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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
 
 
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