ID   GLB2A_ANAIN             Reviewed;         150 AA.
AC   P14821;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Globin-2 A chain;
DE   AltName: Full=Globin II A chain;
DE   AltName: Full=HBII-A;
OS   Anadara inaequivalvis (Inequivalve ark) (Scapharca inaequivalvis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Arcoida; Arcoidea; Arcidae; Anadara.
OX   NCBI_TaxID=2784303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8370466; DOI=10.1016/0014-5793(93)80926-l;
RA   Gambacurta A., Piro M.C., Ascoli F.;
RT   "Cooperative homodimeric hemoglobin from Scapharca inaequivalvis. cDNA
RT   cloning and expression of the fully functional protein in E. coli.";
RL   FEBS Lett. 330:90-94(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8995056; DOI=10.1007/bf02202107;
RA   Piro M.C., Gambacurta A., Ascoli F.;
RT   "Scapharca inaequivalvis tetrameric hemoglobin A and B chains: cDNA
RT   sequencing and genomic organization.";
RL   J. Mol. Evol. 43:594-601(1996).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-150.
RX   PubMed=2599099; DOI=10.1016/0014-5793(89)81512-1;
RA   Petruzzelli R., Boffi A., Barra D., Bossa F., Ascoli F., Chiancone E.;
RT   "Scapharca hemoglobins, type cases of a novel mode of chain assembly and
RT   heme-heme communication. Amino acid sequence and subunit interactions of
RT   the tetrameric component.";
RL   FEBS Lett. 259:133-136(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE OF 41-113.
RA   Gambacurta A.;
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH HEME, AND SUBUNIT.
RX   PubMed=7473710; DOI=10.1006/jmbi.1995.0543;
RA   Royer W.E. Jr., Heard K.S., Harrington D.J., Chiancone E.;
RT   "The 2.0 A crystal structure of Scapharca tetrameric hemoglobin:
RT   cooperative dimers within an allosteric tetramer.";
RL   J. Mol. Biol. 253:168-186(1995).
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC       {ECO:0000269|PubMed:7473710}.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; X71386; CAA50509.1; -; mRNA.
DR   EMBL; S83524; AAL96376.1; -; Genomic_DNA.
DR   EMBL; X98566; CAA67176.1; -; Genomic_DNA.
DR   PIR; S39980; S39980.
DR   PDB; 4HRR; X-ray; 1.25 A; A/C/E/G=2-150.
DR   PDB; 4HRT; X-ray; 1.46 A; A/C/E/G=5-150.
DR   PDBsum; 4HRR; -.
DR   PDBsum; 4HRT; -.
DR   AlphaFoldDB; P14821; -.
DR   SMR; P14821; -.
DR   EvolutionaryTrace; P14821; -.
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   3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Oxygen transport; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2599099"
FT   CHAIN           2..150
FT                   /note="Globin-2 A chain"
FT                   /id="PRO_0000052488"
FT   BINDING         102
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   MOD_RES         2
FT                   /note="Blocked amino end (Val)"
FT                   /evidence="ECO:0000269|PubMed:2599099"
FT   HELIX           3..10
FT                   /evidence="ECO:0007829|PDB:4HRR"
FT   HELIX           13..26
FT                   /evidence="ECO:0007829|PDB:4HRR"
FT   HELIX           27..29
FT                   /evidence="ECO:0007829|PDB:4HRR"
FT   HELIX           30..44
FT                   /evidence="ECO:0007829|PDB:4HRR"
FT   HELIX           46..51
FT                   /evidence="ECO:0007829|PDB:4HRR"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:4HRR"
FT   HELIX           58..63
FT                   /evidence="ECO:0007829|PDB:4HRR"
FT   HELIX           65..83
FT                   /evidence="ECO:0007829|PDB:4HRR"
FT   TURN            84..86
FT                   /evidence="ECO:0007829|PDB:4HRR"
FT   HELIX           88..103
FT                   /evidence="ECO:0007829|PDB:4HRR"
FT   TURN            104..106
FT                   /evidence="ECO:0007829|PDB:4HRR"
FT   HELIX           109..112
FT                   /evidence="ECO:0007829|PDB:4HRR"
FT   HELIX           113..115
FT                   /evidence="ECO:0007829|PDB:4HRR"
FT   HELIX           116..127
FT                   /evidence="ECO:0007829|PDB:4HRR"
FT   HELIX           128..130
FT                   /evidence="ECO:0007829|PDB:4HRR"
FT   HELIX           133..149
FT                   /evidence="ECO:0007829|PDB:4HRR"
SQ   SEQUENCE   150 AA;  16238 MW;  39B996380CBC0315 CRC64;
     MVADAVAKVC GSEAIKANLR RSWGVLSADI EATGLMLMSN LFTLRPDTKT YFTRLGDVQK
     GKANSKLRGH AITLTYALNN FVDSLDDPSR LKCVVEKFAV NHINRKISGD AFGAIVEPMK
     ETLKARMGNY YSDDVAGAWA ALVGVVQAAL