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HBB2_SOMMI
ID   HBB2_SOMMI              Reviewed;         135 AA.
AC   C0HJZ4;
DT   28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2018, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Hemoglobin subunit beta-2 {ECO:0000305|PubMed:29023598};
DE   AltName: Full=Beta-2-globin {ECO:0000305|PubMed:29023598};
DE   AltName: Full=Hemoglobin beta-2 chain {ECO:0000303|PubMed:29023598};
DE   Flags: Fragments;
GN   Name=HBB2 {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 2 is a heterotetramer of two alpha and two beta-2 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; C0HJZ4; -.
DR   SMR; C0HJZ4; -.
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-2"
FT                   /evidence="ECO:0000269|PubMed:29023598"
FT                   /id="PRO_0000443117"
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        79..80
FT                   /evidence="ECO:0000303|PubMed:29023598"
SQ   SEQUENCE   135 AA;  15252 MW;  3B7EB8F5695C10BD CRC64;
     VHWTAEEKAL VNVVWSKTDH QAVVANALGR LFVVYPWTKT YFTKFNGKAG DSAVQTHAGK
     VVSALTLAYN HIDDVKPHFK HYEGFHVDPE NFRLLANCLN VELGHTLHKE FTPELHAAWN
     KFSNVVVDAL SKGYH
 
 
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