HBA_SOMMI
ID HBA_SOMMI Reviewed; 124 AA.
AC C0HJZ2;
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 alpha {ECO:0000250|UniProtKB:P01966};
DE AltName: Full=Alpha-globin {ECO:0000250|UniProtKB:P01966};
DE AltName: Full=Hemoglobin alpha chain {ECO:0000303|PubMed:29023598};
DE Flags: Fragments;
GN Name=HBA {ECO:0000250|UniProtKB:P01966};
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 Hb 2 is a heterotetramer of two alpha and two beta-2 chains. Hb 3 is a
CC 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; C0HJZ2; -.
DR SMR; C0HJZ2; -.
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..124
FT /note="Hemoglobin subunit alpha"
FT /id="PRO_0000443119"
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:0000255|PROSITE-ProRule:PRU00238"
FT BINDING 79
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 57..58
FT /evidence="ECO:0000303|PubMed:29023598"
FT NON_CONS 74..75
FT /evidence="ECO:0000303|PubMed:29023598"
FT NON_CONS 105..106
FT /evidence="ECO:0000303|PubMed:29023598"
SQ SEQUENCE 124 AA; 13391 MW; A1FD070A92BC8034 CRC64;
PLSAADKTII KHLTGSVRTN AEAWGAESLA RLFATSPSTK TYFSKFNDFT ANGKRLHGGK
VLNAVADVTD HLDNLAVLHG TTLLVDPHNF PLLSQSLLVT LAAHLLALDK FLDEVAKALS
SHYR
