HBB3_LITCT
ID HBB3_LITCT Reviewed; 147 AA.
AC P02136;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Hemoglobin subunit beta-3;
DE AltName: Full=Beta-3-globin;
DE AltName: Full=Hemoglobin beta-3 chain;
DE AltName: Full=Hemoglobin beta-III chain, larval;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2449437; DOI=10.1016/s0021-9258(18)69035-0;
RA Dickey L.F., Wang Y.H., Shull G.E., Wortman I.A. III, Theil E.C.;
RT "The importance of the 3'-untranslated region in the translational control
RT of ferritin mRNA.";
RL J. Biol. Chem. 263:3071-3074(1988).
RN [2]
RP PROTEIN SEQUENCE OF 2-147.
RX PubMed=6965940; DOI=10.1016/s0021-9258(19)85698-3;
RA Watt K.W.K., Maruyama T., Riggs A.F.;
RT "Hemoglobins of the tadpole of the bullfrog, Rana catesbeiana. Amino acid
RT sequence of the beta chain of a major component.";
RL J. Biol. Chem. 255:3294-3301(1980).
CC -!- FUNCTION: This is a tadpole (larval) beta chain.
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; M19548; AAA49526.1; -; mRNA.
DR PIR; A02456; HBFG3T.
DR PIR; I51168; I51168.
DR AlphaFoldDB; P02136; -.
DR SMR; P02136; -.
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 Direct protein sequencing; Heme; Iron; Metal-binding; Oxygen transport;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6965940"
FT CHAIN 2..147
FT /note="Hemoglobin subunit beta-3"
FT /id="PRO_0000053087"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
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"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT CONFLICT 57
FT /note="G -> T (in Ref. 1; AAA49526)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="N -> H (in Ref. 1; AAA49526)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="D -> N (in Ref. 1; AAA49526)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="A -> E (in Ref. 1; AAA49526)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="H -> Q (in Ref. 1; AAA49526)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 147 AA; 16478 MW; 7088A793CAEF3810 CRC64;
MVHWTAEEKA VINSVWQKVD VEQDGHEALT RLFIVYPWTQ RYFSTFGDLS SPAAIAGNPK
VHAHGKKILG AIDNAIHNLD DVKGTLHDLS EEHANELHVD PENFRRLGEV LIVVLGAKLG
KAFSPQVQHV WEKFIAVLVD ALSHSYH
