HBB_DIDVI
ID HBB_DIDVI Reviewed; 147 AA.
AC P02109;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Hemoglobin subunit beta-M;
DE AltName: Full=Beta-M-globin;
DE AltName: Full=Hemoglobin beta-M chain;
GN Name=HBB;
OS Didelphis virginiana (North American opossum) (Didelphis marsupialis
OS virginiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Didelphis.
OX NCBI_TaxID=9267;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3375246; DOI=10.1073/pnas.85.11.3893;
RA Koop B., Goodman M.;
RT "Evolutionary and developmental aspects of two hemoglobin beta-chain genes
RT (epsilon M and beta M) of opossum.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:3893-3897(1988).
RN [2]
RP PROTEIN SEQUENCE OF 2-147.
RX PubMed=422568; DOI=10.1016/s0021-9258(17)37767-0;
RA Stenzel P., Brimhall B., Jones R.T., Black J.A., McLachlan A., Gibson D.;
RT "Opossum hemoglobin. The amino acid sequences of the alpha and beta
RT chains.";
RL J. Biol. Chem. 254:2071-2076(1979).
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; J03643; AAA30976.1; -; Genomic_DNA.
DR PIR; B30213; HBOP.
DR AlphaFoldDB; P02109; -.
DR SMR; P02109; -.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02086,
FT ECO:0000269|PubMed:422568"
FT CHAIN 2..147
FT /note="Hemoglobin subunit beta-M"
FT /id="PRO_0000052948"
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 81
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 147 AA; 16211 MW; CC96BB87F2CF13AB CRC64;
MVHLTSEEKN CITTIWSKVQ VDQTGGEALG RMLVVYPWTT RFFGSFGDLS SPGAVMSNSK
VQAHGAKVLT SFGEAVKHLD NLKGTYAKLS ELHCDKLHVD PENFKMLGNI IVICLAEHFG
KDFTPECQVA WQKLVAGVAH ALAHKYH
