ID   GLB4_LUMTE              Reviewed;         151 AA.
AC   P13579;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Extracellular globin-4;
DE   AltName: Full=Erythrocruorin;
DE   AltName: Full=Globin A;
DE   AltName: Full=Globin IV;
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   PROTEIN SEQUENCE OF 1-10.
RX   PubMed=8597573; DOI=10.1016/0167-4838(95)00214-6;
RA   Fushitani K., Higashiyama K., Asao M., Hosokawa K.;
RT   "Characterization of the constituent polypeptides of the extracellular
RT   hemoglobin from Lumbricus terrestris: heterogeneity and discovery of a new
RT   linker chain L4.";
RL   Biochim. Biophys. Acta 1292:273-280(1996).
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PIR; A28151; A28151.
DR   PDB; 1X9F; X-ray; 2.60 A; A/E/I=1-151.
DR   PDB; 2GTL; X-ray; 3.50 A; A/E/I=1-151.
DR   PDB; 4V93; EM; 8.10 A; A2/A3/A7/AA/AE/AF/AJ/AK/AO/AP/AT/AU/AY/AZ/Ad/Ae/Ai/Aj/An/Ao/As/At/Ax/Ay=5-151, B1/B6/BD/BI/BN/BS/BX/Bc/Bh/Bm/Br/Bw=1-151.
DR   PDB; 5M3L; EM; 3.80 A; A/E/I=1-151.
DR   PDBsum; 1X9F; -.
DR   PDBsum; 2GTL; -.
DR   PDBsum; 4V93; -.
DR   PDBsum; 5M3L; -.
DR   AlphaFoldDB; P13579; -.
DR   SMR; P13579; -.
DR   DIP; DIP-29122N; -.
DR   IntAct; P13579; 1.
DR   EvolutionaryTrace; P13579; -.
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; Transport.
FT   CHAIN           1..151
FT                   /note="Extracellular globin-4"
FT                   /id="PRO_0000052515"
FT   BINDING         101
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        6
FT                   /note="Interchain (with chain III)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        7..138
FT                   /evidence="ECO:0000250"
FT   DISULFID        129
FT                   /note="Interchain (with chain I)"
FT                   /evidence="ECO:0000250"
FT   HELIX           9..22
FT                   /evidence="ECO:0007829|PDB:1X9F"
FT   STRAND          26..28
FT                   /evidence="ECO:0007829|PDB:1X9F"
FT   HELIX           29..45
FT                   /evidence="ECO:0007829|PDB:1X9F"
FT   HELIX           47..53
FT                   /evidence="ECO:0007829|PDB:1X9F"
FT   TURN            54..59
FT                   /evidence="ECO:0007829|PDB:1X9F"
FT   HELIX           65..81
FT                   /evidence="ECO:0007829|PDB:1X9F"
FT   TURN            82..85
FT                   /evidence="ECO:0007829|PDB:1X9F"
FT   HELIX           87..102
FT                   /evidence="ECO:0007829|PDB:1X9F"
FT   HELIX           109..126
FT                   /evidence="ECO:0007829|PDB:1X9F"
FT   STRAND          127..129
FT                   /evidence="ECO:0007829|PDB:2GTL"
FT   HELIX           132..146
FT                   /evidence="ECO:0007829|PDB:1X9F"
FT   TURN            147..149
FT                   /evidence="ECO:0007829|PDB:1X9F"
SQ   SEQUENCE   151 AA;  17525 MW;  4A2C7421F0DCBC2F CRC64;
     ADDEDCCSYE DRREIRHIWD DVWSSSFTDR RVAIVRAVFD DLFKHYPTSK ALFERVKIDE
     PESGEFKSHL VRVANGLDLL INLLDDTLVL QSHLGHLADQ HIQRKGVTKE YFRGIGEAFA
     RVLPQVLSCF NVDAWNRCFH RLVARIAKDL P