ID   GLB1B_ANATR             Reviewed;         152 AA.
AC   P04251;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Globin-1 subunit beta;
DE            Short=Globin I beta chain;
OS   Anadara trapezia (Sydney cockle) (Arca trapezia).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Arcoida; Arcoidea; Arcidae; Anadara.
OX   NCBI_TaxID=6556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Blood;
RX   PubMed=8064872; DOI=10.1007/bf00178248;
RA   Nassif N.T., Glenn W.K., Mackinlay A.G.;
RT   "The organization of the beta-globin gene of the bivalve mollusc Anadara
RT   trapezia and its evolutionary relationship to other invertebrate and
RT   vertebrate globin genes.";
RL   J. Mol. Evol. 39:47-55(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-152, AND ACETYLATION AT SER-2.
RX   PubMed=4091752; DOI=10.1071/bi9850221;
RA   Gilbert A.T., Thompson E.O.P.;
RT   "Amino acid sequence of the beta-chain of the tetrameric haemoglobin of the
RT   bivalve mollusc, Anadara trapezia.";
RL   Aust. J. Biol. Sci. 38:221-236(1985).
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; L16978; AAA62149.1; -; Genomic_DNA.
DR   PIR; A02533; GGNKT.
DR   AlphaFoldDB; P04251; -.
DR   SMR; P04251; -.
DR   iPTMnet; P04251; -.
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; 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   SUPFAM; SSF46458; SSF46458; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Oxygen transport; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4091752"
FT   CHAIN           2..152
FT                   /note="Globin-1 subunit beta"
FT                   /id="PRO_0000052485"
FT   BINDING         72
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         104
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   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:4091752"
FT   CONFLICT        143
FT                   /note="S -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        151
FT                   /note="A -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   152 AA;  16524 MW;  2124ED85BEF02A26 CRC64;
     MSTVAELANA VVSNADQKDL LRLSWGVLSV DMEGTGLMLM ANLFKTSSAA RTKFARLGDV
     SAGKDNSKLR GHSITLMYAL QNFIDALDNV DRLKCVVEKF AVNHINRQIS ADEFGEIVGP
     LRQTLKARMG SYFDEDTVSA WASLVAVVQA AL