ID   HBA_CRIGA               Reviewed;         142 AA.
AC   P19014;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Hemoglobin subunit alpha;
DE   AltName: Full=Alpha-globin;
DE   AltName: Full=Hemoglobin alpha chain;
DE   Contains:
DE     RecName: Full=Hemopressin {ECO:0000250|UniProtKB:P01946};
GN   Name=HBA;
OS   Cricetomys gambianus (Northern giant pouched rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Nesomyidae; Cricetomyinae; Cricetomys.
OX   NCBI_TaxID=10085;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-142.
RX   PubMed=2276480; DOI=10.1042/bst0180628;
RA   Hombrados I., Vidal Y., Rodewald K., Braunitzer G., Neuzil E.;
RT   "Primary structure of the alpha-chains of the haemoglobins of the Gambia
RT   rat (Cricetomys gambianus Waterhouse).";
RL   Biochem. Soc. Trans. 18:628-629(1990).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC       peripheral tissues.
CC   -!- FUNCTION: [Hemopressin]: Hemopressin acts as an antagonist peptide of
CC       the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks
CC       cannabinoid receptor CNR1 and subsequent signaling.
CC       {ECO:0000250|UniProtKB:P01946}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; A37171; A37171.
DR   PIR; B37171; B37171.
DR   AlphaFoldDB; P19014; -.
DR   SMR; P19014; -.
DR   GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   CDD; cd08927; Hb-alpha-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; IPR002338; Hemoglobin_a-typ.
DR   InterPro; IPR002339; Hemoglobin_pi.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00612; ALPHAHAEM.
DR   PRINTS; PR00815; PIHAEM.
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; Phosphoprotein; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P18969"
FT   CHAIN           2..142
FT                   /note="Hemoglobin subunit alpha"
FT                   /id="PRO_0000052608"
FT   PEPTIDE         96..104
FT                   /note="Hemopressin"
FT                   /evidence="ECO:0000250|UniProtKB:P01946"
FT                   /id="PRO_0000455860"
FT   BINDING         59
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   BINDING         88
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         4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P69905"
FT   MOD_RES         8
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P01942"
FT   MOD_RES         12
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P01942"
FT   MOD_RES         17
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P69905"
FT   MOD_RES         17
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P01942"
FT   MOD_RES         25
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P69905"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P69905"
FT   MOD_RES         41
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P01942"
FT   MOD_RES         50
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P69905"
FT   MOD_RES         109
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P01942"
FT   MOD_RES         125
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01942"
FT   MOD_RES         132
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01942"
FT   MOD_RES         135
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P01942"
FT   MOD_RES         138
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P01942"
FT   MOD_RES         139
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01942"
FT   VARIANT         45
FT                   /note="P -> A"
SQ   SEQUENCE   142 AA;  15179 MW;  98292AD7B41D6D2F CRC64;
     MVLSADDKAN IKATWEKIGG HGAEYGAEAL ERMFASFPTT KTYFPHFDVS HGSAQVKSHG
     KKVADALANA AHHLDDLPGA LSALSDLHAH KLRVDPVNFK LLGHCLLVTL ATHLQAGLTP
     AAHASLDKFL ASVSTVLTSK YR