ID   GLBT_CHITH              Reviewed;         151 AA.
AC   P02231;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Globin CTT-IIIA;
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   PROTEIN SEQUENCE.
RX   PubMed=7216163; DOI=10.1515/bchm2.1981.362.1.73;
RA   Steer W., Braunitzer G.;
RT   "Hemoglobins, XXXVII. The primary structure of a monomeric insect
RT   hemoglobin (Erythrocruorin), component CTT IIIa of Chironomus thummi
RT   thummi. An anomalous Heme complex: E7 Gln, E11 Ile.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 362:73-80(1981).
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; A02553; GGICEA.
DR   AlphaFoldDB; P02231; -.
DR   SMR; P02231; -.
DR   Allergome; 208; Chi t 4.
DR   Allergome; 3193; Chi t 4.0101.
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..151
FT                   /note="Globin CTT-IIIA"
FT                   /id="PRO_0000052468"
FT   BINDING         98
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"
SQ   SEQUENCE   151 AA;  16155 MW;  38DB0DAC4AE64E2E CRC64;
     VATPAMPSMT DAQVAAVKGD WEKIKGSGVE ILYFFLNKFP GNFPMFKKLG NDLAAAKGTA
     EFKDQADKII AFLQGVIEKL GSDMGGAKAL LNQLGTSHKA MGITKDQFDQ FRQALTELLG
     NLGFGGNIGA WNATVDLMFH VIFNALDGTP V