HBB_RABIT
ID HBB_RABIT Reviewed; 147 AA.
AC P02057;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Hemoglobin subunit beta-1/2;
DE AltName: Full=Beta-1/2-globin;
DE AltName: Full=Hemoglobin beta-1/2 chain;
GN Name=HBB1;
GN and
GN Name=HBB2;
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] (BETA-1).
RX PubMed=482942; DOI=10.1126/science.482942;
RA van Ooyen A., van den Berg J., Mantei N., Weissmann C.;
RT "Comparison of total sequence of a cloned rabbit beta-globin gene and its
RT flanking regions with a homologous mouse sequence.";
RL Science 206:337-344(1979).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (BETA-1).
RX PubMed=558827; DOI=10.1016/0092-8674(77)90090-3;
RA Efstratiadis A., Kafatos F.C., Maniatis T.;
RT "The primary structure of rabbit beta-globin mRNA as determined from cloned
RT DNA.";
RL Cell 10:571-585(1977).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (BETA-1).
RX PubMed=277327; DOI=10.1101/sqb.1978.042.01.095;
RA Sim G.K., Efstratiadis A., Jones C.W., Kafatos F.C., Koehler M.,
RA Kronenberg H.M., Maniatis T., Regier J.C., Roberts B.F., Rosenthal N.;
RT "Studies on the structure of genes expressed during development.";
RL Cold Spring Harb. Symp. Quant. Biol. 42:933-945(1978).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (BETA-2).
RX PubMed=519769; DOI=10.1016/0092-8674(79)90239-3;
RA Hardison R.C., Butler E.T. III, Lacy E., Maniatis T., Rosenthal N.,
RA Efstratiadis A.;
RT "The structure and transcription of four linked rabbit beta-like globin
RT genes.";
RL Cell 18:1285-1297(1979).
RN [5]
RP NUCLEOTIDE SEQUENCE (BETA-2).
RX PubMed=2486295; DOI=10.1016/0022-2836(89)90362-8;
RA Margot J.B., Demers G.W., Hardison R.C.;
RT "Complete nucleotide sequence of the rabbit beta-like globin gene cluster.
RT Analysis of intergenic sequences and comparison with the human beta-like
RT globin gene cluster.";
RL J. Mol. Biol. 205:15-40(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-62 (BETA-1).
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 [7]
RP PROTEIN SEQUENCE OF 2-147 (BETA-1).
RX PubMed=5789874; DOI=10.1515/bchm2.1969.350.1.563;
RA Best J.S., Flamm U., Braunitzer G.;
RT "Haemoglobins, XVII. The primary structure of the beta-chain of rabbit
RT haemoglobin.";
RL Hoppe-Seyler's Z. Physiol. Chem. 350:563-580(1969).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 100-115 (BETA-1).
RX PubMed=264241; DOI=10.1038/276037a0;
RA van den Berg J., van Ooyen A., Mantei N., Schamboeck A., Grosveld G.,
RA Flavell R.A., Weissmann C.;
RT "Comparison of cloned rabbit and mouse beta-globin genes showing strong
RT evolutionary divergence of two homologous pairs of introns.";
RL Nature 276:37-44(1978).
RN [9]
RP OCCURRENCE AND FREQUENCY OF ALLELIC CHAINS.
RX PubMed=4530669; DOI=10.1111/j.1749-6632.1974.tb21899.x;
RA Garrick M.D., Hafner R., Bricker J., Garrick L.M.;
RT "Genetic variation in the primary structure of the beta chain of rabbit
RT hemoglobin.";
RL Ann. N. Y. Acad. Sci. 241:436-438(1974).
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 beta-1; the most frequent of the two common alleles.
CC {ECO:0000305|PubMed:4530669}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J00660; AAA31274.1; -; Genomic_DNA.
DR EMBL; V00882; CAA24251.1; -; Genomic_DNA.
DR EMBL; M18818; AAA02985.1; -; Unassigned_DNA.
DR EMBL; V00878; CAA24247.1; -; Genomic_DNA.
DR EMBL; V00879; CAA24248.1; -; mRNA.
DR EMBL; M10843; AAA31270.1; -; mRNA.
DR EMBL; K03256; AAA31277.1; -; Genomic_DNA.
DR EMBL; M10525; AAA31268.1; -; mRNA.
DR EMBL; M10831; AAA31271.1; -; Genomic_DNA.
DR EMBL; J00659; AAA31273.1; -; Genomic_DNA.
DR EMBL; M10833; AAA31272.1; -; Genomic_DNA.
DR EMBL; M10832; AAA31272.1; JOINED; Genomic_DNA.
DR PIR; I46476; HBRB.
DR RefSeq; NP_001075729.2; NM_001082260.3.
DR PDB; 2RAO; X-ray; 2.00 A; B/D=2-147.
DR PDBsum; 2RAO; -.
DR AlphaFoldDB; P02057; -.
DR SMR; P02057; -.
DR STRING; 9986.ENSOCUP00000000491; -.
DR PRIDE; P02057; -.
DR GeneID; 100009084; -.
DR KEGG; ocu:100009084; -.
DR CTD; 100009084; -.
DR eggNOG; KOG3378; Eukaryota.
DR InParanoid; P02057; -.
DR OrthoDB; 1370439at2759; -.
DR TreeFam; TF333268; -.
DR EvolutionaryTrace; P02057; -.
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: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; cd08925; Hb-beta-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; IPR002337; Hemoglobin_b.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR00814; BETAHAEM.
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 S-nitrosylation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02086"
FT CHAIN 2..147
FT /note="Hemoglobin subunit beta-1/2"
FT /id="PRO_0000053085"
FT BINDING 64
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 93
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:0000250|UniProtKB:P02086"
FT MOD_RES 13
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 60
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 83
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 94
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 145
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT VARIANT 53
FT /note="N -> H (in beta-2)"
FT /evidence="ECO:0000269|PubMed:2486295,
FT ECO:0000269|PubMed:519769"
FT VARIANT 57
FT /note="N -> S (in beta-2)"
FT /evidence="ECO:0000269|PubMed:2486295,
FT ECO:0000269|PubMed:519769"
FT VARIANT 77
FT /note="S -> N (in beta-2)"
FT /evidence="ECO:0000269|PubMed:2486295,
FT ECO:0000269|PubMed:519769"
FT VARIANT 113
FT /note="I -> V (in beta-2)"
FT /evidence="ECO:0000269|PubMed:2486295,
FT ECO:0000269|PubMed:519769"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:2RAO"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:2RAO"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:2RAO"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:2RAO"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:2RAO"
FT HELIX 59..76
FT /evidence="ECO:0007829|PDB:2RAO"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:2RAO"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:2RAO"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:2RAO"
FT HELIX 102..119
FT /evidence="ECO:0007829|PDB:2RAO"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:2RAO"
FT HELIX 125..142
FT /evidence="ECO:0007829|PDB:2RAO"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:2RAO"
SQ SEQUENCE 147 AA; 16133 MW; C119C758DD3361D1 CRC64;
MVHLSSEEKS AVTALWGKVN VEEVGGEALG RLLVVYPWTQ RFFESFGDLS SANAVMNNPK
VKAHGKKVLA AFSEGLSHLD NLKGTFAKLS ELHCDKLHVD PENFRLLGNV LVIVLSHHFG
KEFTPQVQAA YQKVVAGVAN ALAHKYH
