HBB1_XENLA
ID HBB1_XENLA Reviewed; 146 AA.
AC P02132; Q3B895;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Hemoglobin subunit beta-1;
DE AltName: Full=Beta-1-globin;
DE AltName: Full=Hemoglobin beta-1 chain;
DE AltName: Full=Hemoglobin beta-major chain;
GN Name=hbb1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6305990; DOI=10.1016/s0021-9258(18)32083-0;
RA Patient R.K., Harris R., Walmsley M.E., Williams J.G.;
RT "The complete nucleotide sequence of the major adult beta globin gene of
RT Xenopus laevis.";
RL J. Biol. Chem. 258:8521-8523(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7433108; DOI=10.1093/nar/8.18.4247;
RA Williams J.G., Kay R.M., Patient R.K.;
RT "The nucleotide sequence of the major beta-globin mRNA from Xenopus
RT laevis.";
RL Nucleic Acids Res. 8:4247-4258(1980).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-146.
RX PubMed=6249685; DOI=10.1016/0012-1606(80)90326-7;
RA Richardson C., Cappello J., Cochran M.D., Armentrout R.W., Brown R.D.;
RT "Partial sequence analysis of Xenopus alpha- and beta-globin mRNA as
RT determined from recombinant DNA plasmids.";
RL Dev. Biol. 78:161-172(1980).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 133-146.
RX PubMed=7001356; DOI=10.1093/nar/8.12.2691;
RA Kay R.M., Harris R., Patient R.K., Williams J.G.;
RT "Molecular cloning of cDNA sequences coding for the major alpha- and beta-
RT globin polypeptides of adult Xenopus laevis.";
RL Nucleic Acids Res. 8:2691-2707(1980).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RX PubMed=3351944; DOI=10.1016/0022-2836(88)90302-6;
RA Brewer A.C., Enver T., Greaves D.R., Allan J., Patient R.K.;
RT "5' structural motifs and Xenopus beta globin gene activation.";
RL J. Mol. Biol. 199:575-585(1988).
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; M15382; AAA49641.1; -; Genomic_DNA.
DR EMBL; V01433; CAA24697.1; -; mRNA.
DR EMBL; BC106693; AAI06694.1; -; mRNA.
DR EMBL; X07164; CAA30156.1; -; Genomic_DNA.
DR EMBL; M10601; AAA49735.1; -; mRNA.
DR EMBL; J00978; AAA49734.1; -; Genomic_DNA.
DR PIR; A92432; HBXL.
DR PIR; I51430; I51430.
DR RefSeq; NP_001089816.1; NM_001096347.1.
DR AlphaFoldDB; P02132; -.
DR SMR; P02132; -.
DR DNASU; 734881; -.
DR GeneID; 734881; -.
DR KEGG; xla:734881; -.
DR CTD; 734881; -.
DR Xenbase; XB-GENE-5913262; hbg1.L.
DR OMA; TYPWTQR; -.
DR OrthoDB; 1370439at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 734881; Expressed in liver and 19 other tissues.
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 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..146
FT /note="Hemoglobin subunit beta-1"
FT /id="PRO_0000053155"
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 CONFLICT 101
FT /note="L -> A (in Ref. 4; AAA49641)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="K -> G (in Ref. 4; AAA49641)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 146 AA; 16421 MW; 4500CCBDA7748581 CRC64;
MGLTAHDRQL INSTWGKLCA KTIGQEALGR LLWTYPWTQR YFSSFGNLNS ADAVFHNEAV
AAHGEKVVTS IGEAIKHMDD IKGYYAQLSK YHSETLHVDP LNFKRFGGCL SIALARHFHE
EYTPELHAAY EHLFDAIADA LGKGYH
