GLBF1_EPTBU
ID GLBF1_EPTBU Reviewed; 146 AA.
AC Q7SID0;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Globin-F1;
OS Eptatretus burgeri (Inshore hagfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata; Myxini;
OC Myxiniformes; Myxinidae; Eptatretinae; Eptatretus.
OX NCBI_TaxID=7764;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN
RP COMPLEX WITH CARBON MONOXIDE, AND SUBUNIT.
RX PubMed=11923284; DOI=10.1074/jbc.m111492200;
RA Mito M., Chong K.T., Miyazaki G., Adachi S., Park S.Y., Tame J.R.,
RA Morimoto H.;
RT "Crystal structures of deoxy- and carbonmonoxyhemoglobin F1 from the
RT hagfish Eptatretus burgeri.";
RL J. Biol. Chem. 277:21898-21905(2002).
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11923284}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PDB; 1IT2; X-ray; 1.60 A; A/B=1-146.
DR PDB; 1IT3; X-ray; 2.10 A; A/B/C/D=1-146.
DR PDBsum; 1IT2; -.
DR PDBsum; 1IT3; -.
DR AlphaFoldDB; Q7SID0; -.
DR SMR; Q7SID0; -.
DR EvolutionaryTrace; Q7SID0; -.
DR Proteomes; UP000694388; Unplaced.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR013314; Globin_lamprey/hagfish.
DR InterPro; IPR044399; Mb-like_M.
DR PANTHER; PTHR46783; PTHR46783; 1.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR01906; FISHGLOBIN.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Heme; Iron; Metal-binding; Oxygen transport;
KW Reference proteome; Transport.
FT CHAIN 1..146
FT /note="Globin-F1"
FT /id="PRO_0000232421"
FT BINDING 71
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 ECO:0000269|PubMed:11923284"
FT BINDING 103
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 ECO:0000269|PubMed:11923284"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:1IT2"
FT HELIX 13..27
FT /evidence="ECO:0007829|PDB:1IT2"
FT HELIX 30..44
FT /evidence="ECO:0007829|PDB:1IT2"
FT HELIX 46..51
FT /evidence="ECO:0007829|PDB:1IT2"
FT TURN 53..57
FT /evidence="ECO:0007829|PDB:1IT2"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1IT3"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1IT2"
FT HELIX 66..83
FT /evidence="ECO:0007829|PDB:1IT2"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:1IT2"
FT HELIX 89..105
FT /evidence="ECO:0007829|PDB:1IT2"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:1IT2"
FT HELIX 129..143
FT /evidence="ECO:0007829|PDB:1IT2"
SQ SEQUENCE 146 AA; 16843 MW; BDADA2752C60B25D CRC64;
PIIDQGPLPT LTDGDKKAIN KIWPKIYKEY EQYSLNILLR FLKCFPQAQA SFPKFSTKKS
NLEQDPEVKH QAVVIFNKVN EIINSMDNQE EIIKSLKDLS QKHKTVFKVD SIWFKELSSI
FVSTIDGGAE FEKLFSIICI LLRSAY