ID   GLB3_CHITP              Reviewed;         136 AA.
AC   P22431;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Globin CTP-III;
DE   AltName: Full=Erythrocruorin III;
OS   Chironomus thummi piger (Midge) (Chironomus piger).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC   Chironominae; Chironomus.
OX   NCBI_TaxID=7156;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=2590466; DOI=10.1515/bchm3.1989.370.2.839;
RA   Kleinschmidt T., Keyl H.G., Braunitzer G.;
RT   "Comparison of insect hemoglobins (Erythrocruorins) from Chironomus thummi
RT   thummi and Chironomus thummi piger (Diptera). The primary structure of the
RT   monomeric hemoglobin CTP III.";
RL   Biol. Chem. Hoppe-Seyler 370:839-845(1989).
CC   -!- SUBUNIT: Monomer.
CC   -!- MISCELLANEOUS: There are at least 12 different components in Midge
CC       globin.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; A91687; GGICE3.
DR   PIR; S05422; GGIC3.
DR   AlphaFoldDB; P22431; -.
DR   SMR; P22431; -.
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   Direct protein sequencing; Heme; Iron; Metal-binding; Oxygen transport;
KW   Transport.
FT   CHAIN           1..136
FT                   /note="Globin CTP-III"
FT                   /id="PRO_0000052467"
FT   BINDING         87
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="proximal binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT   VARIANT         57
FT                   /note="T -> I"
FT   VARIANT         105
FT                   /note="V -> I"
FT   VARIANT         134
FT                   /note="S -> A"
SQ   SEQUENCE   136 AA;  14784 MW;  6B41264976640245 CRC64;
     LSADQISTVQ ASFDKVKGDP VGILYAVFKA DPSIMAKFTQ FAGKDLESIK GTAPFETHAN
     RIVGFFSKII GELPNIEADV NTFVASHKPR GVTHDQLNNF RAGFVSYMKA HTDFAGAEAA
     WGATLDTFFG MIFSKM