ID   HBB_CRONI               Reviewed;         146 AA.
AC   P02129;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Hemoglobin subunit beta;
DE   AltName: Full=Beta-globin;
DE   AltName: Full=Hemoglobin beta chain;
GN   Name=HBB;
OS   Crocodylus niloticus (Nile crocodile) (African crocodile).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Longirostres; Crocodylidae;
OC   Crocodylus.
OX   NCBI_TaxID=8501;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6286445;
RA   Leclercq F., Schnek A.G., Braunitzer G., Stangl A., Schrank B.;
RT   "Direct reciprocal allosteric interaction of oxygen and hydrogen carbonate
RT   sequence of the haemoglobins of the Caiman (Caiman crocodylus), the Nile
RT   crocodile (Crocodylus niloticus) and the Mississippi crocodile (Alligator
RT   mississippiensis).";
RL   Hoppe-Seyler's Z. Physiol. Chem. 362:1151-1158(1981).
RN   [2]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT ALA-1.
RX   PubMed=7303821;
RA   Schaefer W., Braunitzer G., Stangl A.;
RT   "Direct allosteric interaction of oxygen and bicarbonate: N-acetyl-alanyl-
RT   seryl-phenylalanine, N-terminal sequence of the beta-chains of the
RT   haemoglobins of Nil crocodile (Crocodylusniloticus) and Mississippi
RT   crocodile (Alligator mississippiensis).";
RL   Z. Naturforsch. C 36:902-903(1981).
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; A91695; HBAK.
DR   AlphaFoldDB; P02129; -.
DR   SMR; P02129; -.
DR   iPTMnet; P02129; -.
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; Transport.
FT   CHAIN           1..146
FT                   /note="Hemoglobin subunit beta"
FT                   /id="PRO_0000052937"
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-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:7303821"
SQ   SEQUENCE   146 AA;  16437 MW;  0747C5B2E7E88BFB CRC64;
     ASFDPHEKQL IGDLWHKVDV AHCGGEALSR MLIVYPWKRR YFENFGDISN AQAIMHNEKV
     QAHGKKVLAS FGEAVCHLDG IRAHFANLSK LHCEKLHVDP ENFKLLGDII IIVLAAHYPK
     DFGLECHAAY QKLVRQVAAA LAAEYH