ID   HBBB_CATCL              Reviewed;          48 AA.
AC   P85313;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Hemoglobin subunit beta-B;
DE   AltName: Full=Beta-B-globin;
DE   AltName: Full=Hemoglobin beta-B chain;
DE   Flags: Fragment;
GN   Name=hbbb {ECO:0000250|UniProtKB:P02140, ECO:0000303|PubMed:5076774};
OS   Catostomus clarkii (Desert sucker).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Catostomoidei; Catostomidae; Catostomus.
OX   NCBI_TaxID=7970;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND SUBUNIT.
RC   TISSUE=Blood {ECO:0000269|PubMed:5076774};
RX   PubMed=5076774; DOI=10.1016/s0021-9258(19)44746-7;
RA   Powers D.A., Edmundson A.B.;
RT   "Multiple hemoglobins of catostomid fish. I. Isolation and characterization
RT   of the isohemoglobins from Catostomus clarkii.";
RL   J. Biol. Chem. 247:6686-6693(1972).
CC   -!- FUNCTION: Involved in oxygen transport from gills to the various
CC       peripheral tissues. {ECO:0000305}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC       {ECO:0000269|PubMed:5076774}.
CC   -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC   -!- MISCELLANEOUS: This fish has ten hemoglobins, 8 of which are anodal and
CC       2 cathodal. The cathodal tetramers do not exhibit the Bohr effect, due
CC       to lack of the C-terminal His in the beta chains and to blocking of the
CC       alpha-amino group on the N-terminal residue of the alpha chains. The
CC       possession of both anodal and cathodal hemoglobins may be a
CC       physiological advantage for fish living in fast-moving water habitats.
CC       {ECO:0000269|PubMed:5076774}.
CC   -!- MISCELLANEOUS: This fish possesses 6 types of hemoglobin chains,
CC       including a major alpha chain, a minor alpha chain, two major beta
CC       chains, and two minor beta chains. {ECO:0000269|PubMed:5076774}.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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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   Gene3D; 1.10.490.10; -; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
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..48
FT                   /note="Hemoglobin subunit beta-B"
FT                   /id="PRO_0000312766"
FT   NON_TER         48
FT                   /evidence="ECO:0000303|PubMed:5076774"
SQ   SEQUENCE   48 AA;  5400 MW;  ACD30ECD8790C850 CRC64;
     VEWTDAERGA ILSLWGKIDP DELGPALLAR XXLVYXXTQR YFASFGDL