HBA_PIPAB
ID HBA_PIPAB Reviewed; 143 AA.
AC Q862A7;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 77.
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 Pipistrellus abramus (Japanese pipistrelle) (Pipistrellus javanicus
OS abramus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Pipistrellus.
OX NCBI_TaxID=105295;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RX PubMed=12207041; DOI=10.1266/ggs.77.197;
RA Hamada K., Horiike T., Kanaya S., Nakamura H., Ota H., Yatogo T., Okada K.,
RA Nakamura H., Shinozawa T.;
RT "Changes in body temperature pattern in vertebrates do not influence the
RT codon usages of alpha-globin genes.";
RL Genes Genet. Syst. 77:197-207(2002).
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 EMBL; AB104818; BAC57967.1; -; mRNA.
DR AlphaFoldDB; Q862A7; -.
DR SMR; Q862A7; -.
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 2: Evidence at transcript level;
KW Acetylation; Heme; Iron; Metal-binding; Oxygen transport; Phosphoprotein;
KW Transport.
FT CHAIN 1..143
FT /note="Hemoglobin subunit alpha"
FT /id="PRO_0000052732"
FT PEPTIDE 97..105
FT /note="Hemopressin"
FT /evidence="ECO:0000250|UniProtKB:P01946"
FT /id="PRO_0000455927"
FT BINDING 60
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 89
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 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
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 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 110
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 136
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
SQ SEQUENCE 143 AA; 15456 MW; 4EC8AE7096747380 CRC64;
MVLSPADKTN VKAAWDKVGG HAGDYGAEAL ERMFLSFPTT KTYFPHFSDL SHGSAQVKAH
GKKVGDALNN AVGHMDDLPT ALSALSDLHA HKLRVDPVNF KLLSHCLLVT LACHHPAEFT
PAVHASLDKF LANVSTVLVS KYR