GLB2_PHAPT
ID GLB2_PHAPT Reviewed; 151 AA.
AC P41261;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Hemoglobin-2;
DE AltName: Full=Hemoglobin II;
DE Short=Hb II;
DE Short=HbII;
OS Phacoides pectinatus (Thick lucine) (Lucina pectinata).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Heteroconchia; Euheterodonta; Imparidentia; Lucinida;
OC Lucinoidea; Lucinidae; Phacoides.
OX NCBI_TaxID=244486;
RN [1]
RP PROTEIN SEQUENCE OF 2-151, AND ACETYLATION AT THR-2.
RC TISSUE=Gill;
RX PubMed=1815587; DOI=10.1007/bf01025713;
RA Hockenhull-Johnson J.D., Stern M.S., Martin P., Dass C., Desiderio D.M.,
RA Wittenberg J.B., Vinogradov S.N., Walz D.A.;
RT "The amino acid sequence of hemoglobin II from the symbiont-harboring clam
RT Lucina pectinata.";
RL J. Protein Chem. 10:609-622(1991).
RN [2]
RP CHARACTERIZATION.
RX PubMed=2398044; DOI=10.1016/s0021-9258(17)46185-0;
RA Kraus D.W., Wittenberg J.B.;
RT "Hemoglobins of the Lucina pectinata/bacteria symbiosis. I. Molecular
RT properties, kinetics and equilibria of reactions with ligands.";
RL J. Biol. Chem. 265:16043-16053(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH HEME.
RX PubMed=18203714; DOI=10.1074/jbc.m705026200;
RA Gavira J.A., Camara-Artigas A., De Jesus-Bonilla W., Lopez-Garriga J.,
RA Lewis A., Pietri R., Yeh S.R., Cadilla C.L., Garcia-Ruiz J.M.;
RT "Structure and ligand selection of hemoglobin II from Lucina pectinata.";
RL J. Biol. Chem. 283:9414-9423(2008).
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:18203714}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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 PIR; A61437; A61437.
DR PDB; 2OLP; X-ray; 1.93 A; A/B=2-151.
DR PDB; 3PI1; X-ray; 2.00 A; A/B=2-151.
DR PDB; 3PI2; X-ray; 1.85 A; A/B=2-151.
DR PDB; 3PI3; X-ray; 1.95 A; A/B=2-151.
DR PDB; 3PI4; X-ray; 3.17 A; A/B=2-151.
DR PDB; 3PT7; X-ray; 2.15 A; A=2-151.
DR PDB; 3PT8; X-ray; 1.76 A; A=2-151.
DR PDB; 6OTW; X-ray; 2.45 A; A=1-151.
DR PDB; 6OTX; X-ray; 2.54 A; A=1-151.
DR PDB; 6OTY; X-ray; 2.60 A; A=1-151.
DR PDBsum; 2OLP; -.
DR PDBsum; 3PI1; -.
DR PDBsum; 3PI2; -.
DR PDBsum; 3PI3; -.
DR PDBsum; 3PI4; -.
DR PDBsum; 3PT7; -.
DR PDBsum; 3PT8; -.
DR PDBsum; 6OTW; -.
DR PDBsum; 6OTX; -.
DR PDBsum; 6OTY; -.
DR AlphaFoldDB; P41261; -.
DR SMR; P41261; -.
DR iPTMnet; P41261; -.
DR EvolutionaryTrace; P41261; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
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; Acetylation; Cytoplasm; Direct protein sequencing; Heme;
KW Iron; Metal-binding; Oxygen transport; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1815587"
FT CHAIN 2..151
FT /note="Hemoglobin-2"
FT /id="PRO_0000052493"
FT BINDING 97
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-acetylthreonine"
FT /evidence="ECO:0000269|PubMed:1815587"
FT HELIX 6..20
FT /evidence="ECO:0007829|PDB:3PT8"
FT HELIX 23..37
FT /evidence="ECO:0007829|PDB:3PT8"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:3PT8"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:3PT8"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:3PT8"
FT HELIX 61..78
FT /evidence="ECO:0007829|PDB:3PT8"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:3PT8"
FT HELIX 84..98
FT /evidence="ECO:0007829|PDB:3PT8"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:3PT8"
FT HELIX 104..120
FT /evidence="ECO:0007829|PDB:3PT8"
FT HELIX 128..149
FT /evidence="ECO:0007829|PDB:3PT8"
SQ SEQUENCE 151 AA; 17011 MW; 5A6A5430EE54D733 CRC64;
MTTLTNPQKA AIRSSWSKFM DNGVSNGQGF YMDLFKAHPE TLTPFKSLFG GLTLAQLQDN
PKMKAQSLVF CNGMSSFVDH LDDNMLVVLI QKMAKLHNNR GIRASDLRTA YDILIHYMED
HNHMVGGAKD AWEVFVGFIC KTLGDYMKEL S
