ID   GLB_AEQEI               Reviewed;         147 AA.
AC   Q8T7J9;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Globin;
OS   Aequiyoldia eightsii (Antarctic yoldia) (Yoldia eightsii).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Protobranchia; Nuculanida; Sareptidae; Aequiyoldia.
OX   NCBI_TaxID=2716527;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
RX   PubMed=12423205; DOI=10.1042/bj20020727;
RA   Dewilde S., Angelini E., Kiger L., Marden M.C., Beltramini M., Salvato B.,
RA   Moens L.;
RT   "Structure and function of the globin and globin gene from the Antarctic
RT   mollusc Yoldia eightsi.";
RL   Biochem. J. 370:245-253(2003).
CC   -!- SUBUNIT: Homodimer or homooligomer. {ECO:0000269|PubMed:12423205}.
CC   -!- MISCELLANEOUS: Adapted to the low-temperature environment by a decrease
CC       in the oxygen affinity via an increased ligand-dissociation rate. At 2
CC       degrees Celsius this hemoglobin has an oxygen affinity similar to other
CC       hemoglobins at 25 degrees Celsius.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; AF361744; AAM00251.1; -; mRNA.
DR   AlphaFoldDB; Q8T7J9; -.
DR   SMR; Q8T7J9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
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; 1.
DR   Gene3D; 1.10.490.10; -; 1.
DR   InterPro; IPR002336; Erythrocruorin.
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; 1.
DR   PRINTS; PR00611; ERYTHCRUORIN.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   1: Evidence at protein level;
KW   Heme; Iron; Metal-binding; Muscle protein; Oxygen transport; Transport.
FT   CHAIN           1..147
FT                   /note="Globin"
FT                   /id="PRO_0000260274"
FT   BINDING         64
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         95
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   147 AA;  16164 MW;  849B333E5C274DAA CRC64;
     MSFSAAQVDT VRSNWCSMTA DIDAAGYRIF ELLFQRNPDY QSKFKAFKGL AVSALKGNPN
     AEKHIRIVLG GLGRILGALN TPELDVIYKE MASNHKPRGV MKQQFKDMGQ AIVTALSEIQ
     SKSGGSFDRA TWEALFESVA NGIGQYQ