ID   GLBN_CERLA              Reviewed;         110 AA.
AC   O76242;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Neural hemoglobin;
DE            Short=NrHb;
OS   Cerebratulus lacteus (Milky ribbon worm) (Micrura lactea).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Nemertea; Pilidiophora;
OC   Heteronemertea; Lineidae; Cerebratulus.
OX   NCBI_TaxID=6221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-44, AND
RP   CHARACTERIZATION.
RC   TISSUE=Brain;
RX   PubMed=9642264; DOI=10.1074/jbc.273.27.16998;
RA   Vandergon T.L., Riggs C.K., Gorr T.A., Colacino J.M., Riggs A.F.;
RT   "The mini-hemoglobins in neural and body wall tissue of the nemertean worm,
RT   Cerebratulus lacteus.";
RL   J. Biol. Chem. 273:16998-17011(1998).
RN   [2]
RP   CRYSTALLIZATION.
RX   PubMed=11717510; DOI=10.1107/s0907444901015815;
RA   Pesce A., Nardini M., Dewilde S., Ascenzi P., Riggs A.F., Yamauchi K.,
RA   Geuens E., Moens L., Bolognesi M.;
RT   "Crystallization and preliminary X-ray analysis of neural haemoglobin from
RT   the nemertean worm Cerebratulus lacteus.";
RL   Acta Crystallogr. D 57:1897-1899(2001).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH HEME.
RX   PubMed=12015154; DOI=10.1016/s0969-2126(02)00763-3;
RA   Pesce A., Nardini M., Dewilde S., Geuens E., Yamauchi K., Ascenzi P.,
RA   Riggs A.F., Moens L., Bolognesi M.;
RT   "The 109 residue nerve tissue minihemoglobin from Cerebratulus lacteus
RT   highlights striking structural plasticity of the alpha-helical globin
RT   fold.";
RL   Structure 10:725-735(2002).
CC   -!- FUNCTION: Acts as an oxygen store capable of sustaining neuronal
CC       activity in an anoxic environment for 5 to 30 min.
CC   -!- SUBUNIT: Homotetramer. Self-associates in the deoxy state. Seems to
CC       dissociate upon oxygenation. {ECO:0000269|PubMed:12015154}.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000305}.
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DR   EMBL; AF033001; AAC39125.1; -; Genomic_DNA.
DR   PDB; 1KR7; X-ray; 1.50 A; A=1-110.
DR   PDB; 1V07; X-ray; 1.70 A; A=2-110.
DR   PDB; 2VYY; X-ray; 1.60 A; A=1-110.
DR   PDB; 2VYZ; X-ray; 1.80 A; A=1-110.
DR   PDB; 2XKG; X-ray; 1.60 A; A=1-110.
DR   PDB; 2XKH; X-ray; 2.31 A; A=1-110.
DR   PDB; 2XKI; X-ray; 1.30 A; A=1-110.
DR   PDB; 4AVD; X-ray; 1.50 A; A=1-110.
DR   PDB; 4AVE; X-ray; 1.90 A; A=1-110.
DR   PDB; 4F68; X-ray; 1.80 A; A=1-110.
DR   PDB; 4F69; X-ray; 1.60 A; A=1-110.
DR   PDB; 4F6B; X-ray; 1.64 A; A=1-110.
DR   PDB; 4F6D; X-ray; 1.80 A; A=1-110.
DR   PDB; 4F6F; X-ray; 1.56 A; A=1-110.
DR   PDB; 4F6G; X-ray; 1.64 A; A=1-110.
DR   PDB; 4F6I; X-ray; 1.56 A; A=1-110.
DR   PDB; 4F6J; X-ray; 1.45 A; A=1-110.
DR   PDBsum; 1KR7; -.
DR   PDBsum; 1V07; -.
DR   PDBsum; 2VYY; -.
DR   PDBsum; 2VYZ; -.
DR   PDBsum; 2XKG; -.
DR   PDBsum; 2XKH; -.
DR   PDBsum; 2XKI; -.
DR   PDBsum; 4AVD; -.
DR   PDBsum; 4AVE; -.
DR   PDBsum; 4F68; -.
DR   PDBsum; 4F69; -.
DR   PDBsum; 4F6B; -.
DR   PDBsum; 4F6D; -.
DR   PDBsum; 4F6F; -.
DR   PDBsum; 4F6G; -.
DR   PDBsum; 4F6I; -.
DR   PDBsum; 4F6J; -.
DR   AlphaFoldDB; O76242; -.
DR   SMR; O76242; -.
DR   EvolutionaryTrace; O76242; -.
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.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Oxygen transport; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9642264"
FT   CHAIN           2..110
FT                   /note="Neural hemoglobin"
FT                   /id="PRO_0000052499"
FT   BINDING         70
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="proximal binding residue"
FT   HELIX           4..18
FT                   /evidence="ECO:0007829|PDB:2XKI"
FT   HELIX           20..25
FT                   /evidence="ECO:0007829|PDB:2XKI"
FT   TURN            27..30
FT                   /evidence="ECO:0007829|PDB:2XKI"
FT   HELIX           33..38
FT                   /evidence="ECO:0007829|PDB:2XKI"
FT   HELIX           40..58
FT                   /evidence="ECO:0007829|PDB:2XKI"
FT   HELIX           63..71
FT                   /evidence="ECO:0007829|PDB:2XKI"
FT   TURN            72..74
FT                   /evidence="ECO:0007829|PDB:2XKI"
FT   HELIX           77..93
FT                   /evidence="ECO:0007829|PDB:2XKI"
FT   HELIX           100..107
FT                   /evidence="ECO:0007829|PDB:2XKI"
SQ   SEQUENCE   110 AA;  11530 MW;  0F30C4420773F244 CRC64;
     MVNWAAVVDD FYQELFKAHP EYQNKFGFKG VALGSLKGNA AYKTQAGKTV DYINAAIGGS
     ADAAGLASRH KGRNVGSAEF HNAKACLAKA CSAHGAPDLG HAIDDILSHL