoine M., Erbil C., Muench E., Schnell S., Niessing J.;
RT "Genomic organization and primary structure of five homologous pairs of
RT intron-less genes encoding secretory globins from the insect Chironomus
RT thummi thummi.";
RL Gene 56:41-51(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hankeln T., Amid C., Weich B., Schmidt E.R.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 16-151.
RX PubMed=761849; DOI=10.1515/bchm2.1979.360.1.89;
RA Buse G., Steffens G.J., Braunitzer G., Steer W.;
RT "Hemoglobins, XXV. Hemoglobin (erythrocruorin) CTT III from Chironomus
RT thummi thummi (Diptera). Primary structure and relationship to other heme
RT proteins.";
RL Hoppe-Seyler's Z. Physiol. Chem. 360:89-97(1979).
RN [4]
RP HEME-BINDING.
RX PubMed=5804161; DOI=10.1016/0022-2836(69)90246-0;
RA Huber R., Epp O., Formanek H.;
RT "The environment of the haem group in erythrocruorin (Chironomus thummi).";
RL J. Mol. Biol. 42:591-594(1969).
RN [5]
RP HEME-BINDING.
RX PubMed=5420706;
RA Glossmann H., Horst J., Plagens U., Braunitzer G.;
RT "Hemoglobins, XVIII. Isoelectric focussing of hemoglobins (erythrocruorins)
RT from insects (Chironomus thummi, thummi, Diptera).";
RL Hoppe-Seyler's Z. Physiol. Chem. 351:342-348(1970).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
RX PubMed=642012; DOI=10.1016/0022-2836(78)90071-2;
RA Weber E., Steigemann W., Jones T.A., Huber R.;
RT "The structure of oxy-erythrocruorin at 1.4-A resolution.";
RL J. Mol. Biol. 120:327-336(1978).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=5102553; DOI=10.1111/j.1432-1033.1971.tb01285.x;
RA Huber R., Epp O., Steigemann W., Formanek H.;
RT "The atomic structure of erythrocruorin in the light of the chemical
RT sequence and its comparison with myoglobin.";
RL Eur. J. Biochem. 19:42-50(1971).
CC -!- SUBUNIT: Monomer.
CC -!- MISCELLANEOUS: There are at least 12 different components in Midge
CC globin.
CC -!- MISCELLANEOUS: The sequence of genes B and B' are shown.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; M17600; AAA28249.1; -; Genomic_DNA.
DR EMBL; M17601; AAA28250.1; -; Genomic_DNA.
DR EMBL; M17691; AAA28254.1; -; Genomic_DNA.
DR EMBL; M17692; AAA28255.1; -; Genomic_DNA.
DR EMBL; Y10622; CAA71640.1; -; Genomic_DNA.
DR PDB; 1ECA; X-ray; 1.40 A; A=16-151.
DR PDB; 1ECD; X-ray; 1.40 A; A=16-151.
DR PDB; 1ECN; X-ray; 1.40 A; A=16-151.
DR PDB; 1ECO; X-ray; 1.40 A; A=16-151.
DR PDBsum; 1ECA; -.
DR PDBsum; 1ECD; -.
DR PDBsum; 1ECN; -.
DR PDBsum; 1ECO; -.
DR AlphaFoldDB; P02229; -.
DR SMR; P02229; -.
DR Allergome; 201; Chi t 1.
DR Allergome; 202; Chi t 1.0101.
DR EvolutionaryTrace; P02229; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR CDD; cd01040; Mb-like; 1.
DR Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR002336; Erythrocruorin.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR044399; Mb-like_M.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR00611; ERYTHCRUORIN.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxygen transport; Signal; Transport.
FT SIGNAL 1..15
FT /evidence="ECO:0000269|PubMed:761849"
FT CHAIN 16..151
FT /note="Globin CTT-III"
FT /id="PRO_0000011190"
FT BINDING 73
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 102
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT VARIANT 72
FT /note="I -> T (in A and A')"
FT VARIANT 92..93
FT /note="EA -> DG (in A)"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:1ECA"
FT TURN 30..33
FT /evidence="ECO:0007829|PDB:1ECA"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:1ECA"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:1ECA"
FT TURN 54..58
FT /evidence="ECO:0007829|PDB:1ECA"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:1ECA"
FT HELIX 68..86
FT /evidence="ECO:0007829|PDB:1ECA"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:1ECA"
FT HELIX 92..102
FT /evidence="ECO:0007829|PDB:1ECA"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:1ECA"
FT HELIX 109..126
FT /evidence="ECO:0007829|PDB:1ECA"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:1ECA"
FT HELIX 133..150
FT /evidence="ECO:0007829|PDB:1ECA"
SQ SEQUENCE 151 AA; 16348 MW; 19EF29594AEF9FFB CRC64;
MKFLILALCF AAASALSADQ ISTVQASFDK VKGDPVGILY AVFKADPSIM AKFTQFAGKD
LESIKGTAPF EIHANRIVGF FSKIIGELPN IEADVNTFVA SHKPRGVTHD QLNNFRAGFV
SYMKAHTDFA GAEAAWGATL DTFFGMIFSK M
