HBB3_SOMMI
ID HBB3_SOMMI Reviewed; 135 AA.
AC C0HJZ5;
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-3 {ECO:0000305|PubMed:29023598};
DE AltName: Full=Beta-3-globin {ECO:0000305|PubMed:29023598};
DE AltName: Full=Hemoglobin beta-3 chain {ECO:0000303|PubMed:29023598};
DE Flags: Fragments;
GN Name=HBB3 {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 3 is a heterotetramer of two alpha and two beta-3 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; C0HJZ5; -.
DR SMR; C0HJZ5; -.
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..135
FT /note="Hemoglobin subunit beta-3"
FT /evidence="ECO:0000269|PubMed:29023598"
FT /id="PRO_0000443118"
FT BINDING 57
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:0000250|UniProtKB:P02070"
FT BINDING 81
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:0000250|UniProtKB:P02070"
FT NON_CONS 48..49
FT /evidence="ECO:0000303|PubMed:29023598"
FT NON_CONS 78..79
FT /evidence="ECO:0000303|PubMed:29023598"
SQ SEQUENCE 135 AA; 15287 MW; D94EA64FD8F70A0C CRC64;
VHWTAEEKAL VNVVWSKTDH QAVVANALGR LFVVYPWTKT YFTKFNGKAG DSTVQTHAGK
VVSALTLAYN HIDDVKPHFK HYEGFHVDPE NFRLLANCLN VELGHTLHKE FTPELHAAWN
KFSNVVVDAL SKAYQ
