GLB_APLLI
ID GLB_APLLI Reviewed; 147 AA.
AC P02210; Q93114;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Globin;
DE AltName: Full=Myoglobin;
OS Aplysia limacina (Sea hare).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC Aplysiidae; Aplysia.
OX NCBI_TaxID=6502;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8660313; DOI=10.1042/bj3140083;
RA Cutruzzola F., Travaglini Allocatelli C., Brancaccio A., Brunori M.;
RT "Aplysia limacina myoglobin cDNA cloning: an alternative mechanism of
RT oxygen stabilization as studied by active-site mutagenesis.";
RL Biochem. J. 314:83-90(1996).
RN [2]
RP PROTEIN SEQUENCE OF 2-147, AND ACETYLATION AT SER-2.
RC TISSUE=Buccal muscle;
RX PubMed=4759566; DOI=10.1111/j.1399-3011.1973.tb03452.x;
RA Tentori L., Vivaldi G., Carta S., Marinucci M., Massa A., Antonini E.,
RA Brunori M.;
RT "The amino acid sequence of myoglobin from the mollusc Aplysia limacina.";
RL Int. J. Pept. Protein Res. 5:187-200(1973).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=2926816; DOI=10.1016/0022-2836(89)90224-6;
RA Bolognesi M., Onesti S., Gatti G., Coda A., Ascenzi P., Brunori M.;
RT "Aplysia limacina myoglobin. Crystallographic analysis at 1.6-A
RT resolution.";
RL J. Mol. Biol. 205:529-544(1989).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SEQUENCE REVISION.
RX PubMed=1931125; DOI=10.1002/jmr.300040102;
RA Mattevi A., Gatti G., Coda A., Rizzi M., Ascenzi P., Brunori M.,
RA Bolognesi M.;
RT "Binding mode of azide to ferric Aplysia limacina myoglobin.
RT Crystallographic analysis at 1.9-A resolution.";
RL J. Mol. Recognit. 4:1-6(1991).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS).
RX PubMed=10694477; DOI=10.1006/bbrc.2000.2259;
RA Federici L., Savino C., Musto R., Travaglini-Allocatelli C., Cutruzzola F.,
RA Brunori M.;
RT "Engineering His(E7) affects the control of heme reactivity in Aplysia
RT limacina myoglobin.";
RL Biochem. Biophys. Res. Commun. 269:58-63(2000).
CC -!- SUBUNIT: Monomer.
CC -!- MISCELLANEOUS: This molluscan globin lacks one of the heme-binding
CC histidine residues found in most other globins.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; X79304; CAA55885.1; -; mRNA.
DR PIR; S64703; GGGAA.
DR PDB; 1DM1; X-ray; 1.99 A; A=2-147.
DR PDB; 1MBA; X-ray; 1.60 A; A=2-146.
DR PDB; 2FAL; X-ray; 1.80 A; A=2-146.
DR PDB; 2FAM; X-ray; 2.00 A; A=2-147.
DR PDB; 3MBA; X-ray; 2.00 A; A=2-146.
DR PDB; 4MBA; X-ray; 2.00 A; A=2-146.
DR PDB; 5MBA; X-ray; 1.90 A; A=2-146.
DR PDBsum; 1DM1; -.
DR PDBsum; 1MBA; -.
DR PDBsum; 2FAL; -.
DR PDBsum; 2FAM; -.
DR PDBsum; 3MBA; -.
DR PDBsum; 4MBA; -.
DR PDBsum; 5MBA; -.
DR AlphaFoldDB; P02210; -.
DR SMR; P02210; -.
DR iPTMnet; P02210; -.
DR EvolutionaryTrace; P02210; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
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; IPR002336; Erythrocruorin.
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; PR00611; ERYTHCRUORIN.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Heme; Iron;
KW Metal-binding; Muscle protein; Oxygen transport; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:4759566"
FT CHAIN 2..147
FT /note="Globin"
FT /id="PRO_0000052473"
FT BINDING 96
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 MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:4759566"
FT CONFLICT 23
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 27..28
FT /note="DA -> LD (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 5..20
FT /evidence="ECO:0007829|PDB:1MBA"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:1MBA"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:1MBA"
FT TURN 45..49
FT /evidence="ECO:0007829|PDB:1MBA"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:1MBA"
FT HELIX 61..78
FT /evidence="ECO:0007829|PDB:1MBA"
FT HELIX 82..98
FT /evidence="ECO:0007829|PDB:1MBA"
FT HELIX 103..118
FT /evidence="ECO:0007829|PDB:1MBA"
FT HELIX 127..144
FT /evidence="ECO:0007829|PDB:1MBA"
SQ SEQUENCE 147 AA; 15456 MW; 631C4959E1B7CC86 CRC64;
MSLSAAEADL AGKSWAPVFA NKDANGDAFL VALFEKFPDS ANFFADFKGK SVADIKASPK
LRDVSSRIFT RLNEFVNNAA DAGKMSAMLS QFAKEHVGFG VGSAQFENVR SMFPGFVASV
AAPPAGADAA WTKLFGLIID ALKAAGK
