GLB1_ANAIN
ID GLB1_ANAIN Reviewed; 146 AA.
AC P02213;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Globin-1;
DE AltName: Full=Dimeric hemoglobin;
DE AltName: Full=Globin I;
DE AltName: Full=HbI;
OS Anadara inaequivalvis (Inequivalve ark) (Scapharca inaequivalvis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Arcoida; Arcoidea; Arcidae; Anadara.
OX NCBI_TaxID=2784303;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Hemocyte;
RX PubMed=3996589; DOI=10.1016/0014-5793(85)80632-3;
RA Petruzzelli R., Goffredo B.M., Barra D., Bossa F., Boffi A., Verzili D.,
RA Ascoli F., Chiancone E.;
RT "Amino acid sequence of the cooperative homodimeric hemoglobin from the
RT mollusc Scapharca inaequivalvis and topology of the intersubunit
RT contacts.";
RL FEBS Lett. 184:328-332(1985).
RN [2]
RP SEQUENCE REVISION TO 56.
RX PubMed=8370466; DOI=10.1016/0014-5793(93)80926-l;
RA Gambacurta A., Piro M.C., Ascoli F.;
RT "Cooperative homodimeric hemoglobin from Scapharca inaequivalvis. cDNA
RT cloning and expression of the fully functional protein in E. coli.";
RL FEBS Lett. 330:90-94(1993).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS).
RX PubMed=4022123; DOI=10.1038/316277a0;
RA Royer W.E. Jr., Love W.E., Fenderson F.F.;
RT "Cooperative dimeric and tetrameric clam haemoglobins are novel assemblages
RT of myoglobin folds.";
RL Nature 316:277-280(1985).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=2592366; DOI=10.1016/s0021-9258(19)30044-4;
RA Royer W.E. Jr., Hendrickson W.A., Chiancone E.;
RT "The 2.4-A crystal structure of Scapharca dimeric hemoglobin. Cooperativity
RT based on directly communicating hemes at a novel subunit interface.";
RL J. Biol. Chem. 264:21052-21061(1989).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
RX PubMed=8289287; DOI=10.1006/jmbi.1994.1019;
RA Royer W.E. Jr.;
RT "High-resolution crystallographic analysis of a co-operative dimeric
RT hemoglobin.";
RL J. Mol. Biol. 235:657-681(1994).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANT LEU-97.
RX PubMed=9148933; DOI=10.1074/jbc.272.20.13171;
RA Pardanani A., Gibson Q.H., Colotti G., Royer W.E. Jr.;
RT "Mutation of residue Phe97 to Leu disrupts the central allosteric pathway
RT in Scapharca dimeric hemoglobin.";
RL J. Biol. Chem. 272:13171-13179(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH HEME, AND SUBUNIT.
RX PubMed=9826511; DOI=10.1006/jmbi.1998.2195;
RA Pardanani A., Gambacurta A., Ascoli F., Royer W.E. Jr.;
RT "Mutational destabilization of the critical interface water cluster in
RT scapharca dimeric hemoglobin: structural basis for altered allosteric
RT activity.";
RL J. Mol. Biol. 284:729-739(1998).
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9826511}.
CC -!- INTERACTION:
CC P02213; P02213: -; NbExp=2; IntAct=EBI-15582090, EBI-15582090;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; A02535; GGNKID.
DR PDB; 1HBI; X-ray; 1.70 A; A/B=1-146.
DR PDB; 1JWN; X-ray; 2.10 A; A/B/C/D=1-146.
DR PDB; 1JZK; X-ray; 2.20 A; A/B/C/D=1-146.
DR PDB; 1JZL; X-ray; 1.50 A; A/B=1-146.
DR PDB; 1JZM; X-ray; 1.90 A; A/B=1-146.
DR PDB; 1NWI; X-ray; 2.50 A; A/B/C/D=1-146.
DR PDB; 1NWN; X-ray; 2.80 A; A/B=1-146.
DR PDB; 1NXF; X-ray; 1.85 A; A/B=1-146.
DR PDB; 2AUO; X-ray; 1.53 A; A/B=1-146.
DR PDB; 2AUP; X-ray; 1.80 A; A/B=1-146.
DR PDB; 2AUQ; X-ray; 1.80 A; A/B=1-146.
DR PDB; 2AUR; X-ray; 2.30 A; A/B=1-146.
DR PDB; 2AV0; X-ray; 1.50 A; A/B=1-146.
DR PDB; 2AV3; X-ray; 1.70 A; A/B=1-146.
DR PDB; 2GRF; X-ray; 2.10 A; A/B=1-146.
DR PDB; 2GRH; X-ray; 1.50 A; A/B=1-146.
DR PDB; 2GRZ; X-ray; 1.60 A; A/B=1-146.
DR PDB; 2R4W; X-ray; 1.80 A; A/B=1-146.
DR PDB; 2R4X; X-ray; 2.10 A; A/B=1-146.
DR PDB; 2R4Y; X-ray; 2.00 A; A/B=1-146.
DR PDB; 2R4Z; X-ray; 1.60 A; A/B=1-146.
DR PDB; 2Z85; X-ray; 1.60 A; A/B=1-146.
DR PDB; 2Z8A; X-ray; 1.06 A; A/B=1-146.
DR PDB; 3G46; X-ray; 0.91 A; A/B=1-146.
DR PDB; 3G4Q; X-ray; 1.60 A; A/B=1-146.
DR PDB; 3G4R; X-ray; 1.60 A; A/B=1-146.
DR PDB; 3G4U; X-ray; 2.10 A; A/B=1-146.
DR PDB; 3G4V; X-ray; 2.10 A; A/B=1-146.
DR PDB; 3G4W; X-ray; 1.90 A; A/B=1-146.
DR PDB; 3G4Y; X-ray; 1.70 A; A/B=1-146.
DR PDB; 3G52; X-ray; 1.65 A; A/B=1-146.
DR PDB; 3G53; X-ray; 1.64 A; A/B=1-146.
DR PDB; 3QOB; X-ray; 1.60 A; A/B=1-146.
DR PDB; 3SDH; X-ray; 1.40 A; A/B=1-146.
DR PDB; 3UGY; X-ray; 2.10 A; A/B=1-146.
DR PDB; 3UGZ; X-ray; 1.65 A; A/B=1-146.
DR PDB; 3UH3; X-ray; 1.80 A; A/B=1-146.
DR PDB; 3UH5; X-ray; 2.10 A; A/B=1-146.
DR PDB; 3UH6; X-ray; 2.25 A; A/B=1-146.
DR PDB; 3UH7; X-ray; 1.80 A; A/B=1-146.
DR PDB; 3UHB; X-ray; 1.60 A; A/B=1-146.
DR PDB; 3UHC; X-ray; 1.60 A; A/B=1-146.
DR PDB; 3UHD; X-ray; 1.60 A; A/B=1-146.
DR PDB; 3UHE; X-ray; 2.60 A; A/B=1-146.
DR PDB; 3UHG; X-ray; 1.80 A; A/B=1-146.
DR PDB; 3UHH; X-ray; 1.50 A; A/B=1-146.
DR PDB; 3UHI; X-ray; 2.50 A; A/B/C/D=1-146.
DR PDB; 3UHK; X-ray; 2.00 A; A/B/C/D=1-146.
DR PDB; 3UHN; X-ray; 2.00 A; A/B=1-146.
DR PDB; 3UHQ; X-ray; 1.95 A; A/B=1-146.
DR PDB; 3UHR; X-ray; 1.90 A; A/B=1-146.
DR PDB; 3UHS; X-ray; 2.10 A; A/B=1-146.
DR PDB; 3UHT; X-ray; 2.00 A; A/B=1-146.
DR PDB; 3UHU; X-ray; 2.10 A; A/B=1-146.
DR PDB; 3UHV; X-ray; 1.75 A; A/B=1-146.
DR PDB; 3UHW; X-ray; 2.05 A; A/B=1-146.
DR PDB; 3UHX; X-ray; 1.70 A; A/B=1-146.
DR PDB; 3UHY; X-ray; 2.20 A; A/B=1-146.
DR PDB; 3UHZ; X-ray; 2.00 A; A/B=1-146.
DR PDB; 3UI0; X-ray; 1.80 A; A/B=1-146.
DR PDB; 4HBI; X-ray; 1.60 A; A/B=1-146.
DR PDB; 4SDH; X-ray; 1.60 A; A/B=1-146.
DR PDB; 5HBI; X-ray; 1.60 A; A/B=1-146.
DR PDB; 6HBI; X-ray; 1.80 A; A/B=1-146.
DR PDB; 7HBI; X-ray; 1.60 A; A/B=1-146.
DR PDBsum; 1HBI; -.
DR PDBsum; 1JWN; -.
DR PDBsum; 1JZK; -.
DR PDBsum; 1JZL; -.
DR PDBsum; 1JZM; -.
DR PDBsum; 1NWI; -.
DR PDBsum; 1NWN; -.
DR PDBsum; 1NXF; -.
DR PDBsum; 2AUO; -.
DR PDBsum; 2AUP; -.
DR PDBsum; 2AUQ; -.
DR PDBsum; 2AUR; -.
DR PDBsum; 2AV0; -.
DR PDBsum; 2AV3; -.
DR PDBsum; 2GRF; -.
DR PDBsum; 2GRH; -.
DR PDBsum; 2GRZ; -.
DR PDBsum; 2R4W; -.
DR PDBsum; 2R4X; -.
DR PDBsum; 2R4Y; -.
DR PDBsum; 2R4Z; -.
DR PDBsum; 2Z85; -.
DR PDBsum; 2Z8A; -.
DR PDBsum; 3G46; -.
DR PDBsum; 3G4Q; -.
DR PDBsum; 3G4R; -.
DR PDBsum; 3G4U; -.
DR PDBsum; 3G4V; -.
DR PDBsum; 3G4W; -.
DR PDBsum; 3G4Y; -.
DR PDBsum; 3G52; -.
DR PDBsum; 3G53; -.
DR PDBsum; 3QOB; -.
DR PDBsum; 3SDH; -.
DR PDBsum; 3UGY; -.
DR PDBsum; 3UGZ; -.
DR PDBsum; 3UH3; -.
DR PDBsum; 3UH5; -.
DR PDBsum; 3UH6; -.
DR PDBsum; 3UH7; -.
DR PDBsum; 3UHB; -.
DR PDBsum; 3UHC; -.
DR PDBsum; 3UHD; -.
DR PDBsum; 3UHE; -.
DR PDBsum; 3UHG; -.
DR PDBsum; 3UHH; -.
DR PDBsum; 3UHI; -.
DR PDBsum; 3UHK; -.
DR PDBsum; 3UHN; -.
DR PDBsum; 3UHQ; -.
DR PDBsum; 3UHR; -.
DR PDBsum; 3UHS; -.
DR PDBsum; 3UHT; -.
DR PDBsum; 3UHU; -.
DR PDBsum; 3UHV; -.
DR PDBsum; 3UHW; -.
DR PDBsum; 3UHX; -.
DR PDBsum; 3UHY; -.
DR PDBsum; 3UHZ; -.
DR PDBsum; 3UI0; -.
DR PDBsum; 4HBI; -.
DR PDBsum; 4SDH; -.
DR PDBsum; 5HBI; -.
DR PDBsum; 6HBI; -.
DR PDBsum; 7HBI; -.
DR AlphaFoldDB; P02213; -.
DR SMR; P02213; -.
DR DIP; DIP-60313N; -.
DR EvolutionaryTrace; P02213; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; Cytoplasm; Direct protein sequencing; Heme; Iron;
KW Metal-binding; Oxygen transport; Transport.
FT CHAIN 1..146
FT /note="Globin-1"
FT /id="PRO_0000052487"
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 HELIX 3..8
FT /evidence="ECO:0007829|PDB:3G46"
FT HELIX 12..25
FT /evidence="ECO:0007829|PDB:3G46"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:3G46"
FT HELIX 29..43
FT /evidence="ECO:0007829|PDB:3G46"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:3G46"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:3G46"
FT HELIX 64..82
FT /evidence="ECO:0007829|PDB:3G46"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:3G46"
FT HELIX 87..103
FT /evidence="ECO:0007829|PDB:3G46"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:3G46"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:3G46"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:3G46"
FT HELIX 129..145
FT /evidence="ECO:0007829|PDB:3G46"
SQ SEQUENCE 146 AA; 15946 MW; 6C55C768BA9FAA3A CRC64;
PSVYDAAAQL TADVKKDLRD SWKVIGSDKK GNGVALMTTL FADNQETIGY FKRLGDVSQG
MANDKLRGHS ITLMYALQNF IDQLDNPDDL VCVVEKFAVN HITRKISAAE FGKINGPIKK
VLASKNFGDK YANAWAKLVA VVQAAL
