TRHBN_PARCA
ID TRHBN_PARCA Reviewed; 117 AA.
AC P15160;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Group 1 truncated hemoglobin trHbN;
DE Short=PtrHb;
DE Short=Truncated Hb;
DE AltName: Full=Hemoglobin;
DE AltName: Full=Myoglobin;
OS Paramecium caudatum.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5885;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1731779; DOI=10.1016/s0006-291x(05)80130-5;
RA Yamauchi K., Mukai M., Ochiai T., Usuki I.;
RT "Molecular cloning of the cDNA for the major hemoglobin component from
RT Paramecium caudatum.";
RL Biochem. Biophys. Res. Commun. 182:195-200(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1420365; DOI=10.1016/0167-4781(92)90142-m;
RA Yamauchi K., Ochiai T., Usuki I.;
RT "The unique structure of the Paramecium caudatum hemoglobin gene: the
RT presence of one intron in the middle of the coding region.";
RL Biochim. Biophys. Acta 1171:81-87(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8482540; DOI=10.1016/0378-1119(93)90373-b;
RA Yamauchi K., Tada H., Ochiai T., Usuki I.;
RT "Structure of the Paramecium caudatum gene encoding the B-type of the major
RT hemoglobin component.";
RL Gene 126:243-246(1993).
RN [4]
RP PROTEIN SEQUENCE OF 2-117, AND ACETYLATION AT SER-2.
RX PubMed=2769763; DOI=10.1016/0022-2836(89)90395-1;
RA Iwaasa H., Takagi T., Shikama K.;
RT "Protozoan myoglobin from Paramecium caudatum. Its unusual amino acid
RT sequence.";
RL J. Mol. Biol. 208:355-358(1989).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 2-116 IN THE AQUO-MET FORM, AND
RP SUBUNIT.
RX PubMed=10835341; DOI=10.1093/emboj/19.11.2424;
RA Pesce A., Couture M., Dewilde S., Guertin M., Yamauchi K., Ascenzi P.,
RA Moens L., Bolognesi M.;
RT "A novel two-over-two alpha-helical sandwich fold is characteristic of the
RT truncated hemoglobin family.";
RL EMBO J. 19:2424-2434(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2-116, AND SUBUNIT.
RX PubMed=15016811; DOI=10.1074/jbc.m401320200;
RA Milani M., Pesce A., Ouellet Y., Dewilde S., Friedman J., Ascenzi P.,
RA Guertin M., Bolognesi M.;
RT "Heme-ligand tunneling in group I truncated hemoglobins.";
RL J. Biol. Chem. 279:21520-21525(2004).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=Binds 1 heme group per subunit.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10835341,
CC ECO:0000269|PubMed:15016811}.
CC -!- SIMILARITY: Belongs to the truncated hemoglobin family. Group I
CC subfamily. {ECO:0000305}.
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DR EMBL; S49254; AAB24268.2; -; Genomic_DNA.
DR EMBL; M99047; AAA29447.2; -; Genomic_DNA.
DR EMBL; M57542; AAA29446.2; -; mRNA.
DR EMBL; D12916; BAA02300.1; -; Genomic_DNA.
DR PIR; S27185; S27185.
DR PDB; 1DLW; X-ray; 1.54 A; A=2-117.
DR PDB; 1UVY; X-ray; 2.40 A; A=2-117.
DR PDBsum; 1DLW; -.
DR PDBsum; 1UVY; -.
DR AlphaFoldDB; P15160; -.
DR SMR; P15160; -.
DR iPTMnet; P15160; -.
DR EvolutionaryTrace; P15160; -.
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 Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR019795; Globin_bac-like_CS.
DR InterPro; IPR001486; Hemoglobin_trunc.
DR InterPro; IPR016339; Hemoglobin_trunc_I.
DR Pfam; PF01152; Bac_globin; 1.
DR PIRSF; PIRSF002030; Globin_Protozoa/Cyanobacteria; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01213; GLOBIN_FAM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Heme; Iron;
KW Metal-binding; Oxygen transport; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2769763"
FT CHAIN 2..117
FT /note="Group 1 truncated hemoglobin trHbN"
FT /id="PRO_0000162648"
FT BINDING 21
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="distal binding residue"
FT BINDING 69
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:2769763"
FT CONFLICT 18
FT /note="A -> D (in Ref. 2; AAA29446)"
FT /evidence="ECO:0000305"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:1DLW"
FT HELIX 10..25
FT /evidence="ECO:0007829|PDB:1DLW"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:1DLW"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:1DLW"
FT HELIX 39..53
FT /evidence="ECO:0007829|PDB:1DLW"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:1DLW"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1UVY"
FT HELIX 76..92
FT /evidence="ECO:0007829|PDB:1DLW"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:1DLW"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:1DLW"
SQ SEQUENCE 117 AA; 12039 MW; 5B46E33165D0A338 CRC64;
MSLFEQLGGQ AAVQAVTAQF YANIQADATV ATFFNGIDMP NQTNKTAAFL CAALGGPNAW
TGRNLKEVHA NMGVSNAQFT TVIGHLRSAL TGAGVAAALV EQTVAVAETV RGDVVTV
