HBBC_TRENE
ID HBBC_TRENE Reviewed; 146 AA.
AC P45721;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Hemoglobin subunit beta-C;
DE AltName: Full=Beta-C-globin;
DE AltName: Full=Hemoglobin beta-C chain;
OS Trematomus newnesi (Dusky notothen).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Trematomus.
OX NCBI_TaxID=35730;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND SUBUNIT.
RX PubMed=8144556; DOI=10.1016/s0021-9258(17)36935-1;
RA D'Avino R., Caruso C., Tamburrini M., Romano M., Rutigliano B.,
RA Polverino de Laureto P., Camardella L., Carratore V., di Prisco G.;
RT "Molecular characterization of the functionally distinct hemoglobins of the
RT Antarctic fish Trematomus newnesi.";
RL J. Biol. Chem. 269:9675-9681(1994).
CC -!- FUNCTION: Involved in oxygen transport from gills to the various
CC peripheral tissues. {ECO:0000269|PubMed:8144556}.
CC -!- SUBUNIT: HbC is a heterotetramer of two alpha-1 chains and two beta-C
CC chains. {ECO:0000269|PubMed:8144556}.
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- MISCELLANEOUS: This fish has three hemoglobins: Hb1 (major, about 65-
CC 70% of the total), Hb2 (about 5% of the total) and HbC (about 20-25% of
CC the total).
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; D54403; D54403.
DR PDB; 2AA1; X-ray; 1.80 A; B/D=1-146.
DR PDBsum; 2AA1; -.
DR AlphaFoldDB; P45721; -.
DR SMR; P45721; -.
DR EvolutionaryTrace; P45721; -.
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 3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxygen transport; Transport.
FT CHAIN 1..146
FT /note="Hemoglobin subunit beta-C"
FT /id="PRO_0000053137"
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 HELIX 5..17
FT /evidence="ECO:0007829|PDB:2AA1"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:2AA1"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:2AA1"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:2AA1"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:2AA1"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:2AA1"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:2AA1"
FT HELIX 81..94
FT /evidence="ECO:0007829|PDB:2AA1"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:2AA1"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:2AA1"
FT HELIX 124..142
FT /evidence="ECO:0007829|PDB:2AA1"
SQ SEQUENCE 146 AA; 16260 MW; 9C05E8B66E092979 CRC64;
VEWTDFERAT IKDIFSKLEY DVVGPATLAR CLVVYPWTQR YFGKFGNLYN AAAIAQNAMV
SKHGTTILNG LDRAVKNMDD ITNTYAELSV LHSEKLHVDP DNFKLLADCL TIVVAARFGS
AFTGEVQAAF QKFMAVVVSS LGKQYR
