HBA_RABIT
ID HBA_RABIT Reviewed; 142 AA.
AC P01948;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Hemoglobin subunit alpha-1/2;
DE AltName: Full=Alpha-1/2-globin;
DE AltName: Full=Hemoglobin alpha-1/2 chain;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALPHA-1).
RX PubMed=3001084; DOI=10.1016/s0021-9258(17)36172-0;
RA Cheng J.-F., Raid L., Hardison R.C.;
RT "Isolation and nucleotide sequence of the rabbit globin gene cluster psi
RT zeta-alpha 1-psi alpha. Absence of a pair of alpha-globin genes evolving in
RT concert.";
RL J. Biol. Chem. 261:839-848(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-121.
RX PubMed=699050; DOI=10.1016/0092-8674(78)90081-8;
RA Heindell H.C., Liu A., Paddock G.V., Studnicka G.M., Salser W.A.;
RT "The primary sequence of rabbit alpha-globin mRNA.";
RL Cell 15:43-54(1978).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-41.
RX PubMed=7357610; DOI=10.1016/0092-8674(80)90391-8;
RA Pavlakis G.N., Lockard R.E., Vamvakopoulos N., Rieser L., RajBhandary U.L.,
RA Vournakis J.N.;
RT "Secondary structure of mouse and rabbit alpha- and beta-globin mRNAs:
RT differential accessibility of alpha and beta initiator AUG codons towards
RT nucleases.";
RL Cell 19:91-102(1980).
RN [4]
RP PROTEIN SEQUENCE OF 2-142.
RX PubMed=5679924;
RA Braunitzer G., Flamm U., Best J.S., Schrank B.;
RT "Phylogeny of hemoglobins: the constitution of the alpha-chain of rabbit
RT hemoglobin.";
RL Hoppe-Seyler's Z. Physiol. Chem. 349:1073-1075(1968).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 79-104.
RX PubMed=847466; DOI=10.1126/science.847466;
RA Liu A.Y., Paddock G.V., Heindell H.C., Salser W.;
RT "Nucleotide sequences from a rabbit alpha globin gene inserted in a
RT chimeric plasmid.";
RL Science 196:192-195(1977).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 108-142.
RX PubMed=70277; DOI=10.1016/0092-8674(77)90293-8;
RA Proudfoot N.J., Gillam S., Smith M., Longley J.I.;
RT "Nucleotide sequence of the 3' terminal third of rabbit alpha-globin
RT messenger RNA: comparison with human alpha-globin messenger RNA.";
RL Cell 11:807-818(1977).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 116-142.
RX PubMed=3031053; DOI=10.1016/s0021-9258(18)61204-9;
RA Cheng J.F.F., Raid L., Hardison R.C.;
RT "Block duplications of a zeta-zeta-alpha-theta gene set in the rabbit
RT alpha-like globin gene cluster.";
RL J. Biol. Chem. 262:5414-5421(1987).
RN [8]
RP VARIANTS.
RC STRAIN=Lop ear Dutch;
RX PubMed=5811910; DOI=10.1038/2231270a0;
RA Hunter T., Munro A.;
RT "Allelic variants in the amino-acid sequence of the alpha chain of rabbit
RT haemoglobin.";
RL Nature 223:1270-1272(1969).
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- POLYMORPHISM: There are two alleles. The sequence shown is that of
CC alpha-1. {ECO:0000269|PubMed:5811910}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; X04751; CAA28447.1; -; Genomic_DNA.
DR EMBL; M11113; AAA31267.1; -; Genomic_DNA.
DR EMBL; V00875; CAA24244.2; -; mRNA.
DR EMBL; M10467; AAA31263.1; -; mRNA.
DR EMBL; M10846; AAA31266.1; -; mRNA.
DR EMBL; M15847; AAA31264.1; -; Genomic_DNA.
DR PIR; A25625; HARB.
DR RefSeq; NP_001075858.1; NM_001082389.2.
DR PDB; 2RAO; X-ray; 2.00 A; A/C=2-142.
DR PDBsum; 2RAO; -.
DR AlphaFoldDB; P01948; -.
DR SMR; P01948; -.
DR PRIDE; P01948; -.
DR GeneID; 100009249; -.
DR KEGG; ocu:100009249; -.
DR CTD; 15121; -.
DR EvolutionaryTrace; P01948; -.
DR Proteomes; UP000001811; Unplaced.
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 GO; GO:0006417; P:regulation of translation; IDA:UniProtKB.
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 3D-structure; Acetylation; Direct protein sequencing; Heme; Iron;
KW Metal-binding; Oxygen transport; Phosphoprotein; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:5679924"
FT CHAIN 2..142
FT /note="Hemoglobin subunit alpha-1/2"
FT /id="PRO_0000052746"
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 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 41
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
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 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 30
FT /note="V -> L (in alpha-2)"
FT /evidence="ECO:0000269|PubMed:5811910"
FT VARIANT 49..50
FT /note="FT -> LS (in alpha-2)"
FT /evidence="ECO:0000269|PubMed:5811910"
FT CONFLICT 65
FT /note="E -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:2RAO"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:2RAO"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:2RAO"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:2RAO"
FT HELIX 54..71
FT /evidence="ECO:0007829|PDB:2RAO"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:2RAO"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:2RAO"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:2RAO"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:2RAO"
FT HELIX 97..113
FT /evidence="ECO:0007829|PDB:2RAO"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:2RAO"
FT HELIX 120..137
FT /evidence="ECO:0007829|PDB:2RAO"
SQ SEQUENCE 142 AA; 15589 MW; D117DDF66C13DD2B CRC64;
MVLSPADKTN IKTAWEKIGS HGGEYGAEAV ERMFLGFPTT KTYFPHFDFT HGSEQIKAHG
KKVSEALTKA VGHLDDLPGA LSTLSDLHAH KLRVDPVNFK LLSHCLLVTL ANHHPSEFTP
AVHASLDKFL ANVSTVLTSK YR
