ID HBB2_TRICR STANDARD; PRT; 145 AA. AC P10786; DT 01-JUL-1989 (Rel. 11, Created) DT 01-JUL-1989 (Rel. 11, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Hemoglobin beta-2 chain (Minor). GN HBB2. OS Triturus cristatus (Great crested newt) (Warty newt). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Caudata; Salamandroidea; Salamandridae; OC Triturus. OX NCBI_TaxID=8323; RN [1] RP SEQUENCE. RX MEDLINE=89207117; PubMed=3242554; RA Kleinschmidt T., Sgouros J.G., Braunitzer G.; RT "The first sequenced normal hemoglobin lacking histidine in position RT 146 of the beta-chains. The primary structures of the major and minor RT hemoglobin components of the great crested newt (Triturus cristatus, RT Urodela, Amphibia)."; RL Biol. Chem. Hoppe-Seyler 369:1343-1360(1988). CC -!- FUNCTION: INVOLVED IN OXYGEN TRANSPORT FROM THE LUNG TO THE CC VARIOUS PERIPHERAL TISSUES. CC -!- SUBUNIT: MINOR HEMOGLOBIN IS A TETRAMER OF TWO ALPHA-2 CHAINS AND CC TWO BETA-2 CHAINS. CC -!- TISSUE SPECIFICITY: Red blood cells. CC -!- SIMILARITY: BELONGS TO THE GLOBIN FAMILY. 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 HSSP; P02070; 1FSX. DR InterPro; IPR000971; Globin. DR Pfam; PF00042; globin; 1. DR PROSITE; PS01033; GLOBIN; 1. KW Heme; Oxygen transport; Transport; Erythrocyte. FT METAL 63 63 IRON (HEME DISTAL LIGAND). FT METAL 92 92 IRON (HEME PROXIMAL LIGAND). SQ SEQUENCE 145 AA; 16218 MW; 04C8F25E427BAAC5 CRC64; VHLTAEDRKE IAAILGKVNV DSLGGQCLAR LIVVNPWSRR YFHDFGDLSS CDAICRNPKV LAHGAKVMRS IVEATKHLDN LREYYADLSV THSLKFYVDP ENFKLFSGIV IVCLALTLQT DFSCHKQLAF EKLMKGVSHA LGHGY //