HBBF_BOVIN
ID HBBF_BOVIN Reviewed; 145 AA.
AC P02081; Q3SX09;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Hemoglobin fetal subunit beta;
DE AltName: Full=Beta-globin, fetal;
DE AltName: Full=Hemoglobin beta chain, fetal;
DE AltName: Full=Hemoglobin gamma chain;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=5958205; DOI=10.1021/bi00868a025;
RA Babin D.R., Schroeder W.A., Shelton J.R., Shelton J.B., Robberson B.;
RT "The amino acid sequence of the gamma chain of bovine fetal hemoglobin.";
RL Biochemistry 5:1297-1310(1966).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6322113; DOI=10.1093/nar/12.3.1641;
RA Schimenti J.C., Duncan C.H.;
RT "Ruminant globin gene structures suggest an evolutionary role for Alu-type
RT repeats.";
RL Nucleic Acids Res. 12:1641-1655(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; X00354; CAA25101.1; -; Genomic_DNA.
DR EMBL; M63452; AAA30519.1; -; Genomic_DNA.
DR EMBL; BC104565; AAI04566.2; -; mRNA.
DR PIR; A93504; HBBOF.
DR RefSeq; NP_001014902.1; NM_001014902.3.
DR RefSeq; NP_001103979.1; NM_001110509.2.
DR AlphaFoldDB; P02081; -.
DR SMR; P02081; -.
DR STRING; 9913.ENSBTAP00000043063; -.
DR PaxDb; P02081; -.
DR PeptideAtlas; P02081; -.
DR PRIDE; P02081; -.
DR Ensembl; ENSBTAT00000045694; ENSBTAP00000043063; ENSBTAG00000038748.
DR GeneID; 511735; -.
DR KEGG; bta:511735; -.
DR CTD; 511735; -.
DR VEuPathDB; HostDB:ENSBTAG00000038748; -.
DR eggNOG; KOG3378; Eukaryota.
DR GeneTree; ENSGT00940000156216; -.
DR HOGENOM; CLU_003827_10_0_1; -.
DR InParanoid; P02081; -.
DR OMA; HITLCMA; -.
DR OrthoDB; 1370439at2759; -.
DR TreeFam; TF333268; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000038748; Expressed in floor plate of diencephalon and 60 other tissues.
DR GO; GO:0031838; C:haptoglobin-hemoglobin complex; IBA:GO_Central.
DR GO; GO:0005833; C:hemoglobin complex; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0031721; F:hemoglobin alpha binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043177; F:organic acid binding; IBA:GO_Central.
DR GO; GO:0019825; F:oxygen binding; IBA:GO_Central.
DR GO; GO:0005344; F:oxygen carrier activity; IBA:GO_Central.
DR GO; GO:0098869; P:cellular oxidant detoxification; IEA:GOC.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
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 Direct protein sequencing; Heme; Iron; Metal-binding; Oxygen transport;
KW Reference proteome; Transport.
FT CHAIN 1..145
FT /note="Hemoglobin fetal subunit beta"
FT /id="PRO_0000052893"
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"
SQ SEQUENCE 145 AA; 15859 MW; 78B8722915E9C221 CRC64;
MLSAEEKAAV TSLFAKVKVD EVGGEALGRL LVVYPWTQRF FESFGDLSSA DAILGNPKVK
AHGKKVLDSF CEGLKQLDDL KGAFASLSEL HCDKLHVDPE NFRLLGNVLV VVLARRFGSE
FSPELQASFQ KVVTGVANAL AHRYH