GLBA2_OLIMA
ID GLBA2_OLIMA Reviewed; 158 AA.
AC Q7M413; Q5KSC0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Extracellular giant hemoglobin major globin subunit A2;
DE AltName: Full=Major globin chain a5;
DE Flags: Precursor;
GN Name=ghbA2;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 37-158, PROTEIN SEQUENCE OF 17-44, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=8814231; DOI=10.1016/0167-4838(96)00081-7;
RA Yuasa H.J., Green B.N., Takagi T., Suzuki N., Vinogradov S.N., Suzuki T.;
RT "Electrospray ionization mass spectrometric composition of the 400 kDa
RT hemoglobin from the pogonophoran Oligobrachia mashikoi and the primary
RT structures of three major globin chains.";
RL Biochim. Biophys. Acta 1296:235-244(1996).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 17-158, 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 hydrosulfide 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; AB185391; BAD86542.1; -; mRNA.
DR PIR; S72251; S72251.
DR PDB; 2D2M; X-ray; 2.85 A; B=17-158.
DR PDB; 2D2N; X-ray; 3.20 A; B=17-158.
DR PDB; 2ZFO; X-ray; 1.95 A; B=17-158.
DR PDB; 2ZS0; X-ray; 1.60 A; B=17-158.
DR PDB; 2ZS1; X-ray; 1.70 A; B=17-158.
DR PDB; 7E96; X-ray; 2.40 A; B=17-158.
DR PDB; 7E97; X-ray; 2.70 A; B=17-158.
DR PDB; 7E98; X-ray; 2.20 A; B=17-158.
DR PDB; 7E99; X-ray; 2.10 A; B=17-158.
DR PDBsum; 2D2M; -.
DR PDBsum; 2D2N; -.
DR PDBsum; 2ZFO; -.
DR PDBsum; 2ZS0; -.
DR PDBsum; 2ZS1; -.
DR PDBsum; 7E96; -.
DR PDBsum; 7E97; -.
DR PDBsum; 7E98; -.
DR PDBsum; 7E99; -.
DR AlphaFoldDB; Q7M413; -.
DR SMR; Q7M413; -.
DR EvolutionaryTrace; Q7M413; -.
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; IPR002336; Erythrocruorin.
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 PRINTS; PR00611; ERYTHCRUORIN.
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 ECO:0000269|PubMed:8814231"
FT CHAIN 17..158
FT /note="Extracellular giant hemoglobin major globin subunit
FT A2"
FT /id="PRO_0000052517"
FT BINDING 89
FT /ligand="hydrogen sulfide"
FT /ligand_id="ChEBI:CHEBI:29919"
FT /evidence="ECO:0000305"
FT BINDING 110
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..148
FT /evidence="ECO:0000269|PubMed:16204001"
FT CONFLICT 39
FT /note="N -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:7E99"
FT HELIX 39..54
FT /evidence="ECO:0007829|PDB:7E99"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:7E99"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:7E99"
FT HELIX 73..91
FT /evidence="ECO:0007829|PDB:7E99"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:7E99"
FT HELIX 96..110
FT /evidence="ECO:0007829|PDB:7E99"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:7E99"
FT HELIX 119..135
FT /evidence="ECO:0007829|PDB:7E99"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:7E96"
FT HELIX 142..156
FT /evidence="ECO:0007829|PDB:7E99"
SQ SEQUENCE 158 AA; 16966 MW; 68F104F295746358 CRC64;
MKSLIVFACL VAYAAADCTS LNRLLVKRQW AEAYGEGTNR ELLGNRIWED LFANMPDARG
LFSRVNGNDI DSSEFQAHSL RVLGGLDMCV ASLDDVPVLN ALLARLNSQH DSRGIPAAGY
PAFVASAISA VRATVGARSF DNDAWNSCMN QIVSGISG
