ID   GLB2_LUMTE              Reviewed;         145 AA.
AC   P02218;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Extracellular globin-2;
DE   AltName: Full=Erythrocruorin;
DE   AltName: Full=Globin AIII;
DE   AltName: Full=Globin B;
DE   AltName: Full=Globin II;
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   PROTEIN SEQUENCE.
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   [2]
RP   PRELIMINARY PROTEIN SEQUENCE.
RX   PubMed=7096348; DOI=10.1016/s0021-9258(18)34233-9;
RA   Garlick R.L., Riggs A.F.;
RT   "The amino acid sequence of a major polypeptide chain of earthworm
RT   hemoglobin.";
RL   J. Biol. Chem. 257:9005-9015(1982).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH HEME, AND 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   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; A02540; GGEWA3.
DR   PIR; B28151; B28151.
DR   PDB; 1X9F; X-ray; 2.60 A; B/F/J=1-145.
DR   PDB; 2GTL; X-ray; 3.50 A; B/F/J=1-145.
DR   PDB; 4V93; EM; 8.10 A; A4/AB/AG/AL/AQ/AV/Aa/Af/Ak/Ap/Au/Az/B2/B3/B7/BA/BE/BF/BJ/BK/BO/BP/BT/BU/BY/BZ/Bd/Be/Bi/Bj/Bn/Bo/Bs/Bt/Bx/By=1-145.
DR   PDB; 5M3L; EM; 3.80 A; B/F/J=1-145.
DR   PDBsum; 1X9F; -.
DR   PDBsum; 2GTL; -.
DR   PDBsum; 4V93; -.
DR   PDBsum; 5M3L; -.
DR   AlphaFoldDB; P02218; -.
DR   SMR; P02218; -.
DR   DIP; DIP-29123N; -.
DR   IntAct; P02218; 1.
DR   EvolutionaryTrace; P02218; -.
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; IPR014610; Haemoglobin_extracell.
DR   InterPro; IPR044399; Mb-like_M.
DR   Pfam; PF00042; Globin; 1.
DR   PIRSF; PIRSF036517; Ext_hemo; 1.
DR   PRINTS; PR00611; ERYTHCRUORIN.
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; Transport.
FT   CHAIN           1..145
FT                   /note="Extracellular globin-2"
FT                   /id="PRO_0000052512"
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   DISULFID        4..133
FT                   /evidence="ECO:0000250"
FT   DISULFID        124
FT                   /note="Interchain (with chain IV)"
FT                   /evidence="ECO:0000250"
FT   HELIX           6..20
FT                   /evidence="ECO:0007829|PDB:1X9F"
FT   HELIX           23..40
FT                   /evidence="ECO:0007829|PDB:1X9F"
FT   HELIX           42..51
FT                   /evidence="ECO:0007829|PDB:1X9F"
FT   TURN            52..54
FT                   /evidence="ECO:0007829|PDB:1X9F"
FT   HELIX           59..77
FT                   /evidence="ECO:0007829|PDB:1X9F"
FT   TURN            78..80
FT                   /evidence="ECO:0007829|PDB:1X9F"
FT   HELIX           82..96
FT                   /evidence="ECO:0007829|PDB:1X9F"
FT   HELIX           103..121
FT                   /evidence="ECO:0007829|PDB:1X9F"
FT   HELIX           127..142
FT                   /evidence="ECO:0007829|PDB:1X9F"
SQ   SEQUENCE   145 AA;  16254 MW;  5F62E08A11AA52A6 CRC64;
     KKQCGVLEGL KVKSEWGRAY GSGHDREAFS QAIWRATFAQ VPESRSLFKR VHGDDTSHPA
     FIAHAERVLG GLDIAISTLD QPATLKEELD HLQVQHEGRK IPDNYFDAFK TAILHVVAAQ
     LGRCYDREAW DACIDHIEDG IKGHH