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HBB_MACFA
ID   HBB_MACFA               Reviewed;         147 AA.
AC   P68223; P02027; Q9TSL4;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Hemoglobin subunit beta;
DE   AltName: Full=Beta-globin;
DE   AltName: Full=Hemoglobin beta chain;
GN   Name=HBB;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-121.
RX   PubMed=3110424; DOI=10.1007/bf02134129;
RA   Savatier P., Trabuchet G., Chebloune Y., Faure C., Verdier G., Nigon V.M.;
RT   "Nucleotide sequence of the beta-globin genes in gorilla and macaque: the
RT   origin of nucleotide polymorphisms in human.";
RL   J. Mol. Evol. 24:309-318(1987).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-147.
RX   PubMed=5499429; DOI=10.1016/0005-2795(70)90216-3;
RA   Wade P.T., Barnicot N.A., Huehns E.R.;
RT   "Structural studies on the major and minor haemoglobin of the monkey Macaca
RT   irus.";
RL   Biochim. Biophys. Acta 221:450-466(1970).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 107-147.
RC   TISSUE=Blood;
RX   PubMed=10723742; DOI=10.1093/oxfordjournals.molbev.a026321;
RA   Francino M.P., Ochman H.;
RT   "Strand symmetry around the beta-globin origin of replication in
RT   primates.";
RL   Mol. Biol. Evol. 17:416-422(2000).
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; X05665; CAA29153.1; -; Genomic_DNA.
DR   EMBL; AF205410; AAF23761.1; -; Genomic_DNA.
DR   PIR; A29665; HBMQC.
DR   RefSeq; NP_001270296.1; NM_001283367.1.
DR   AlphaFoldDB; P68223; -.
DR   SMR; P68223; -.
DR   STRING; 9541.XP_005578972.1; -.
DR   GeneID; 101926697; -.
DR   eggNOG; KOG3378; Eukaryota.
DR   OrthoDB; 1370439at2759; -.
DR   Proteomes; UP000233100; 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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P02086,
FT                   ECO:0000269|PubMed:5499429"
FT   CHAIN           2..147
FT                   /note="Hemoglobin subunit beta"
FT                   /id="PRO_0000053000"
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;  16114 MW;  1F796B304891A55B CRC64;
     MVHLTPEEKN AVTTLWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS SPDAVMGNPK
     VKAHGKKVLG AFSDGLNHLD NLKGTFAQLS ELHCDKLHVD PENFKLLGNV LVCVLAHHFG
     KEFTPQVQAA YQKVVAGVAN ALAHKYH
 
 
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