HBB_SHEEP
ID HBB_SHEEP Reviewed; 145 AA.
AC P02075;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=HBB;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE (ALLELE B).
RX PubMed=2494347; DOI=10.1007/bf02102474;
RA Garner K.J., Lingrel J.B.;
RT "A comparison of the beta A- and beta B-globin gene clusters of sheep.";
RL J. Mol. Evol. 28:175-184(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28; 39-59; 72-85 AND 104-145 (ALLELE
RP A).
RX PubMed=6161931; DOI=10.1016/s0021-9258(19)69903-5;
RA Kretschmer P.J., Coon H.C., Davis A., Harrison M., Nienhuis A.W.;
RT "Hemoglobin switching in sheep. Isolation of the fetal gamma-globin gene
RT and demonstration that the fetal gamma- and adult beta A-globin genes lie
RT within eight kilobase segments of homologous DNA.";
RL J. Biol. Chem. 256:1975-1982(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-28 (ALLELE B).
RX PubMed=3367782; DOI=10.1093/oxfordjournals.molbev.a040486;
RA Garner K.J., Lingrel J.B.;
RT "Structural organization of the beta-globin locus of B-haplotype sheep.";
RL Mol. Biol. Evol. 5:134-140(1988).
RN [4]
RP PROTEIN SEQUENCE (ALLELE B).
RX PubMed=6022868; DOI=10.1016/s0021-9258(18)96038-2;
RA Boyer S.H., Hathaway P., Pascasio F., Bordley J., Orton C., Naughton M.A.;
RT "Differences in the amino acid sequences of tryptic peptides from three
RT sheep hemoglobin beta chains.";
RL J. Biol. Chem. 242:2211-2232(1967).
RN [5]
RP VARIANT ALLELE A.
RX PubMed=6033754; DOI=10.1042/bj1030129;
RA Beale D.;
RT "A partial amino acid sequence for sheep haemoblogin A.";
RL Biochem. J. 103:129-140(1967).
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: Sheep has two allelic beta chains, A and B. The B allele
CC sequence is shown. {ECO:0000269|PubMed:6022868,
CC ECO:0000269|PubMed:6033754}.
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; X14727; CAA32849.1; -; Genomic_DNA.
DR EMBL; K02820; AAA31529.1; -; Genomic_DNA.
DR EMBL; K02821; AAA31530.1; -; Genomic_DNA.
DR EMBL; K02822; AAA31531.1; -; Genomic_DNA.
DR EMBL; K02823; AAA31532.1; -; Genomic_DNA.
DR EMBL; M19754; AAA31528.1; -; mRNA.
DR PIR; A94556; HBSHA.
DR PIR; S10073; HBSHB.
DR RefSeq; XP_004016289.1; XM_004016240.2.
DR PDB; 2QU0; X-ray; 2.70 A; B/D=1-145.
DR PDBsum; 2QU0; -.
DR AlphaFoldDB; P02075; -.
DR SMR; P02075; -.
DR STRING; 9940.ENSOARP00000020586; -.
DR PRIDE; P02075; -.
DR eggNOG; KOG3378; Eukaryota.
DR OMA; TPDAVMN; -.
DR OrthoDB; 1370439at2759; -.
DR EvolutionaryTrace; P02075; -.
DR Proteomes; UP000002356; 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 CHAIN 1..145
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000053105"
FT BINDING 62
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 91
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 11
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 58
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 81
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 92
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 143
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT VARIANT 49
FT /note="N -> S (in allele A)"
FT /evidence="ECO:0000269|PubMed:6033754,
FT ECO:0000269|PubMed:6161931"
FT VARIANT 57
FT /note="P -> A (in allele A)"
FT /evidence="ECO:0000269|PubMed:6033754,
FT ECO:0000269|PubMed:6161931"
FT VARIANT 74..75
FT /note="MK -> VQ (in allele A)"
FT /evidence="ECO:0000269|PubMed:6033754,
FT ECO:0000269|PubMed:6161931"
FT VARIANT 119
FT /note="N -> S (in allele A)"
FT /evidence="ECO:0000269|PubMed:6033754,
FT ECO:0000269|PubMed:6161931"
FT VARIANT 128
FT /note="D -> E (in allele A)"
FT /evidence="ECO:0000269|PubMed:6033754,
FT ECO:0000269|PubMed:6161931"
FT VARIANT 143
FT /note="K -> R (in allele A)"
FT /evidence="ECO:0000269|PubMed:6033754,
FT ECO:0000269|PubMed:6161931"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:2QU0"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:2QU0"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:2QU0"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:2QU0"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:2QU0"
FT HELIX 57..73
FT /evidence="ECO:0007829|PDB:2QU0"
FT HELIX 80..93
FT /evidence="ECO:0007829|PDB:2QU0"
FT HELIX 100..117
FT /evidence="ECO:0007829|PDB:2QU0"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:2QU0"
FT HELIX 123..141
FT /evidence="ECO:0007829|PDB:2QU0"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:2QU0"
SQ SEQUENCE 145 AA; 16073 MW; 6CA7CFA4574DD140 CRC64;
MLTAEEKAAV TGFWGKVKVD EVGAEALGRL LVVYPWTQRF FEHFGDLSNA DAVMNNPKVK
AHGKKVLDSF SNGMKHLDDL KGTFAQLSEL HCDKLHVDPE NFRLLGNVLV VVLARHHGNE
FTPVLQADFQ KVVAGVANAL AHKYH
