HBB_CYPCA
ID HBB_CYPCA Reviewed; 147 AA.
AC P02139; Q9PRW6; Q9PRW7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Hemoglobin subunit beta-A/B;
DE AltName: Full=Hemoglobin beta-A/B chain;
DE AltName: Full=Hemoglobin subunit beta-1/2;
OS Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=7450680;
RA Grujic-Injac B., Braunitzer G., Stangl A.;
RT "Hemoglobins, XXXV. The sequence of the beta A- and beta B-Chains of the
RT hemoglobins of the carp (Cyprinus carpio L.).";
RL Hoppe-Seyler's Z. Physiol. Chem. 361:1629-1639(1980).
RN [2]
RP PROTEIN SEQUENCE OF 1-40.
RX PubMed=8014260; DOI=10.1007/bf00714576;
RA Ohkudo N., Watabe S., Oshiro T., Takashima F., Nakajima H.;
RT "Subunit structures of multiple hemoglobins in carp.";
RL J. Comp. Physiol. B 164:88-88(1994).
CC -!- FUNCTION: Involved in oxygen transport from gills to the various
CC peripheral tissues.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- POLYMORPHISM: There are two alleles. The sequence shown is that of
CC beta-A. {ECO:0000269|PubMed:7450680}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; A02459; HBCAA.
DR AlphaFoldDB; P02139; -.
DR SMR; P02139; -.
DR Proteomes; UP000694384; Unplaced.
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 Reference proteome; Transport.
FT CHAIN 1..147
FT /note="Hemoglobin subunit beta-A/B"
FT /id="PRO_0000052943"
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 VARIANT 13
FT /note="A -> G (in beta-B chain)"
FT /evidence="ECO:0000269|PubMed:7450680"
FT VARIANT 41
FT /note="F -> Y (in beta-B chain)"
FT /evidence="ECO:0000269|PubMed:7450680"
FT VARIANT 122
FT /note="G -> A (in beta-B chain)"
FT /evidence="ECO:0000269|PubMed:7450680"
FT VARIANT 143
FT /note="K -> C (in beta-B chain)"
FT /evidence="ECO:0000269|PubMed:7450680"
FT CONFLICT 26
FT /note="E -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="C -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 147 AA; 16262 MW; 464BD37A04658956 CRC64;
VEWTDAERSA IIALWGKLNP DELGPEALAR CLIVYPWTQR FFASYGNLSS PAAIMGNPKV
AAHGRTVEGG LMRAIKDMDN IKATYAPLSV MHSEKLHVDP DNFRLLADCI TVCAAMKFGP
SGFSPNVQEA WQKFLSVVVN ALKRQYH