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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
 
 
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