ID   GLB1_CHITH              Reviewed;         158 AA.
AC   P02221;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   04-NOV-2026, entry version 97.
DE   RecName: Full=Globin CTT-I/CTT-IA;
DE   AltName: Full=Erythrocruorin;
DE   Flags: Precursor;
GN   Name=CTT-1;
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] (CTT-I).
RX   PubMed=7769612; DOI=10.1007/bf00164021;
RA   Kao W.-Y., Hankeln T., Schmidt E.R., Bergtrom G.;
RT   "Sequence and evolution of the gene for the monomeric globin I and its
RT   linkage to genes coding for dimeric globins in the insect Chironomus
RT   thummi.";
RL   J. Mol. Evol. 40:354-361(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 16-158 (CTT-I).
RX   PubMed=7380386;
RA   Kleinschmidt T., von der Mark-Neuwirth H., Braunitzer G.;
RT   "Hemoglobin, XXXI. Analysis or the primary structure of the monomeric
RT   hemoglobin CTT I (erythrocruorin) of Chironomus thummi thummi, Diptera.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 361:401-411(1980).
RN   [3]
RP   PROTEIN SEQUENCE OF 16-158 (CTT-IA).
RX   PubMed=6862374; DOI=10.1515/bchm2.1983.364.1.205;
RA   Goodman M., Braunitzer G., Kleinschmidt T., Aschauer H.;
RT   "The analysis of a protein-polymorphism. Evolution of monomeric and
RT   homodimeric haemoglobins (erythrocruorins) of Chironomus thummi thummi
RT   (Insecta, Diptera).";
RL   Hoppe-Seyler's Z. Physiol. Chem. 364:205-217(1983).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 83-158 (CTT-IA).
RX   PubMed=2055487; DOI=10.1016/0378-1119(91)90414-7;
RA   Saffarini D.A., Trewitt P.M., Luhm R.A., Bergtrom G.;
RT   "Differential regulation of insect globin and actin mRNAs during larval
RT   development in Chironomus thummi.";
RL   Gene 101:215-222(1991).
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   EMBL; U14627; AAA80189.1; -; Genomic_DNA.
DR   EMBL; U14628; AAA80190.1; -; Genomic_DNA.
DR   EMBL; U14629; AAA80191.1; -; Genomic_DNA.
DR   EMBL; M57410; AAA62727.1; -; mRNA.
DR   PIR; A91690; GGICE1.
DR   PIR; A91719; GGIC1A.
DR   AlphaFoldDB; P02221; -.
DR   SMR; P02221; -.
DR   Allergome; 1650; Chi t 2.
DR   Allergome; 205; Chi t 2.0101.
DR   Allergome; 206; Chi t 2.0102.
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   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.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Iron; Metal-binding; Oxygen transport;
KW   Signal; Transport.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000269|PubMed:6862374,
FT                   ECO:0000269|PubMed:7380386"
FT   CHAIN           16..158
FT                   /note="Globin CTT-I/CTT-IA"
FT                   /id="PRO_0000011188"
FT   DOMAIN          16..158
FT                   /note="Globin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT   BINDING         74
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="distal binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT   BINDING         109
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         113
FT                   /note="A -> T (in CTT-IA)"
SQ   SEQUENCE   158 AA;  17012 MW;  9639E8A38908B8AB CRC64;
     MKFLILALCV AAAMAGPSGD QIAAAKASWN TVKNNQVDIL YAVFKANPDI QTAFSQFAGK
     DLDSIKGTPD FSKHAGRVVG LFSEVMDLLG NDANTPTILA KAKDFGKSHK SRASPAQLDN
     FRKSLVVYLK GATKWDSAVE SSWAPVLDFV FSTLKNEL
//