ID   HBB_BOSMU               Reviewed;         145 AA.
AC   P02072; A1BMY9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Hemoglobin subunit beta;
DE   AltName: Full=Beta-globin;
DE   AltName: Full=Hemoglobin beta chain;
GN   Name=HBB;
OS   Bos mutus grunniens (Wild yak) (Bos grunniens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=30521;
RN   [1]
RP   PROTEIN SEQUENCE (ALLELES BETA-I AND BETA-II).
RX   PubMed=4005038; DOI=10.1515/bchm3.1985.366.1.63;
RA   Lalthantluanga R., Wiesner H., Braunitzer G.;
RT   "Studies on yak hemoglobin (Bos grunniens, Bovidae): structural basis for
RT   high intrinsic oxygen affinity?";
RL   Biol. Chem. Hoppe-Seyler 366:63-68(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Piao Y., Zheng Y.;
RT   "Cloning and sequencing yak hemoglobin beta globin.";
RL   Submitted (NOV-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   -!- POLYMORPHISM: The beta-II allele is shown. It occurs much more
CC       frequently than the beta-I allele. {ECO:0000269|PubMed:4005038}.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; DQ277007; ABB91431.1; -; mRNA.
DR   PIR; A02390; HBYA2.
DR   AlphaFoldDB; P02072; -.
DR   SMR; P02072; -.
DR   Proteomes; UP000694520; 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   Acetylation; Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Oxygen transport; Phosphoprotein; Reference proteome; S-nitrosylation;
KW   Transport.
FT   CHAIN           1..145
FT                   /note="Hemoglobin subunit beta"
FT                   /id="PRO_0000052891"
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         43
FT                   /note="Phosphoserine"
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   VARIANT         49
FT                   /note="S -> T (in allele beta-I)"
FT                   /evidence="ECO:0000269|PubMed:4005038"
FT   VARIANT         116
FT                   /note="H -> N (in allele beta-I)"
FT                   /evidence="ECO:0000269|PubMed:4005038"
FT   VARIANT         134
FT                   /note="V -> A (in allele beta-I)"
FT                   /evidence="ECO:0000269|PubMed:4005038"
FT   CONFLICT        134
FT                   /note="V -> N (in Ref. 2; ABB91431)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   145 AA;  15991 MW;  F937353D4A65FAA2 CRC64;
     MLTAEEKAAV TAFWGKVKVD EVGGEALGRL LVVYPWTQRF FESFGDLSSA DAVMNNPKVK
     AHGKKVLDSF SNGMKHLDDL KGTFAALSEL HCDKLHVDPE NFKLLGNVLV VVLARHFGKE
     FTPVLQADFQ KVVVGVANAL AHRYH