GLB_ASCSU
ID GLB_ASCSU Reviewed; 338 AA.
AC P28316;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Extracellular globin;
DE Flags: Precursor;
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1465385; DOI=10.1073/pnas.89.24.11696;
RA Sherman D.R., Kloek A.P., Krishnan B.R., Guinn B., Goldberg D.E.;
RT "Ascaris hemoglobin gene: plant-like structure reflects the ancestral
RT globin gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:11696-11700(1992).
RN [2]
RP PROTEIN SEQUENCE OF 19-333.
RX PubMed=1584800; DOI=10.1073/pnas.89.10.4638;
RA de Baere I., Liu L., Moens L., van Beeumen J., Gielens C., Richelle J.,
RA Trotman C., Finch J., Gerstein M., Perutz M.;
RT "Polar zipper sequence in the high-affinity hemoglobin of Ascaris suum:
RT amino acid sequence and structural interpretation.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4638-4642(1992).
RN [3]
RP REVIEW.
RX PubMed=7748168; DOI=10.1002/bies.950170213;
RA Goldberg D.E.;
RT "The enigmatic oxygen-avid hemoglobin of Ascaris.";
RL Bioessays 17:177-182(1995).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 19-167.
RX PubMed=7753786; DOI=10.1073/pnas.92.10.4224;
RA Yang J., Kloek A.P., Goldberg D.E., Mathews F.S.;
RT "The structure of Ascaris hemoglobin domain I at 2.2-A resolution:
RT molecular features of oxygen avidity.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:4224-4228(1995).
CC -!- FUNCTION: Has an extremely high oxygen affinity. In a vacuum, it takes
CC several minutes to release its oxygen compared to milliseconds for a
CC normal globin. Could be used as an oxygen scavenger for sterol
CC biosynthesis.
CC -!- SUBUNIT: Homooctamer.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- DOMAIN: Consists of two tandemly linked globin-like sequences which
CC each bind a heme group and a C-terminal extension which may act as a
CC cement between the eight subunits.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; L03351; AAA29374.1; -; mRNA.
DR PIR; A47183; A47183.
DR PDB; 1ASH; X-ray; 2.15 A; A=18-167.
DR PDBsum; 1ASH; -.
DR AlphaFoldDB; P28316; -.
DR SMR; P28316; -.
DR iPTMnet; P28316; -.
DR EvolutionaryTrace; P28316; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
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 CDD; cd01040; Mb-like; 2.
DR Gene3D; 1.10.490.10; -; 2.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR044399; Mb-like_M.
DR Pfam; PF00042; Globin; 2.
DR SUPFAM; SSF46458; SSF46458; 2.
DR PROSITE; PS01033; GLOBIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycoprotein; Heme; Iron;
KW Metal-binding; Oxygen transport; Repeat; Secreted; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:1584800"
FT CHAIN 19..338
FT /note="Extracellular globin"
FT /id="PRO_0000011185"
FT REGION 19..162
FT /note="Globin-like 1"
FT REGION 163..312
FT /note="Globin-like 2"
FT REGION 313..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 82
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 BINDING 114
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 BINDING 231
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 BINDING 263
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 CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1584800"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1584800"
FT CONFLICT 117
FT /note="D -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 169..172
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="L -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:1ASH"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:1ASH"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1ASH"
FT HELIX 38..54
FT /evidence="ECO:0007829|PDB:1ASH"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:1ASH"
FT TURN 63..67
FT /evidence="ECO:0007829|PDB:1ASH"
FT HELIX 70..75
FT /evidence="ECO:0007829|PDB:1ASH"
FT HELIX 77..95
FT /evidence="ECO:0007829|PDB:1ASH"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:1ASH"
FT HELIX 100..116
FT /evidence="ECO:0007829|PDB:1ASH"
FT HELIX 123..140
FT /evidence="ECO:0007829|PDB:1ASH"
FT HELIX 145..162
FT /evidence="ECO:0007829|PDB:1ASH"
SQ SEQUENCE 338 AA; 40648 MW; DD362C1B49C06CA9 CRC64;
MRSLLLLSIV FFVVTVSANK TRELCMKSLE HAKVDTSNEA RQDGIDLYKH MFENYPPLRK
YFKNREEYTA EDVQNDPFFA KQGQKILLAC HVLCATYDDR ETFNAYTREL LDRHARDHVH
MPPEVWTDFW KLFEEYLGKK TTLDEPTKQA WHEIGREFAK EINKHGRHAV RHQCMRSLQH
IDIGHSETAK QNGIDLYKHM FENYPSMREA FKDRENYTAE DVQKDPFFVK QGQRILLACH
LLCASYDDEE TFHMYVHELM ERHERLGVQL PDQHWTDFWK LFEEFLEKKS HLCEHTKHAW
AVIGKEFAYE ATRHGKEHHE HKEEHKEEHK EEHKEEQH
