ID   HBA_LOXAF               Reviewed;         141 AA.
AC   P01955;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 113.
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   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6479896; DOI=10.1515/bchm2.1984.365.2.743;
RA   Braunitzer G., Stangl A., Schrank B., Krombach C., Wiesner H.;
RT   "Phosphate-haemoglobin interaction. The primary structure of the
RT   haemoglobin of the African elephant (Loxodonta africana, Proboscidea):
RT   asparagine in position 2 of the beta-chain.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 365:743-749(1984).
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; A02278; HAELA.
DR   AlphaFoldDB; P01955; -.
DR   SMR; P01955; -.
DR   STRING; 9785.ENSLAFP00000013265; -.
DR   eggNOG; KOG3378; Eukaryota.
DR   HOGENOM; CLU_003827_10_2_1; -.
DR   InParanoid; P01955; -.
DR   OMA; FGKIGGQ; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
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; 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   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00612; ALPHAHAEM.
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; Reference proteome; Transport.
FT   CHAIN           1..141
FT                   /note="Hemoglobin subunit alpha"
FT                   /id="PRO_0000052670"
FT   PEPTIDE         95..103
FT                   /note="Hemopressin"
FT                   /evidence="ECO:0000250|UniProtKB:P01946"
FT                   /id="PRO_0000455891"
FT   BINDING         58
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         87
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         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P69905"
FT   MOD_RES         7
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P01942"
FT   MOD_RES         8
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P69905"
FT   MOD_RES         11
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P01942"
FT   MOD_RES         16
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P69905"
FT   MOD_RES         16
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P01942"
FT   MOD_RES         24
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P69905"
FT   MOD_RES         35
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P69905"
FT   MOD_RES         40
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P01942"
FT   MOD_RES         102
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01942"
FT   MOD_RES         108
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P01942"
FT   MOD_RES         124
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01942"
FT   MOD_RES         134
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P01942"
FT   MOD_RES         137
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P01942"
FT   MOD_RES         138
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P01942"
SQ   SEQUENCE   141 AA;  15501 MW;  EB91597BBF674AC4 CRC64;
     VLSDNDKTNV KATWSKVGDH ASDYVAEALE RMFFSFPTTK TYFPHFDLGH GSGQVKAHGK
     KVGEALTQAV GHLDDLPSAL SALSDLHAHK LRVDPVNFKL LSHCLLVTLS SHQPTEFTPE
     VHASLDKFLS NVSTVLTSKY R