GLB2_ASCSU
ID GLB2_ASCSU Reviewed; 153 AA.
AC P49672;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Myoglobin;
DE AltName: Full=Globin, body wall isoform;
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], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Body wall muscle;
RX PubMed=7982924; DOI=10.1016/s0021-9258(18)43794-5;
RA Blaxter M.L., Vanfleteren J.R., Xia J., Moens L.;
RT "Structural characterization of an Ascaris myoglobin.";
RL J. Biol. Chem. 269:30181-30186(1994).
CC -!- FUNCTION: High oxygen affinity. Probably supplies oxygen needed for
CC muscle activity.
CC -!- SUBUNIT: Homodimer; disulfide-linked.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Body wall globin is localized in cellular
CC compartments belonging to the hypodermis, the dorsal, ventral and
CC lateral cords, the nerve ring, and body wall muscle.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; U17337; AAA64695.1; -; mRNA.
DR PIR; A55139; A55139.
DR AlphaFoldDB; P49672; -.
DR SMR; P49672; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IPR012085; Globin_nematode.
DR InterPro; IPR044399; Mb-like_M.
DR Pfam; PF00042; Globin; 1.
DR PIRSF; PIRSF002026; Nematode_globin; 1.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Disulfide bond; Heme; Iron;
KW Metal-binding; Oxygen transport; Transport.
FT CHAIN 1..153
FT /note="Myoglobin"
FT /id="PRO_0000052460"
FT BINDING 94
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"
SQ SEQUENCE 153 AA; 17454 MW; 1B3EF94A15B49B98 CRC64;
MATACVKSLE SVQCGTCEKT IANGTEFYAL LFDKHPDLRH YFKGNENLTG ADVKKSDHFK
KQGQRLLLAC HVLAHLENDP ASFKAYAREI VDPHLRMSVH LEPKLWSEFW PIWLDYLSTK
ESVDDATKNA WLALGKKFSD ECLDHLKNLG QPH