HBAC_OPHSE
ID HBAC_OPHSE Reviewed; 142 AA.
AC B3EWR7;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Hemoglobin cathodic subunit alpha {ECO:0000303|PubMed:23632627};
DE AltName: Full=Hemoglobin cathodic alpha chain {ECO:0000303|PubMed:23632627};
OS Ophisurus serpens (Serpent eel) (Muraena serpens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Ophichthidae;
OC Ophisurus.
OX NCBI_TaxID=1234705;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND
RP ACETYLATION AT SER-1.
RC TISSUE=Erythrocyte {ECO:0000269|PubMed:23632627};
RX PubMed=23632627; DOI=10.1007/s00360-013-0759-y;
RA Manconi B., Pellegrini M., Messana I., Sanna M.T., Castagnola M.,
RA Iavarone F., Coluccia E., Giardina B., Olianas A.;
RT "The hemoglobin system of the serpent eel Ophisurus serpens: structural and
RT functional characterization.";
RL J. Comp. Physiol. B 183:905-919(2013).
CC -!- FUNCTION: Involved in oxygen transport from the gills to various
CC peripheral tissues. {ECO:0000305|PubMed:23632627}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC {ECO:0000250|UniProtKB:P29623}.
CC -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000269|PubMed:23632627}.
CC -!- PTM: Acetylated on Ser-1. {ECO:0000269|PubMed:23632627}.
CC -!- MASS SPECTROMETRY: Mass=15345; Mass_error=3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:23632627};
CC -!- MISCELLANEOUS: This fish has two types of hemoglobin: one cathodic Hb
CC and four anodic Hbs. The cathodic Hb displays a small normal Bohr
CC effect and a reverse Bohr effect in the presence and absence of
CC phosphate respectively. In addition, the cathodic Hb displays a large
CC phosphate effect. {ECO:0000269|PubMed:23632627}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR iPTMnet; B3EWR7; -.
DR GO; GO:0005833; C:hemoglobin complex; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR CDD; cd08927; Hb-alpha-like; 1.
DR Gene3D; 1.10.490.10; -; 1.
DR InterPro; IPR000971; Globin.
DR InterPro; IPR009050; Globin-like_sf.
DR InterPro; IPR012292; Globin/Proto.
DR InterPro; IPR002338; Hemoglobin_a-typ.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR00612; ALPHAHAEM.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxygen transport; Transport.
FT CHAIN 1..142
FT /note="Hemoglobin cathodic subunit alpha"
FT /id="PRO_0000423887"
FT BINDING 59
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:P29623,
FT ECO:0000255|PROSITE-ProRule:PRU00238"
FT BINDING 88
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:P29623,
FT ECO:0000255|PROSITE-ProRule:PRU00238"
FT MOD_RES 1
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:23632627"
FT UNSURE 2
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:23632627"
FT UNSURE 17
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:23632627"
FT UNSURE 29
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:23632627"
FT UNSURE 49
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:23632627"
FT UNSURE 62
FT /note="I or L"
FT /evidence="ECO:0000269|PubMed:23632627"
FT UNSURE 63
FT /note="I or L"
FT /evidence="ECO:0000269|PubMed:23632627"
FT UNSURE 74
FT /note="I or L"
FT /evidence="ECO:0000269|PubMed:23632627"
FT UNSURE 77
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:23632627"
FT UNSURE 81
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:23632627"
FT UNSURE 84
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:23632627"
FT UNSURE 87
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:23632627"
FT UNSURE 92
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:23632627"
FT UNSURE 107
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:23632627"
FT UNSURE 110
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:23632627"
FT UNSURE 122
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:23632627"
FT UNSURE 126
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:23632627"
FT UNSURE 137
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:23632627"
SQ SEQUENCE 142 AA; 15220 MW; 7157CB2FBE134BDA CRC64;
SLSDKDKTFV KAFWGKLKGK ADDVGAEALA RMFGAFPATK SYFAHWPDLS AGSGPVKKHG
KIIMAGVGDA VDKIDNLVSG LSKLSDLHAT KLRIDXXXXX XXXXXXLVTL AANFPADFTP
ELHVSLDKFF AAVGAALSDK YR
