ID HBB2_TRICR Reviewed; 145 AA. AC P10786; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 14-DEC-2022, entry version 89. 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 Triturus cristatus (Great crested newt) (Warty newt). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Caudata; Salamandroidea; Salamandridae; Pleurodelinae; Triturus. OX NCBI_TaxID=8323; RN [1] RP PROTEIN SEQUENCE. RX PubMed=3242554; DOI=10.1515/bchm3.1988.369.2.1343; RA Kleinschmidt T., Sgouros J.G., Braunitzer G.; RT "The first sequenced normal hemoglobin lacking histidine in position 146 of RT the beta-chains. The primary structures of the major and minor hemoglobin RT components of the great crested newt (Triturus cristatus, Urodela, RT Amphibia)."; RL Biol. Chem. Hoppe-Seyler 369:1343-1360(1988). CC -!- FUNCTION: Involved in oxygen transport from the lung to the various CC peripheral tissues. CC -!- SUBUNIT: Minor hemoglobin is a tetramer of two alpha-2 chains and two CC beta-2 chains. CC -!- TISSUE SPECIFICITY: Red blood cells. CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE- CC ProRule:PRU00238}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR PIR; S02027; S02027. DR AlphaFoldDB; P10786; -. DR SMR; P10786; -. 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; Globin-like; 1. DR PROSITE; PS01033; GLOBIN; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Heme; Iron; Metal-binding; Oxygen transport; KW Transport. FT CHAIN 1..145 FT /note="Hemoglobin subunit beta-2" FT /id="PRO_0000053139" 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" SQ SEQUENCE 145 AA; 16218 MW; 04C8F25E427BAAC5 CRC64; VHLTAEDRKE IAAILGKVNV DSLGGQCLAR LIVVNPWSRR YFHDFGDLSS CDAICRNPKV LAHGAKVMRS IVEATKHLDN LREYYADLSV THSLKFYVDP ENFKLFSGIV IVCLALTLQT DFSCHKQLAF EKLMKGVSHA LGHGY //