HBB_PERCR
ID HBB_PERCR Reviewed; 146 AA.
AC B3EWD4;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Hemoglobin subunit beta {ECO:0000303|PubMed:22718635};
OS Peromyscus crinitus (Canyon mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Neotominae; Peromyscus.
OX NCBI_TaxID=144753;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
RC TISSUE=Erythrocyte {ECO:0000269|PubMed:22718635};
RX PubMed=22718635; DOI=10.1515/hsz-2011-0196;
RA Laskay U.A., Burg J., Kaleta E.J., Vilcins I.M., Telford Iii S.R.,
RA Barbour A.G., Wysocki V.H.;
RT "Development of a host blood meal database: de novo sequencing of
RT hemoglobin from nine small mammals using mass spectrometry.";
RL Biol. Chem. 393:195-201(2012).
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues. {ECO:0000305}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR AlphaFoldDB; B3EWD4; -.
DR SMR; B3EWD4; -.
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 CHAIN 1..146
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000415596"
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 /evidence="ECO:0000250|UniProtKB:P02070,
FT ECO:0000255|PROSITE-ProRule:PRU00238"
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 /evidence="ECO:0000250|UniProtKB:P02070,
FT ECO:0000255|PROSITE-ProRule:PRU00238"
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"
FT UNSURE 3
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 10
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 14
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 23
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 28
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 31
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 32
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 48
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 54
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 68
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 75
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 78
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 81
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 88
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 91
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 96
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 105
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 106
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 110
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 112
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 118
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
FT UNSURE 141
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:22718635"
SQ SEQUENCE 146 AA; 15807 MW; 875BF22808E2B8BC CRC64;
VHLTDAEKAL VTGLWGKVKP DELGGEALGR LLGVYPWTQR FFDSFGDLSS ASALMSNAKV
KAHGKKVLDS FSEGLKHLDN LKGTFASLSE LHCDKLHVDP ENFKLLGNML VLVMAHHLGK
DFTPAAQAAY QKVVAGVATA LAHKYH
