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Extracellular globin

 GLB_ASCSU               Reviewed;         338 AA.
P28316;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 2.
25-OCT-2017, entry version 95.
RecName: Full=Extracellular globin;
Flags: Precursor;
Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Ascaridida;
Ascaridoidea; Ascarididae; Ascaris.
NCBI_TaxID=6253;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1465385; DOI=10.1073/pnas.89.24.11696;
Sherman D.R., Kloek A.P., Krishnan B.R., Guinn B., Goldberg D.E.;
"Ascaris hemoglobin gene: plant-like structure reflects the ancestral
globin gene.";
Proc. Natl. Acad. Sci. U.S.A. 89:11696-11700(1992).
[2]
PROTEIN SEQUENCE OF 19-333.
PubMed=1584800; DOI=10.1073/pnas.89.10.4638;
de Baere I., Liu L., Moens L., van Beeumen J., Gielens C.,
Richelle J., Trotman C., Finch J., Gerstein M., Perutz M.;
"Polar zipper sequence in the high-affinity hemoglobin of Ascaris
suum: amino acid sequence and structural interpretation.";
Proc. Natl. Acad. Sci. U.S.A. 89:4638-4642(1992).
[3]
REVIEW.
PubMed=7748168; DOI=10.1002/bies.950170213;
Goldberg D.E.;
"The enigmatic oxygen-avid hemoglobin of Ascaris.";
Bioessays 17:177-182(1995).
[4]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 19-167.
PubMed=7753786; DOI=10.1073/pnas.92.10.4224;
Yang J., Kloek A.P., Goldberg D.E., Mathews F.S.;
"The structure of Ascaris hemoglobin domain I at 2.2-A resolution:
molecular features of oxygen avidity.";
Proc. Natl. Acad. Sci. U.S.A. 92:4224-4228(1995).
-!- FUNCTION: Has an extremely high oxygen affinity. In a vacuum, it
takes several minutes to release its oxygen compared to
milliseconds for a normal globin. Could be used as an oxygen
scavenger for sterol biosynthesis.
-!- SUBUNIT: Homooctamer.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space.
-!- DOMAIN: Consists of two tandemly linked globin-like sequences
which each bind a heme group and a C-terminal extension which may
act as a cement between the eight subunits.
-!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
ProRule:PRU00238}.
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EMBL; L03351; AAA29374.1; -; mRNA.
PIR; A47183; A47183.
PDB; 1ASH; X-ray; 2.15 A; A=18-167.
PDBsum; 1ASH; -.
ProteinModelPortal; P28316; -.
SMR; P28316; -.
iPTMnet; P28316; -.
EvolutionaryTrace; P28316; -.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-KW.
InterPro; IPR000971; Globin.
InterPro; IPR009050; Globin-like.
Pfam; PF00042; Globin; 2.
SUPFAM; SSF46458; SSF46458; 2.
PROSITE; PS01033; GLOBIN; 2.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Glycoprotein; Heme; Iron;
Metal-binding; Oxygen transport; Repeat; Secreted; Signal; Transport.
SIGNAL 1 18 {ECO:0000269|PubMed:1584800}.
CHAIN 19 338 Extracellular globin.
/FTId=PRO_0000011185.
REGION 19 162 Globin-like 1.
REGION 163 312 Globin-like 2.
COMPBIAS 313 338 Asp/Glu/His/Lys-rich.
METAL 82 82 Iron (heme distal ligand).
METAL 114 114 Iron (heme proximal ligand).
METAL 231 231 Iron (heme distal ligand).
METAL 263 263 Iron (heme proximal ligand).
CARBOHYD 19 19 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:1584800}.
CARBOHYD 216 216 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:1584800}.
CONFLICT 117 117 D -> L (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 169 172 Missing (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 266 266 L -> D (in Ref. 2; AA sequence).
{ECO:0000305}.
HELIX 19 28 {ECO:0000244|PDB:1ASH}.
HELIX 29 31 {ECO:0000244|PDB:1ASH}.
STRAND 35 37 {ECO:0000244|PDB:1ASH}.
HELIX 38 54 {ECO:0000244|PDB:1ASH}.
HELIX 56 61 {ECO:0000244|PDB:1ASH}.
TURN 63 67 {ECO:0000244|PDB:1ASH}.
HELIX 70 75 {ECO:0000244|PDB:1ASH}.
HELIX 77 95 {ECO:0000244|PDB:1ASH}.
TURN 96 98 {ECO:0000244|PDB:1ASH}.
HELIX 100 116 {ECO:0000244|PDB:1ASH}.
HELIX 123 140 {ECO:0000244|PDB:1ASH}.
HELIX 145 162 {ECO:0000244|PDB:1ASH}.
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


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