ID   GLB3_PHAPT              Reviewed;         153 AA.
AC   P41262;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Hemoglobin-3;
DE   AltName: Full=Hemoglobin III;
DE            Short=Hb III;
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 2-153, AND ACETYLATION AT SER-2.
RC   TISSUE=Gill;
RX   PubMed=8397786; DOI=10.1007/bf01028189;
RA   Hockenhull-Johnson J.D., Stern M.S., Wittenberg J.B., Vinogradov S.N.,
RA   Kapp O.H., Walz D.A.;
RT   "The amino acid sequence of hemoglobin III from the symbiont-harboring clam
RT   Lucina pectinata.";
RL   J. Protein Chem. 12:261-277(1993).
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}.
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; A53873; A53873.
DR   PDB; 3PT7; X-ray; 2.15 A; B=2-153.
DR   PDB; 3PT8; X-ray; 1.76 A; B=2-153.
DR   PDB; 6OTW; X-ray; 2.45 A; B=2-153.
DR   PDB; 6OTX; X-ray; 2.54 A; B=2-153.
DR   PDB; 6OTY; X-ray; 2.60 A; B=2-153.
DR   PDBsum; 3PT7; -.
DR   PDBsum; 3PT8; -.
DR   PDBsum; 6OTW; -.
DR   PDBsum; 6OTX; -.
DR   PDBsum; 6OTY; -.
DR   AlphaFoldDB; P41262; -.
DR   SMR; P41262; -.
DR   iPTMnet; P41262; -.
DR   PRIDE; P41262; -.
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:8397786"
FT   CHAIN           2..153
FT                   /note="Hemoglobin-3"
FT                   /id="PRO_0000052494"
FT   BINDING         99
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-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:8397786"
FT   HELIX           7..21
FT                   /evidence="ECO:0007829|PDB:3PT8"
FT   HELIX           24..38
FT                   /evidence="ECO:0007829|PDB:3PT8"
FT   HELIX           40..46
FT                   /evidence="ECO:0007829|PDB:3PT8"
FT   TURN            47..52
FT                   /evidence="ECO:0007829|PDB:3PT8"
FT   HELIX           55..58
FT                   /evidence="ECO:0007829|PDB:3PT8"
FT   HELIX           62..79
FT                   /evidence="ECO:0007829|PDB:3PT8"
FT   TURN            80..83
FT                   /evidence="ECO:0007829|PDB:3PT8"
FT   HELIX           85..100
FT                   /evidence="ECO:0007829|PDB:3PT8"
FT   TURN            101..103
FT                   /evidence="ECO:0007829|PDB:3PT8"
FT   HELIX           106..122
FT                   /evidence="ECO:0007829|PDB:3PT8"
FT   HELIX           128..150
FT                   /evidence="ECO:0007829|PDB:3PT8"
SQ   SEQUENCE   153 AA;  17560 MW;  0105926F45F19E26 CRC64;
     MSSGLTGPQK AALKSSWSRF MDNAVTNGTN FYMDLFKAYP DTLTPFKSLF EDVSFNQMTD
     HPTMKAQALV FCDGMSSFVD NLDDHEVLVV LLQKMAKLHF NRGIRIKELR DGYGVLLRYL
     EDHCHVEGST KNAWEDFIAY ICRVQGDFMK ERL