HBB2_PANON
ID HBB2_PANON Reviewed; 147 AA.
AC P68064; P10884;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Hemoglobin subunit beta-2;
DE AltName: Full=Beta-2-globin;
DE AltName: Full=Hemoglobin beta-2 chain;
GN Name=HBB2;
OS Panthera onca (Jaguar) (Felis onca).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Pantherinae;
OC Panthera.
OX NCBI_TaxID=9690;
RN [1]
RP PROTEIN SEQUENCE OF 2-147.
RX PubMed=3426807; DOI=10.1515/bchm3.1987.368.2.1385;
RA Ahmed A., Jahan M., Zaidi Z.H., Braunitzer G., Goeltenboth R.;
RT "The primary structure of the hemoglobins of the adult jaguar (Panthera
RT onco, Carnivora).";
RL Biol. Chem. Hoppe-Seyler 368:1385-1390(1987).
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 -!- MISCELLANEOUS: In the cat family (felidae), the oxygen affinity of
CC hemoglobin depends little or not at all on the association with
CC diphosphoglycerate (DPG).
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; S00522; HBJU.
DR AlphaFoldDB; P68064; -.
DR SMR; P68064; -.
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 Direct protein sequencing; Heme; Iron; Metal-binding; Methylation;
KW Oxygen transport; Phosphoprotein; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3426807"
FT CHAIN 2..147
FT /note="Hemoglobin subunit beta-2"
FT /id="PRO_0000053055"
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 18
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02089"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02089"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02091"
FT MOD_RES 60
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P02089"
FT MOD_RES 105
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P02089"
SQ SEQUENCE 147 AA; 16129 MW; 91A7DB9B4F0CBD3B CRC64;
MGFLSAEEKG LVNGLWSKVN VDEVGGEALG RLLVVYPWTQ RFFQSFGDLS SADAIMSNAK
VKAHGKKVLN SFSDGLKNID DLKGAFAKLS ELHCDKLHVD PENFRLLGNV LVCVLAHHFG
HEFNPQVQAA FQKVVAGVAK ALAHRYH
