ID   HBB2_TAPTE              Reviewed;         146 AA.
AC   P02065;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Hemoglobin subunit beta-2;
DE   AltName: Full=Beta-2-globin;
DE   AltName: Full=Hemoglobin beta-2 chain;
DE   AltName: Full=Hemoglobin beta-minor chain;
GN   Name=HBB2;
OS   Tapirus terrestris (Lowland tapir) (Brazilian tapir).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Tapiridae; Tapirus.
OX   NCBI_TaxID=9801;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6149994;
RA   Mazur G., Braunitzer G.;
RT   "Perissodactyla: the primary structure of hemoglobins from the lowland
RT   tapir (Tapirus terrestris): glutamic acid in position 2 of the beta
RT   chains.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 365:1097-1106(1984).
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; A02383; HBTPN.
DR   AlphaFoldDB; P02065; -.
DR   SMR; P02065; -.
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   Methylation; Oxygen transport; Phosphoprotein; Transport.
FT   CHAIN           1..146
FT                   /note="Hemoglobin subunit beta-2"
FT                   /id="PRO_0000053125"
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         17
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02089"
FT   MOD_RES         44
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P02089"
FT   MOD_RES         59
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P02089"
FT   MOD_RES         104
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P02089"
FT   MOD_RES         123
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P11517"
SQ   SEQUENCE   146 AA;  16004 MW;  D4EE027FF554A271 CRC64;
     VHLHGDEKAA VLALWDKVDE EKVGGEALGR LLVVYPWTQR FFDSFGDLST AAAVMGNPKV
     KAHGKKVLHS FGEGVHHLDD LKVTFAQLSE LHCDKLHVDP ENFRLLGNVL VVVLAQQFGK
     AFTPELQAAY QKVVAGVASA LAHKYH