GLB7A_CHITH
ID GLB7A_CHITH Reviewed; 161 AA.
AC P02226; O02368;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Globin CTT-VIIA;
DE Flags: Precursor;
GN Name=ctt-7A.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].
RX PubMed=8006991; DOI=10.1007/bf00176086;
RA Kao W.-Y., Trewitt P.M., Bergtrom G.;
RT "Intron-containing globin genes in the insect Chironomus thummi.";
RL J. Mol. Evol. 38:241-249(1994).
RN [2]
RP PROTEIN SEQUENCE OF 17-161.
RX PubMed=7399413;
RA Kleinschmidt T., Braunitzer G.;
RT "Hemoglobins, XXXII. Analysis of the primary structure of the monomeric
RT hemoglobin CTT VIIA (erythrocruorin) or Chironomus thummi thummi,
RT Diptera.";
RL Hoppe-Seyler's Z. Physiol. Chem. 361:933-942(1980).
CC -!- SUBUNIT: Homodimer.
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; AF001292; AAB58930.1; -; Genomic_DNA.
DR PIR; A02548; GGICE7.
DR AlphaFoldDB; P02226; -.
DR SMR; P02226; -.
DR Allergome; 207; Chi t 3.
DR Allergome; 210; Chi t 3.0301.
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..16
FT /evidence="ECO:0000269|PubMed:7399413"
FT CHAIN 17..161
FT /note="Globin CTT-VIIA"
FT /id="PRO_0000011193"
FT BINDING 76
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 111
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 CONFLICT 17
FT /note="S -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="A -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 161 AA; 16830 MW; 4C3A620317025D30 CRC64;
MKFFAVLALC IVGAIASPLS ADQAALVKST WAQVRNSEVE ILAAVFTAYP DIQARFPQFA
GKDVASIKDT GAFATHAGRI VGFVSEIIAL IGNESNAPAV QTLVGQLAAS HKARGISQAQ
FNEFRAGLVS YVSSNVAWNA AAESAWTAGL DNIFGLLFAA L