HBB_MUSPF
ID HBB_MUSPF Reviewed; 146 AA.
AC P68044; P19017;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=HBB;
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae;
OC Mustela.
OX NCBI_TaxID=9669;
RN [1]
RP PROTEIN SEQUENCE.
RA Pauplin Y., Hombrados I., Faure F., Han K.K., Neuzil E.;
RT "The primary structure of the beta-chain of the haemoglobins of the ferret
RT (Mustela putorius furo).";
RL Biochem. Soc. Trans. 16:608-609(1988).
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=2610931; DOI=10.1515/bchm3.1989.370.2.1133;
RA Hombrados I., Vidal Y., Rodewald K., Braunitzer G., Neuzil E.;
RT "Carnivora: the primary structure of the alpha-chains of ferret (Mustela
RT putorius furo, Mustelidae) hemoglobins.";
RL Biol. Chem. Hoppe-Seyler 370:1133-1138(1989).
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 PIR; S11534; HBMN.
DR AlphaFoldDB; P68044; -.
DR SMR; P68044; -.
DR STRING; 9668.ENSMPUP00000010075; -.
DR eggNOG; KOG3378; Eukaryota.
DR HOGENOM; CLU_003827_10_0_1; -.
DR InParanoid; P68044; -.
DR OMA; TPDAVMN; -.
DR Proteomes; UP000000715; 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 CHAIN 1..146
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000053030"
FT BINDING 63
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 92
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 1
FT /note="N-acetylvaline"
FT /evidence="ECO:0000250|UniProtKB:P02086"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 59
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 82
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 93
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 144
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
SQ SEQUENCE 146 AA; 15994 MW; DC99326ED2F4D8A4 CRC64;
VHLTGEEKAA VTALWGKVNV DEVGGETLGR LLVVYPWTQR FFDSFGDLSS PDAVMSNPKV
KAHGKKVLNS FSEGLKNLDN LKGTFAKLSE LHCDKLHVDP ENFKLLGNVL VCVLAHHFGK
EFTPQVQAAY QKVVAGVANA LAHKYH
