ID   HBF1_URECA              Reviewed;         142 AA.
AC   P06148;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Hemoglobin F-I;
OS   Urechis caupo (Innkeeper worm) (Spoonworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Echiura; Xenopneusta; Urechidae; Urechis.
OX   NCBI_TaxID=6431;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3782128; DOI=10.1016/s0021-9258(18)66586-x;
RA   Garey J.R., Riggs A.F.;
RT   "The hemoglobin of Urechis caupo. The cDNA-derived amino acid sequence.";
RL   J. Biol. Chem. 261:16446-16450(1986).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 2-142 IN COMPLEX WITH HEME.
RX   PubMed=1515107; DOI=10.1107/s0108768191012363;
RA   Kolatkar P.R., Ernst S.R., Hackert M.L., Ogata C.M., Hendrickson W.A.,
RA   Merrit E.A., Phizackerley R.P.;
RT   "Structure determination and refinement of homotetrameric hemoglobin from
RT   Urechis caupo at 2.5-A resolution.";
RL   Acta Crystallogr. B 48:191-199(1992).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=8133523; DOI=10.1006/jmbi.1994.1211;
RA   Kolatkar P.R., Hackert M.L., Riggs A.F.;
RT   "Structural analysis of Urechis caupo hemoglobin.";
RL   J. Mol. Biol. 237:87-97(1994).
CC   -!- FUNCTION: Hemoglobin F-I appears to function in storage, rather than
CC       transport of oxygen.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- MISCELLANEOUS: Hemoglobin F-I binds oxygen non-cooperatively and almost
CC       independently of pH.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; J02624; AAA30331.1; -; mRNA.
DR   PIR; A25537; A25537.
DR   PDB; 1ITH; X-ray; 2.50 A; A/B=2-142.
DR   PDBsum; 1ITH; -.
DR   AlphaFoldDB; P06148; -.
DR   SMR; P06148; -.
DR   EvolutionaryTrace; P06148; -.
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; 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   SUPFAM; SSF46458; SSF46458; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Heme; Iron; Metal-binding; Oxygen transport; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..142
FT                   /note="Hemoglobin F-I"
FT                   /id="PRO_0000053232"
FT   BINDING         95
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:0000269|PubMed:8133523,
FT                   ECO:0007744|PDB:1ITH"
FT   HELIX           5..18
FT                   /evidence="ECO:0007829|PDB:1ITH"
FT   HELIX           20..22
FT                   /evidence="ECO:0007829|PDB:1ITH"
FT   HELIX           23..37
FT                   /evidence="ECO:0007829|PDB:1ITH"
FT   HELIX           39..44
FT                   /evidence="ECO:0007829|PDB:1ITH"
FT   TURN            46..50
FT                   /evidence="ECO:0007829|PDB:1ITH"
FT   HELIX           53..58
FT                   /evidence="ECO:0007829|PDB:1ITH"
FT   HELIX           60..78
FT                   /evidence="ECO:0007829|PDB:1ITH"
FT   TURN            79..83
FT                   /evidence="ECO:0007829|PDB:1ITH"
FT   HELIX           84..89
FT                   /evidence="ECO:0007829|PDB:1ITH"
FT   HELIX           92..96
FT                   /evidence="ECO:0007829|PDB:1ITH"
FT   TURN            97..99
FT                   /evidence="ECO:0007829|PDB:1ITH"
FT   HELIX           102..119
FT                   /evidence="ECO:0007829|PDB:1ITH"
FT   HELIX           124..139
FT                   /evidence="ECO:0007829|PDB:1ITH"
SQ   SEQUENCE   142 AA;  15194 MW;  0958B579212FEB05 CRC64;
     MGLTTAQIKA IQDHWFLNIK GCLQAAADSI FFKYLTAYPG DLAFFHKFSS VPLYGLRSNP
     AYKAQTLTVI NYLDKVVDAL GGNAGALMKA KVPSHDAMGI TPKHFGQLLK LVGGVFQEEF
     SADPTTVAAW GDAAGVLVAA MK