GLB6_CHITH
ID GLB6_CHITH Reviewed; 162 AA.
AC P02224;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Globin CTT-VI;
DE Flags: Precursor;
GN Name=CTT-6;
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=7875590; DOI=10.1016/0378-1119(94)00773-l;
RA Kao W.-Y., Bergtrom G.;
RT "Sequences of globin 6 gene alleles and linkage of globin 6 and 7B genes in
RT the insect Chironomus thummi thummi.";
RL Gene 153:209-213(1995).
RN [2]
RP PROTEIN SEQUENCE OF 16-162.
RX PubMed=7227979; DOI=10.1515/bchm2.1981.362.1.261;
RA Aschauer H., Zaidi Z.H., Braunitzer G.;
RT "Hemoglobins, XXXVIII. Amino acid sequence of a dimeric hemoglobin
RT (erythrocruorin), component VI from Chironomus thummi thummi (CTT VI).";
RL Hoppe-Seyler's Z. Physiol. Chem. 362:261-273(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 124-162.
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: 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; U01340; AAA69813.1; -; Genomic_DNA.
DR EMBL; U01341; AAA69814.1; -; Genomic_DNA.
DR EMBL; M57411; AAA62728.1; -; mRNA.
DR PIR; A02546; GGICE6.
DR AlphaFoldDB; P02224; -.
DR SMR; P02224; -.
DR Allergome; 207; Chi t 3.
DR Allergome; 3194; Chi t 3.0201.
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:7227979"
FT CHAIN 16..162
FT /note="Globin CTT-VI"
FT /id="PRO_0000011192"
FT BINDING 75
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 110
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 162 AA; 17709 MW; 73F256783F62C05E CRC64;
MKFLVLALCI AAASAAVLTT EQADLVKKTW STVKFNEVDI LYAVFKAYPD IMAKFPQFAG
KDLDSIKDSA AFATHATRIV SFLSEVISLA GSDANIPAIQ NLAKELATSH KPRGVSKDQF
TEFRTALFTY LKAHINFDGP TETAWTLALD TTYAMLFSAM DS
