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 04-NOV-2026, entry version 113. 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; Altocrustacea; Allotriocarida; OC Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota; OC Aparaglossata; Panorpida; 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. 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. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; P02229; -. DR Allergome; 201; Chi t 1. DR Allergome; 202; Chi t 1.0101. DR EvolutionaryTrace; P02229; -. DR PRO; PR:P02229; -. DR CDD; cd01040; Mb-like; 1. DR Gene3D; 1.10.490.10; Globins; 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 PANTHER; PTHR47217; GLOBIN-LIKE PROTEIN; 1. DR PANTHER; PTHR47217:SF1; GLOBIN-LIKE PROTEIN; 1. DR Pfam; PF00042; Globin; 1. DR PRINTS; PR00611; ERYTHCRUORIN. DR SUPFAM; SSF46458; Globin-like; 1. DR PROSITE; PS01033; GLOBIN; 1. 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:0019825; F:oxygen binding; IEA:InterPro. DR GO; GO:0015671; P:oxygen transport; IEA:InterPro. DR AlphaFoldDB; P02229; -. DR MDposit; P02229; -. 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 DOMAIN 16..151 FT /note="Globin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00238" 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 //