HBB1_SOMMI
ID HBB1_SOMMI Reviewed; 128 AA.
AC C0HJZ3;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 1.
DT 03-AUG-2022, entry version 9.
DE RecName: Full=Hemoglobin subunit beta-1 {ECO:0000305|PubMed:29023598};
DE AltName: Full=Beta-1-globin {ECO:0000305|PubMed:29023598};
DE AltName: Full=Hemoglobin beta-1 chain {ECO:0000303|PubMed:29023598};
DE Flags: Fragments;
GN Name=HBB1 {ECO:0000305|PubMed:29023598};
OS Somniosus microcephalus (Greenland sleeper shark) (Squalus microcephalus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Squalomorphii; Squaliformes; Somniosidae; Somniosus.
OX NCBI_TaxID=191813 {ECO:0000303|PubMed:29023598};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Erythrocyte {ECO:0000303|PubMed:29023598};
RX PubMed=29023598; DOI=10.1371/journal.pone.0186181;
RA Russo R., Giordano D., Paredi G., Marchesani F., Milazzo L., Altomonte G.,
RA Del Canale P., Abbruzzetti S., Ascenzi P., di Prisco G., Viappiani C.,
RA Fago A., Bruno S., Smulevich G., Verde C.;
RT "The Greenland shark Somniosus microcephalus-Hemoglobins and ligand-binding
RT properties.";
RL PLoS ONE 12:E0186181-E0186181(2017).
CC -!- FUNCTION: Involved in oxygen transport from gills to the various
CC peripheral tissues. {ECO:0000269|PubMed:29023598}.
CC -!- SUBUNIT: Hb 1 is a heterotetramer of two alpha and two beta-1 chains.
CC {ECO:0000269|PubMed:29023598}.
CC -!- TISSUE SPECIFICITY: Red blood cells (at protein level).
CC {ECO:0000269|PubMed:29023598}.
CC -!- MISCELLANEOUS: This fish has three hemoglobins: Hb 1, Hb 2 and Hb 3.
CC They all have a similar Bohr effect. {ECO:0000269|PubMed:29023598}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR AlphaFoldDB; C0HJZ3; -.
DR SMR; C0HJZ3; -.
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 Pfam; PF00042; Globin; 1.
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..128
FT /note="Hemoglobin subunit beta-1"
FT /evidence="ECO:0000269|PubMed:29023598"
FT /id="PRO_0000443116"
FT BINDING 51
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT BINDING 74
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT NON_CONS 42..43
FT /evidence="ECO:0000303|PubMed:29023598"
FT NON_CONS 72..73
FT /evidence="ECO:0000303|PubMed:29023598"
SQ SEQUENCE 128 AA; 14484 MW; 2FE5D2E77755524B CRC64;
VHWTAEEKAL VNVVWSKTDH QAVVANALGR LFVVYPWTKR YFAGDSAVQT HAGKVVSALT
LAYNHIDDVK PHKHYEGFHV DPENFRLLAN CLNVELGHTL HKEFTPELHA AWNKFSNVVV
DALSKGYH
