ID   HBB_ATEPA               Reviewed;         147 AA.
AC   Q6WN22; P02034;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Hemoglobin subunit beta;
DE   AltName: Full=Beta-globin;
DE   AltName: Full=Hemoglobin beta chain;
GN   Name=HBB;
OS   Ateles paniscus (Black spider monkey) (Red-faced black spider monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Atelidae;
OC   Atelinae; Ateles.
OX   NCBI_TaxID=9510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Prychitko T.M., Goodman M., Johnson R.M.;
RT   "The molecular evolution of the primate beta globin gene: an evaluation of
RT   gene conversion and phylogeny and an analysis of phylogenetic footprints in
RT   noncoding DNA.";
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 2-147.
RX   PubMed=4981734; DOI=10.1111/j.1749-6632.1969.tb27806.x;
RA   Boyer S.H., Crosby E.F., Fuller G.F., Noyes A.N., Adams J.G.;
RT   "The structure and biosynthesis of hemoglobins A and A2 in the new world
RT   primate Ateles paniscus: a preliminary account.";
RL   Ann. N. Y. Acad. Sci. 165:360-377(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   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; AY279117; AAQ18225.1; -; Genomic_DNA.
DR   PIR; A90034; HBMKK.
DR   AlphaFoldDB; Q6WN22; -.
DR   SMR; Q6WN22; -.
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; S-nitrosylation; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P02086,
FT                   ECO:0000269|PubMed:4981734"
FT   CHAIN           2..147
FT                   /note="Hemoglobin subunit beta"
FT                   /id="PRO_0000052885"
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   CONFLICT        10
FT                   /note="S -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        14
FT                   /note="T -> A (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        51
FT                   /note="S -> T (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        57
FT                   /note="G -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   147 AA;  16046 MW;  311A793EFAFCF09A CRC64;
     MVHLTGEEKS AVTTLWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS SPDAVMGNPK
     VKAHGKKVLG AFSDGLAHLD NLKGTFAQLS ELHCDKLHVD PENFRLLGNV LVCVLAHHFG
     KEFTPQLQAA YQKVVAGVAN ALAHKYH