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 27-MAR-2024, entry version 132. 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}. 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; 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 STRING; 7757.ENSPMAP00000005891; -. DR Ensembl; ENSPMAT00000005918.1; ENSPMAP00000005891.1; ENSPMAG00000005343.1. DR Ensembl; ENSPMAT00000005931.1; ENSPMAP00000005904.1; ENSPMAG00000005354.1. DR GeneTree; ENSGT00940000155004; -. DR HOGENOM; CLU_003827_10_1_1; -. DR OMA; IRETWRE; -. DR OrthoDB; 4233999at2759; -. 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; Globins; 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; CYTOGLOBIN; 1. DR PANTHER; PTHR46783:SF2; CYTOGLOBIN-1-RELATED; 1. DR Pfam; PF00042; Globin; 1. DR PRINTS; PR01906; FISHGLOBIN. DR SUPFAM; SSF46458; Globin-like; 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 //