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HBB_PANPA
ID   HBB_PANPA               Reviewed;         147 AA.
AC   P68872; P02023; Q13852; Q14481; Q14510; Q9BX96; Q9UCP8; Q9UCP9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Hemoglobin subunit beta;
DE   AltName: Full=Beta-globin;
DE   AltName: Full=Hemoglobin beta chain;
GN   Name=HBB;
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-147.
RX   PubMed=6406908; DOI=10.1038/303546a0;
RA   Goodman M., Braunitzer G., Stangl A., Schrank B.;
RT   "Evidence on human origins from haemoglobins of African apes.";
RL   Nature 303:546-548(1983).
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 in
CC       adult hemoglobin A (HbA).
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; D93303; HBCZP.
DR   RefSeq; XP_003819077.1; XM_003819029.2.
DR   AlphaFoldDB; P68872; -.
DR   BMRB; P68872; -.
DR   SMR; P68872; -.
DR   STRING; 9597.XP_003819077.1; -.
DR   Ensembl; ENSPPAT00000021208; ENSPPAP00000004625; ENSPPAG00000019351.
DR   GeneID; 100976465; -.
DR   KEGG; pps:100976465; -.
DR   eggNOG; KOG3378; Eukaryota.
DR   GeneTree; ENSGT00940000163476; -.
DR   OMA; TPDAVMN; -.
DR   OrthoDB; 1370439at2759; -.
DR   Proteomes; UP000240080; Chromosome 11.
DR   Bgee; ENSPPAG00000019351; Expressed in liver and 6 other tissues.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0031838; C:haptoglobin-hemoglobin complex; IEA:Ensembl.
DR   GO; GO:0005833; C:hemoglobin complex; IEA:Ensembl.
DR   GO; GO:0031720; F:haptoglobin binding; IEA:Ensembl.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0030492; F:hemoglobin binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019825; F:oxygen binding; IEA:Ensembl.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IEA:Ensembl.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:Ensembl.
DR   GO; GO:0030185; P:nitric oxide transport; IEA:Ensembl.
DR   GO; GO:0010942; P:positive regulation of cell death; IEA:Ensembl.
DR   GO; GO:0070293; P:renal absorption; IEA:Ensembl.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P02086,
FT                   ECO:0000269|PubMed:6406908"
FT   CHAIN           2..147
FT                   /note="Hemoglobin subunit beta"
FT                   /id="PRO_0000053056"
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"
SQ   SEQUENCE   147 AA;  15998 MW;  A31F6D621C6556A1 CRC64;
     MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS TPDAVMGNPK
     VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELHCDKLHVD PENFRLLGNV LVCVLAHHFG
     KEFTPPVQAA YQKVVAGVAN ALAHKYH
 
 
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