ID   HBBC_OVIMU              Reviewed;         141 AA.
AC   P68057; P02079;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
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 musimon (Mouflon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9938;
RN   [1]
RP   PARTIAL PROTEIN SEQUENCE, AND AMINO-ACID COMPOSITION OF TRYPTIC PEPTIDES.
RX   PubMed=5496230; DOI=10.1007/bf00486382;
RA   Wilson J.B., Miller A., Huisman T.H.J.;
RT   "Production of hemoglobin C in the Moufflon (Ovis musimon Pallas, 1811) and
RT   the Barbary sheep (Ammotragus lervia Pallas, 1777) during experimental
RT   anemia: amino acid composition of tryptic peptides from the beta B and beta
RT   C chains.";
RL   Biochem. Genet. 4:677-688(1970).
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   PIR; A90232; HBMFC.
DR   AlphaFoldDB; P68057; -.
DR   SMR; P68057; -.
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   CHAIN           1..141
FT                   /note="Hemoglobin subunit beta-C"
FT                   /id="PRO_0000053045"
FT   BINDING         58
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         87
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   UNSURE          64
FT   UNSURE          68
FT   UNSURE          71
FT   UNSURE          74..75
FT   UNSURE          82
FT   UNSURE          85
FT   UNSURE          94
FT   UNSURE          96..97
FT   UNSURE          103
SQ   SEQUENCE   141 AA;  15619 MW;  3409EDB54528C358 CRC64;
     PNKALITGFW SKVKVDEVGA EALGRLLVVY PWTQRFFEHF GDLSTADAVL GNAKVKAHGK
     KVLDSFSNGV QHLDDLKGTF AQLSELHCDK LHVDPENFRL LGNVLVVVLA RHFGKEFTPE
     LQAEFQKVVA GVASALAHRY H