HBBC_SHEEP
ID HBBC_SHEEP Reviewed; 142 AA.
AC P68056; P02079;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Hemoglobin subunit beta-C;
DE AltName: Full=Beta-C-globin;
DE AltName: Full=Hemoglobin beta-C chain;
GN Name=HBBC;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2494347; DOI=10.1007/bf02102474;
RA Garner K.J., Lingrel J.B.;
RT "A comparison of the beta A- and beta B-globin gene clusters of sheep.";
RL J. Mol. Evol. 28:175-184(1989).
RN [2]
RP PROTEIN SEQUENCE OF 2-142.
RC STRAIN=Rambouillet;
RA Wilson J.B., Edwards W.C., McDaniel M., Dobbs M.M., Huisman T.H.J.;
RT "The structure of sheep hemoglobins. II. The amino acid composition of the
RT tryptic peptides of the non-alpha chains of hemoglobins A, B, C, and F.";
RL Arch. Biochem. Biophys. 115:385-400(1966).
RN [3]
RP PROTEIN SEQUENCE OF 2-142.
RC STRAIN=Dorset;
RX PubMed=6022868; DOI=10.1016/s0021-9258(18)96038-2;
RA Boyer S.H., Hathaway P., Pascasio F., Bordley J., Orton C., Naughton M.A.;
RT "Differences in the amino acid sequences of tryptic peptides from three
RT sheep hemoglobin beta chains.";
RL J. Biol. Chem. 242:2211-2232(1967).
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 -!- MISCELLANEOUS: This type of beta-C chain is found when anemia has been
CC experimentally produced.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; X14728; CAA32850.1; -; Genomic_DNA.
DR PIR; S10074; HBSHC.
DR RefSeq; NP_001106896.1; NM_001113425.1.
DR AlphaFoldDB; P68056; -.
DR SMR; P68056; -.
DR GeneID; 100134870; -.
DR KEGG; oas:100134870; -.
DR Proteomes; UP000002356; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6022868, ECO:0000269|Ref.2"
FT CHAIN 2..142
FT /note="Hemoglobin subunit beta-C"
FT /id="PRO_0000053106"
FT BINDING 59
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 88
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 83
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 142 AA; 15750 MW; 1539EDCBF4394B37 CRC64;
MPNKALITGF WSKVKVDEVG AEALGRLLVV YPWTQRFFEH FGDLSTADAV LGNAKVKAHG
KKVLDSFSNG VQHLDDLKGT FAQLSELHCD KLHVDPENFR LLGNVLVVVL ARHFGKEFTP
ELQAEFQKVV AGVASALAHR YH
