GLB_PSEDC
ID GLB_PSEDC Reviewed; 333 AA.
AC P26914;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Extracellular globin;
DE Flags: Precursor;
OS Pseudoterranova decipiens (Sealworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Pseudoterranova.
OX NCBI_TaxID=6271;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Larva;
RX PubMed=2062843; DOI=10.1073/pnas.88.13.5655;
RA Dixon B., Walker B., Kimmins W., Pohajdak B.;
RT "Isolation and sequencing of a cDNA for an unusual hemoglobin from the
RT parasitic nematode Pseudoterranova decipiens.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:5655-5659(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1501253; DOI=10.1007/bf00183224;
RA Dixon B., Walker B., Kimmins W., Pohajdak B.;
RT "A nematode hemoglobin gene contains an intron previously thought to be
RT unique to plants.";
RL J. Mol. Evol. 35:131-136(1992).
CC -!- SUBUNIT: Homooctamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- DOMAIN: Consist of two tandemly linked globin-like sequences which
CC probably each bind a heme group and a C-terminal extension which may
CC act as a cement between the eight subunits.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; M63298; AAA29797.1; -; mRNA.
DR EMBL; Z11681; CAA77743.1; -; Genomic_DNA.
DR PIR; S24615; A41099.
DR AlphaFoldDB; P26914; -.
DR SMR; P26914; -.
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; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Heme; Iron; Metal-binding; Oxygen transport; Repeat;
KW Secreted; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..333
FT /note="Extracellular globin"
FT /id="PRO_0000011184"
FT REGION 19..162
FT /note="Globin-like 1"
FT REGION 163..310
FT /note="Globin-like 2"
FT REGION 314..333
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 9
FT /note="I -> T (in Ref. 2; CAA77743)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 39452 MW; ABF6F9ADBA111A47 CRC64;
MHSSIVLAIV LFVAIASASK TRELCMKSLE HAKVGTSKEA KQDGIDLYKH MFEHYPAMKK
YFKHRENYTP ADVQKDPFFI KQGQNILLAC HVLCATYDDR ETFDAYVGEL MARHERDHVK
IPNDVWNHFW EHFIEFLGSK TTLDEPTKHA WQEIGKEFSH EISHHGRHSV RDHCMNSLEY
IAIGDKEHQK QNGIDLYKHM FEHYPHMRKA FKGRENFTKE DVQKDAFFVK QGHKILLALR
MLCSSYDDEP TFDYFVDALM DRHIKDDIHL PQEQWHEFWK LFAEYLNEKS HQHLTEAEKH
AWSTIGEDFA HEADKHAKAE KDHHEGEHKE EHH