ID   HBB1_XENTR              Reviewed;         147 AA.
AC   P07429; Q5I0S7;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Hemoglobin subunit beta-1;
DE   AltName: Full=Beta-1-globin;
DE   AltName: Full=Hemoglobin beta-1 chain;
GN   Name=hbb1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3100812; DOI=10.1007/bf02115578;
RA   Knoechel W., Korge E., Basner A., Meyerhof W.;
RT   "Globin evolution in the genus Xenopus: comparative analysis of cDNAs
RT   coding for adult globin polypeptides of Xenopus borealis and Xenopus
RT   tropicalis.";
RL   J. Mol. Evol. 23:211-223(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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   EMBL; M32457; AAA49659.1; -; mRNA.
DR   EMBL; BC088022; AAH88022.1; -; mRNA.
DR   PIR; B25929; B25929.
DR   RefSeq; NP_988859.1; NM_203528.2.
DR   AlphaFoldDB; P07429; -.
DR   SMR; P07429; -.
DR   PaxDb; P07429; -.
DR   Ensembl; ENSXETT00000054566; ENSXETP00000054566; ENSXETG00000025667.
DR   GeneID; 394453; -.
DR   KEGG; xtr:394453; -.
DR   CTD; 3047; -.
DR   Xenbase; XB-GENE-5912896; hbg1.
DR   eggNOG; KOG3378; Eukaryota.
DR   HOGENOM; CLU_003827_10_0_1; -.
DR   InParanoid; P07429; -.
DR   OMA; TYPWTQR; -.
DR   OrthoDB; 1370439at2759; -.
DR   PhylomeDB; P07429; -.
DR   TreeFam; TF333268; -.
DR   Reactome; R-XTR-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR   Reactome; R-XTR-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR   Reactome; R-XTR-2168880; Scavenging of heme from plasma.
DR   Reactome; R-XTR-6798695; Neutrophil degranulation.
DR   Reactome; R-XTR-9707564; Cytoprotection by HMOX1.
DR   Reactome; R-XTR-9707616; Heme signaling.
DR   Proteomes; UP000008143; Chromosome 9.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000025667; Expressed in liver and 14 other tissues.
DR   GO; GO:0031838; C:haptoglobin-hemoglobin complex; IBA:GO_Central.
DR   GO; GO:0005833; C:hemoglobin complex; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043177; F:organic acid binding; IBA:GO_Central.
DR   GO; GO:0019825; F:oxygen binding; IBA:GO_Central.
DR   GO; GO:0005344; F:oxygen carrier activity; IBA:GO_Central.
DR   GO; GO:0098869; P:cellular oxidant detoxification; IEA:GOC.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Heme; Iron; Metal-binding; Oxygen transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..147
FT                   /note="Hemoglobin subunit beta-1"
FT                   /id="PRO_0000053158"
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"
SQ   SEQUENCE   147 AA;  16483 MW;  107457F9258A26B6 CRC64;
     MVNLTAKERQ LITGTWSKIC AKTLGKQALG SMLYTYPWTQ RYFSSFGNLS SIEAIFHNAA
     VATHGEKVLT SIGEAIKHMD DIKGYYAQLS KYHSETLHVD PYNFKRFCSC TIISMAQTLQ
     EDFTPELQAA FEKLFAAIAD ALGKGYH