GLB1_CHITH
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 03-AUG-2022, entry version 92.
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; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; 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: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 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 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
