ID   GLB1A_ANATR             Reviewed;         151 AA.
AC   P14395;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Globin-1 subunit alpha;
DE   AltName: Full=Globin I alpha 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   PROTEIN SEQUENCE OF 2-151, AND ACETYLATION AT VAL-2.
RA   Como P.F., Thompson E.O.P.;
RT   "Amino acid sequence of the alpha-chain of the tetrameric haemoglobin of
RT   the bivalve mollusc Anadara trapezia.";
RL   Aust. J. Biol. Sci. 33:653-664(1980).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 104-151.
RC   TISSUE=Blood;
RX   PubMed=8359016; DOI=10.1016/0305-0491(93)90230-3;
RA   Nassif N.T., Mackinlay A.G., Thompson E.O.P.;
RT   "PCR amplification of partial mRNA sequences encoding the alpha- and beta-
RT   globin chains of the bivalve mollusc Anadara trapezia: correction of the C-
RT   terminal amino acid sequence of the alpha-chain.";
RL   Comp. Biochem. Physiol. 105B:283-287(1993).
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; L24375; AAA53651.1; -; mRNA.
DR   PIR; S06503; S06503.
DR   AlphaFoldDB; P14395; -.
DR   SMR; P14395; -.
DR   PRIDE; P14395; -.
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|Ref.1"
FT   CHAIN           2..151
FT                   /note="Globin-1 subunit alpha"
FT                   /id="PRO_0000052484"
FT   BINDING         103
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="N-acetylvaline"
FT                   /evidence="ECO:0000269|Ref.1"
FT   CONFLICT        118..119
FT                   /note="EP -> PE (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        132
FT                   /note="Missing (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        137..138
FT                   /note="AG -> GA (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141..149
FT                   /note="AALIGVVQA -> VQAILGMQNAVLS (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   151 AA;  16431 MW;  250BB3A611AA7E48 CRC64;
     MVADAVAKVC GSEAIKGNLR RSWGVLMSAD IEATGLTYLA NLFTLRPDTK TYFTRLGDVQ
     KGKANSKLRG HAITLTYALD WFVDSLDDPS RLKCVVEKFA VNHINRKISG DAFGSIIEPM
     KETLKARMGS YYSDDVAGAW AALIGVVQAA L