GLBB1_OLIMA
ID GLBB1_OLIMA Reviewed; 161 AA.
AC Q5KSB7;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Extracellular giant hemoglobin major globin subunit B1;
DE AltName: Full=Major globin chain d;
DE Flags: Precursor;
GN Name=ghbB1;
OS Oligobrachia mashikoi (Beard worm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC Sedentaria; Canalipalpata; Sabellida; Siboglinidae; Oligobrachia.
OX NCBI_TaxID=55676;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 17-36.
RX PubMed=15795490; DOI=10.2108/zsj.22.283;
RA Nakagawa T., Onoda S., Kanemori M., Sasayama Y., Fukumori Y.;
RT "Purification, characterization and sequence analyses of the extracellular
RT giant hemoglobin from Oligobrachia mashikoi.";
RL Zool. Sci. 22:283-291(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 17-161, SUBUNIT, METAL, AND
RP DISULFIDE BONDS.
RX PubMed=16204001; DOI=10.1073/pnas.0501541102;
RA Numoto N., Nakagawa T., Kita A., Sasayama Y., Fukumori Y., Miki K.;
RT "Structure of an extracellular giant hemoglobin of the gutless beard worm
RT Oligobrachia mashikoi.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:14521-14526(2005).
CC -!- FUNCTION: The extracellular giant hemoglobin is able to bind and
CC transport oxygen and sulfide simultaneously and reversibly at two
CC different sites.
CC -!- SUBUNIT: The 400 kDa hemoglobin consists of a spherical 24-mer arranged
CC as a double layer of dome-shaped dodecamers. Each dodecamer is composed
CC of the 3-fold trimer of the tetramer A1-A2-B1-B2 having one intra-
CC tetramer (A1-B2) disulfide bond and one inter-tetramer (B1-B2)
CC disulfide bond per tetramer. {ECO:0000269|PubMed:16204001}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; AB185394; BAD86545.1; -; mRNA.
DR PDB; 2D2M; X-ray; 2.85 A; D=17-161.
DR PDB; 2D2N; X-ray; 3.20 A; D=17-161.
DR PDB; 2ZFO; X-ray; 1.95 A; D=17-161.
DR PDB; 2ZS0; X-ray; 1.60 A; D=17-161.
DR PDB; 2ZS1; X-ray; 1.70 A; D=17-161.
DR PDBsum; 2D2M; -.
DR PDBsum; 2D2N; -.
DR PDBsum; 2ZFO; -.
DR PDBsum; 2ZS0; -.
DR PDBsum; 2ZS1; -.
DR AlphaFoldDB; Q5KSB7; -.
DR SMR; Q5KSB7; -.
DR EvolutionaryTrace; Q5KSB7; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
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 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; IPR014610; Haemoglobin_extracell.
DR InterPro; IPR044399; Mb-like_M.
DR Pfam; PF00042; Globin; 1.
DR PIRSF; PIRSF036517; Ext_hemo; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Heme; Iron;
KW Metal-binding; Oxygen transport; Secreted; Signal; Transport.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:15795490"
FT CHAIN 17..161
FT /note="Extracellular giant hemoglobin major globin subunit
FT B1"
FT /id="PRO_5000051511"
FT BINDING 112
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 DISULFID 18
FT /note="Interchain (with C-19 in subunit B2)"
FT /evidence="ECO:0000269|PubMed:16204001"
FT DISULFID 19..149
FT /evidence="ECO:0000269|PubMed:16204001"
FT CONFLICT 27
FT /note="V -> K (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 21..34
FT /evidence="ECO:0007829|PDB:2D2M"
FT TURN 37..42
FT /evidence="ECO:0007829|PDB:2D2M"
FT HELIX 44..59
FT /evidence="ECO:0007829|PDB:2D2M"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:2D2N"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:2D2M"
FT HELIX 75..92
FT /evidence="ECO:0007829|PDB:2D2M"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:2D2M"
FT HELIX 98..113
FT /evidence="ECO:0007829|PDB:2D2M"
FT HELIX 120..137
FT /evidence="ECO:0007829|PDB:2D2M"
FT HELIX 143..157
FT /evidence="ECO:0007829|PDB:2D2M"
SQ SEQUENCE 161 AA; 16384 MW; C0451ED6BE5D2DA0 CRC64;
MTILVLFLSC AALASAECCS RGDAEVVISE WDQVFNAAMA GSSESAVGVA IFDAFFASSG
VSPSMFPGGG DSNNPEFLAQ VSRVVSGADI AINSLTNRAT CDSLLSHLNA QHRAISGVTG
AAVTHLSQAI SSVVAQVLPS AHIDAWEYCM AYIAAGIGAG L
