ID   GLB4_GLYDI              Reviewed;         148 AA.
AC   P15447; P81779;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Globin, monomeric component M-IV;
DE   AltName: Full=GMH4;
OS   Glycera dibranchiata (Bloodworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Errantia; Phyllodocida; Glyceridae; Glycera.
OX   NCBI_TaxID=6350;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-25.
RX   PubMed=2605202; DOI=10.1021/bi00447a038;
RA   Simons P.C., Satterlee J.D.;
RT   "cDNA cloning and predicted amino acid sequence of Glycera dibranchiata
RT   monomer hemoglobin IV.";
RL   Biochemistry 28:8525-8530(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-148, MASS SPECTROMETRY, AND 3D-STRUCTURE MODELING.
RC   TISSUE=Erythrocyte;
RX   PubMed=8060489; DOI=10.1007/bf01891974;
RA   Alam S.L., Satterlee J.D., Edmonds C.G.;
RT   "Complete amino acid sequence of the Glycera dibranchiata monomer
RT   hemoglobin component IV: structural implications.";
RL   J. Protein Chem. 13:151-164(1994).
RN   [3]
RP   STRUCTURE BY NMR.
RX   PubMed=9692983; DOI=10.1021/bi980810b;
RA   Volkman B.F., Alam S.L., Satterlee J.D., Markley J.L.;
RT   "Solution structure and backbone dynamics of component IV Glycera
RT   dibranchiata monomeric hemoglobin-CO.";
RL   Biochemistry 37:10906-10919(1998).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS)IN COMPLEX WITH HEME, AND SUBUNIT.
RX   PubMed=12211015; DOI=10.1002/prot.10199;
RA   Park H.J., Yang C., Treff N., Satterlee J.D., Kang C.;
RT   "Crystal structures of unligated and CN-ligated Glycera dibranchiata
RT   monomer ferric hemoglobin components III and IV.";
RL   Proteins 49:49-60(2002).
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12211015}.
CC   -!- MASS SPECTROMETRY: Mass=15031.6; Mass_error=3.8; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:8060489};
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; J02873; AAA29162.1; -; mRNA.
DR   PIR; A33420; A33420.
DR   PDB; 1JF4; X-ray; 1.40 A; A=2-148.
DR   PDB; 1JL6; X-ray; 1.40 A; A=2-148.
DR   PDB; 1VRE; NMR; -; A=2-148.
DR   PDB; 1VRF; NMR; -; A=2-148.
DR   PDBsum; 1JF4; -.
DR   PDBsum; 1JL6; -.
DR   PDBsum; 1VRE; -.
DR   PDBsum; 1VRF; -.
DR   AlphaFoldDB; P15447; -.
DR   BMRB; P15447; -.
DR   SMR; P15447; -.
DR   EvolutionaryTrace; P15447; -.
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; Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Oxygen transport; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2605202,
FT                   ECO:0000269|PubMed:8060489"
FT   CHAIN           2..148
FT                   /note="Globin, monomeric component M-IV"
FT                   /id="PRO_0000052502"
FT   BINDING         91
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT   HELIX           5..19
FT                   /evidence="ECO:0007829|PDB:1JF4"
FT   TURN            20..24
FT                   /evidence="ECO:0007829|PDB:1JF4"
FT   HELIX           25..38
FT                   /evidence="ECO:0007829|PDB:1JF4"
FT   HELIX           40..42
FT                   /evidence="ECO:0007829|PDB:1JF4"
FT   HELIX           43..46
FT                   /evidence="ECO:0007829|PDB:1JF4"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:1VRE"
FT   HELIX           55..72
FT                   /evidence="ECO:0007829|PDB:1JF4"
FT   TURN            73..75
FT                   /evidence="ECO:0007829|PDB:1JF4"
FT   HELIX           77..90
FT                   /evidence="ECO:0007829|PDB:1JF4"
FT   HELIX           91..93
FT                   /evidence="ECO:0007829|PDB:1JF4"
FT   STRAND          94..97
FT                   /evidence="ECO:0007829|PDB:1JF4"
FT   HELIX           101..103
FT                   /evidence="ECO:0007829|PDB:1JF4"
FT   HELIX           104..119
FT                   /evidence="ECO:0007829|PDB:1JF4"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:1JF4"
FT   HELIX           125..146
FT                   /evidence="ECO:0007829|PDB:1JF4"
SQ   SEQUENCE   148 AA;  15178 MW;  9206F7FBE1CAB7F1 CRC64;
     MGLSAAQRQV VASTWKDIAG SDNGAGVGKE CFTKFLSAHH DIAAVFGFSG ASDPGVADLG
     AKVLAQIGVA VSHLGDEGKM VAEMKAVGVR HKGYGYKHIK AEYFEPLGAS LLSAMEHRIG
     GKMTAAAKDA WAAAYADISG ALISGLQS