GLB3_LUMTE
ID GLB3_LUMTE Reviewed; 170 AA.
AC P11069;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 3.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Extracellular globin-3;
DE AltName: Full=Erythrocruorin;
DE AltName: Full=Extracellular globin III;
DE AltName: Full=Globin C;
DE Flags: Precursor;
OS Lumbricus terrestris (Common earthworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Oligochaeta; Crassiclitellata; Lumbricina; Lumbricidae; Lumbricinae;
OC Lumbricus.
OX NCBI_TaxID=6398;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2808405; DOI=10.1016/s0021-9258(19)47257-8;
RA Jhiang S.M., Riggs A.F.;
RT "The structure of the gene encoding chain c of the hemoglobin of the
RT earthworm, Lumbricus terrestris.";
RL J. Biol. Chem. 264:19003-19008(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2832953; DOI=10.1126/science.2832953;
RA Jhiang S.M., Garey J.R., Riggs A.F.;
RT "Exon-intron organization in genes of earthworm and vertebrate globins.";
RL Science 240:334-336(1988).
RN [3]
RP PROTEIN SEQUENCE OF 18-170.
RX PubMed=3360792; DOI=10.1016/s0021-9258(18)68671-5;
RA Fushitani K., Matsuura M.S.A., Riggs A.F.;
RT "The amino acid sequences of chains a, b, and c that form the trimer
RT subunit of the extracellular hemoglobin from Lumbricus terrestris.";
RL J. Biol. Chem. 263:6502-6517(1988).
RN [4]
RP PROTEIN SEQUENCE OF 18-39.
RX PubMed=3593201; DOI=10.1042/bj2410441;
RA Gotoh T., Shishikura F., Snow J.W., Ereifej K.I., Vinogradov S.N.,
RA Walz D.A.;
RT "Two globin strains in the giant annelid extracellular haemoglobins.";
RL Biochem. J. 241:441-445(1987).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 18-170 IN COMPLEX WITH HEME, AND
RP SUBUNIT.
RX PubMed=15504406; DOI=10.1016/j.jmb.2004.08.094;
RA Strand K., Knapp J.E., Bhyravbhatla B., Royer W.E. Jr.;
RT "Crystal structure of the hemoglobin dodecamer from Lumbricus
RT erythrocruorin: allosteric core of giant annelid respiratory complexes.";
RL J. Mol. Biol. 344:119-134(2004).
CC -!- SUBUNIT: The extracellular hemoglobin of the earthworm consists of 12
CC subunits that have a hexagonal bilayer structure with a molecular
CC weight near 3.8 million. Each one-twelfth subunit is composed primarily
CC of disulfide linked trimers (chains A, B, and C) and monomers (chain
CC D). {ECO:0000269|PubMed:15504406}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; J03082; AAA75013.1; -; mRNA.
DR EMBL; J05161; AAA98622.1; -; Genomic_DNA.
DR PIR; A28563; A28563.
DR PIR; A34433; A34433.
DR PIR; C28151; C28151.
DR PDB; 1X9F; X-ray; 2.60 A; C/G/K=18-170.
DR PDB; 2GTL; X-ray; 3.50 A; C/G/K=18-170.
DR PDB; 4V93; EM; 8.10 A; A0/A5/AC/AH/AM/AR/AW/Ab/Ag/Al/Aq/Av=20-168, B4/BB/BG/BL/BQ/BV/Ba/Bf/Bk/Bp/Bu/Bz/C3/CA/CF/CK/CP/CU/CZ/Ce/Cj/Co/Ct/Cy=1-170.
DR PDB; 5M3L; EM; 3.80 A; C/G/K=18-170.
DR PDBsum; 1X9F; -.
DR PDBsum; 2GTL; -.
DR PDBsum; 4V93; -.
DR PDBsum; 5M3L; -.
DR AlphaFoldDB; P11069; -.
DR SMR; P11069; -.
DR DIP; DIP-29124N; -.
DR IntAct; P11069; 1.
DR EvolutionaryTrace; P11069; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR014610; Haemoglobin_extracell.
DR InterPro; IPR044399; Mb-like_M.
DR Pfam; PF00042; Globin; 1.
DR PIRSF; PIRSF036517; Ext_hemo; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Heme; Iron;
KW Metal-binding; Oxygen transport; Secreted; Signal; Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:3360792,
FT ECO:0000269|PubMed:3593201"
FT CHAIN 18..170
FT /note="Extracellular globin-3"
FT /id="PRO_0000011213"
FT BINDING 119
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 DISULFID 23
FT /note="Interchain (with chain IV)"
FT /evidence="ECO:0000250"
FT DISULFID 24..156
FT /evidence="ECO:0000250"
FT CONFLICT 17
FT /note="A -> T (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:2GTL"
FT HELIX 26..37
FT /evidence="ECO:0007829|PDB:1X9F"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:1X9F"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1X9F"
FT HELIX 45..63
FT /evidence="ECO:0007829|PDB:1X9F"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:1X9F"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1X9F"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1X9F"
FT HELIX 82..100
FT /evidence="ECO:0007829|PDB:1X9F"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:1X9F"
FT HELIX 105..120
FT /evidence="ECO:0007829|PDB:1X9F"
FT HELIX 127..144
FT /evidence="ECO:0007829|PDB:1X9F"
FT HELIX 150..165
FT /evidence="ECO:0007829|PDB:1X9F"
SQ SEQUENCE 170 AA; 19082 MW; 03306F66E8BE3057 CRC64;
MLRQLLVLVG LAVVCLADEH EHCCSEEDHR IVQKQWDILW RDTESSKIKI GFGRLLLTKL
AKDIPDVNDL FKRVDIEHAE GPKFSAHALR ILNGLDLAIN LLDDPPALDA ALDHLAHQHE
VREGVQKAHF KKFGEILATG LPQVLDDYDA LAWKSCLKGI LTKISSRLNA
