HBB_AILME
ID HBB_AILME Reviewed; 147 AA.
AC P18983; Q5XLE6;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=HBB;
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA He P., Fang S.;
RT "Construction of the liver and brain cDNA libraries of the giant panda.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-147.
RX PubMed=3762727; DOI=10.1007/bf00367205;
RA Tagle D.A., Miyamoto M.M., Goodman M., Hofmann O., Braunitzer G.,
RA Goeltenboth R., Jalanka H.;
RT "Hemoglobin of pandas: phylogenetic relationships of carnivores as
RT ascertained with protein sequence data.";
RL Naturwissenschaften 73:512-514(1986).
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; AY753985; AAV28720.1; -; mRNA.
DR PIR; S06529; HBFQG.
DR RefSeq; NP_001291812.1; NM_001304883.1.
DR AlphaFoldDB; P18983; -.
DR SMR; P18983; -.
DR STRING; 9646.ENSAMEP00000014174; -.
DR GeneID; 100499573; -.
DR KEGG; aml:100499573; -.
DR eggNOG; KOG3378; Eukaryota.
DR HOGENOM; CLU_003827_10_0_1; -.
DR InParanoid; P18983; -.
DR OMA; TPDAVMN; -.
DR OrthoDB; 1370439at2759; -.
DR TreeFam; TF333268; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
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:3762727"
FT CHAIN 2..147
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000052859"
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 108
FT /note="G -> S (in Ref. 1; AAV28720)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 147 AA; 16153 MW; 30B99C14DB574EA2 CRC64;
MVHLTGEEKA AVTGLWSKVN VDEVGGEALG RLLVVYPWTQ RFFDSFGDLS TPDAVMNNPK
VKAHGKKVLN SFSEGLKNLD NLKGTFAKLS ELHCDKLHVD PENFKLLGNV LVCVLAHHFG
KEFTPQVQAA YQKVVAGVAN ALAHKYH
