P80043 (HBA_TREBE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hemoglobin subunit alpha

Alternative name(s):
Alpha-globin
Hemoglobin alpha chain

Gene names

Name:

hba

Organism

Trematomus bernacchii (Emerald rockcod) (Pagothenia bernacchii)

Taxonomic identifier

40690 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Actinopterygii › Actinopteri › Neopterygii › Teleostei › Elopocephala › Clupeocephala › Euteleostei › Neognathi › Neoteleostei › Eurypterygii › Ctenosquamata › Acanthomorpha › Euacanthomorpha › Holacanthopterygii › Acanthopterygii › Euacanthopterygii › Percomorpha › Perciformes › Notothenioidei › Nototheniidae › Trematomus

Protein attributes

Sequence length	142 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in oxygen transport from gills to the various peripheral tissues. Ref.1
Subunit structure	Hb1 is a heterotetramer of two alpha chains and two beta chains. HbC is a heterotetramer of two alpha chains and two beta-C chains. Ref.1
Tissue specificity	Red blood cells.
Miscellaneous	This fish has three hemoglobins: Hb1 (major) and two minor hemoglobins (about 1-2% of the total). Hb1 has a strong alkaline Bohr effect, and at low pH exhibits the reduced ligand affinity and cooperativity that comprise the Root effect.
Sequence similarities	Belongs to the globin family.

Ontologies

Keywords
Biological process	Oxygen transport Transport
Ligand	Heme Iron Metal-binding
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular_component	hemoglobin complex Inferred from sequence or structural similarity PubMed 15340169. Source: UniProtKB
Molecular_function	heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro oxygen binding Inferred from electronic annotation. Source: InterPro oxygen transporter activity Inferred from sequence or structural similarity PubMed 15340169. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 142

142

Hemoglobin subunit alpha

PRO_0000052712

Sites

Metal binding

59

1

Iron (heme distal ligand)

Metal binding

88

1

Iron (heme proximal ligand)

Amino acid modifications

Modified residue

1

1

N-acetylserine

Secondary structure

1

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142

Helix Strand Turn

Details...

Helix

4 – 17

14

Helix

18 – 20

3

Helix

21 – 35

15

Helix

37 – 43

7

Beta strand

50 – 52

3

Helix

54 – 72

19

Turn

73 – 75

3

Helix

77 – 80

4

Helix

82 – 90

9

Helix

97 – 113

17

Turn

115 – 117

3

Helix

120 – 137

18

Turn

138 – 140

3

Sequences

	Sequence		Length	Mass (Da)
	P80043 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 24C8759C565202A4	FASTA	142	15,632
	10 20 30 40 50 60 SLSDKDKAAV RALWSKIGKS ADAIGNDALS RMIVVYPQTK TYFSHWPDVT PGSPHIKAHG 70 80 90 100 110 120 KKVMGGIALA VSKIDDLKTG LMELSEQHAY KLRVDPANFK ILNHCILVVI STMFPKEFTP 130 140 EAHVSLDKFL SGVALALAER YR

References

[1]	"Haemoglobin of the antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen equilibria and crystal structure of its carbonmonoxy derivative." Camardella L., Caruso C., D'Avino R., di Prisco G., Rutigliano B., Tamburrini M., Fermi G., Perutz M.F. J. Mol. Biol. 224:449-460(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT, X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). Tissue: Blood.
[2]	"Structure of deoxyhaemoglobin of the antarctic fish Pagothenia bernacchii with an analysis of the structural basis of the Root effect by comparison of the liganded and unliganded haemoglobin structures." Ito N., Komiyama N.H., Fermi G. J. Mol. Biol. 250:648-658(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

PIR

S21677.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HBH	X-ray	2.20	A/C	1-142	[»]
1PBX	X-ray	2.50	A	1-142	[»]
1S5X	X-ray	2.40	A	1-142	[»]
1S5Y	X-ray	2.50	A/C	1-142	[»]
2H8D	X-ray	1.78	A/C	1-142	[»]
2H8F	X-ray	1.30	A/C	1-142	[»]
2PEG	X-ray	1.48	A	1-142	[»]
3GKV	X-ray	1.40	A	1-142	[»]
3GQG	X-ray	1.73	A/C	1-142	[»]
4G51	X-ray	2.50	A/C	1-142	[»]
4IRO	X-ray	2.20	A/C	1-142	[»]

ProteinModelPortal

P80043.

SMR

P80043. Positions 1-142.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1507077.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG009709.

Family and domain databases

Gene3D

1.10.490.10. 1 hit.

InterPro

IPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR002338. Haemoglobin_a.
IPR002339. Haemoglobin_pi.
[Graphical view]

Pfam

PF00042. Globin. 1 hit.
[Graphical view]

PRINTS

PR00612. ALPHAHAEM.
PR00815. PIHAEM.

SUPFAM

SSF46458. Globin_like. 1 hit.

PROSITE

PS01033. GLOBIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P80043.

Entry information

Entry name

HBA_TREBE

Accession

Primary (citable) accession number: P80043

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	May 29, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program