GLB5_PETMA
ID GLB5_PETMA Reviewed; 150 AA.
AC P02208;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Globin-5;
DE AltName: Full=Hemoglobin V;
OS Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757;
RN [1]
RP PROTEIN SEQUENCE OF 2-150.
RX PubMed=6409159; DOI=10.1016/s0300-9084(83)80276-4;
RA Hombrados I., Rodewald K., Neuzil E., Braunitzer G.;
RT "Haemoglobins, LX. Primary structure of the major haemoglobin of the sea
RT lamprey Petromyzon marinus (var. Garonne, Loire).";
RL Biochimie 65:247-257(1983).
RN [2]
RP PROTEIN SEQUENCE OF 2-150.
RX PubMed=5484471; DOI=10.1016/s0021-9258(18)62673-0;
RA Li S.L., Riggs A.;
RT "The amino acid sequence of hemoglobin V from the lamprey, Petromyzon
RT marinus.";
RL J. Biol. Chem. 245:6149-6169(1970).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=4692855; DOI=10.1016/0022-2836(73)90377-x;
RA Hendrickson W.A., Love W.E., Karle J.;
RT "Crystal structure analysis of sea lamprey hemoglobin at 2-A resolution.";
RL J. Mol. Biol. 74:331-361(1973).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=4032476; DOI=10.1016/0022-2836(85)90049-x;
RA Honzatko R.B., Hendrickson W.A., Love W.E.;
RT "Refinement of a molecular model for lamprey hemoglobin from Petromyzon
RT marinus.";
RL J. Mol. Biol. 184:147-164(1985).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=10378271; DOI=10.1016/s0969-2126(99)80068-9;
RA Heaslet H.A., Royer W.E. Jr.;
RT "The 2.7-A crystal structure of deoxygenated hemoglobin from the sea
RT lamprey (Petromyzon marinus): structural basis for a lowered oxygen
RT affinity and Bohr effect.";
RL Structure 7:517-526(1999).
CC -!- SUBUNIT: Monomer at high oxygen tension and high pH and dimeric at low
CC oxygen tension and lower pH.
CC -!- MISCELLANEOUS: Globin V is the major component of the 6 globins found
CC in the Sea lamprey.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; A90676; GGLMS.
DR PDB; 1F5O; X-ray; 2.90 A; A/B/C/D/E/F=2-150.
DR PDB; 1F5P; X-ray; 2.90 A; A/B/C/D/E/F=2-150.
DR PDB; 2LHB; X-ray; 2.00 A; A=2-150.
DR PDB; 3LHB; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=2-150.
DR PDBsum; 1F5O; -.
DR PDBsum; 1F5P; -.
DR PDBsum; 2LHB; -.
DR PDBsum; 3LHB; -.
DR AlphaFoldDB; P02208; -.
DR SMR; P02208; -.
DR Ensembl; ENSPMAT00000005918; ENSPMAP00000005891; ENSPMAG00000005343.
DR Ensembl; ENSPMAT00000005931; ENSPMAP00000005904; ENSPMAG00000005354.
DR GeneTree; ENSGT00940000155004; -.
DR HOGENOM; CLU_003827_10_1_1; -.
DR OMA; IRETWRE; -.
DR TreeFam; TF332967; -.
DR EvolutionaryTrace; P02208; -.
DR Proteomes; UP000245300; Unplaced.
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 Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR013314; Globin_lamprey/hagfish.
DR PANTHER; PTHR46783; PTHR46783; 1.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR01906; FISHGLOBIN.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxygen transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..150
FT /note="Globin-5"
FT /id="PRO_0000052529"
FT BINDING 74
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="distal binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00238,
FT ECO:0000269|PubMed:4032476"
FT BINDING 106
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00238,
FT ECO:0000269|PubMed:4032476"
FT VARIANT 30
FT /note="T -> N"
FT CONFLICT 96
FT /note="S -> SS (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 99..100
FT /note="Missing (in Ref. 2; AA sequence and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="M -> R (in Ref. 2; AA sequence and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 14..29
FT /evidence="ECO:0007829|PDB:3LHB"
FT HELIX 31..45
FT /evidence="ECO:0007829|PDB:3LHB"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:3LHB"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:3LHB"
FT HELIX 62..67
FT /evidence="ECO:0007829|PDB:3LHB"
FT HELIX 69..87
FT /evidence="ECO:0007829|PDB:3LHB"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:3LHB"
FT HELIX 92..108
FT /evidence="ECO:0007829|PDB:3LHB"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3LHB"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:3LHB"
FT HELIX 133..147
FT /evidence="ECO:0007829|PDB:3LHB"
SQ SEQUENCE 150 AA; 16401 MW; 39BE05B24670A88A CRC64;
MPIVDTGSVA PLSAAEKTKI RSAWAPVYST YETSGVDILV KFFTSTPAAQ EFFPKFKGLT
TADQLKKSAD VRWHAERIIN AVNDAVASMD DTEKMSMKLR DLSGKHAKSF QVDPQYFKVL
AAVIADTVAA GDAGFEKLMS MICILLRSAY
