P80044 (HBB_TREBE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hemoglobin subunit beta

Alternative name(s):
Beta-globin
Hemoglobin beta chain

Gene names

Name:

hbb

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	147 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in oxygen transport from gills to the various peripheral tissues. Ref.2
Subunit structure	Hb1 is a heterotetramer of two alpha chains and two beta chains. Ref.2
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
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular_component	hemoglobin complex Inferred from electronic annotation. Source: InterPro
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 electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 147

146

Hemoglobin subunit beta

PRO_0000053046

Sites

Metal binding

64

1

Iron (heme distal ligand)

Metal binding

93

1

Iron (heme proximal ligand)

Secondary structure

1

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147

Helix Strand Turn

Details...

Helix

6 – 18

13

Helix

21 – 35

15

Helix

37 – 42

6

Helix

44 – 46

3

Helix

52 – 56

5

Helix

59 – 70

12

Helix

73 – 76

4

Turn

77 – 80

4

Helix

82 – 85

4

Helix

87 – 95

9

Helix

102 – 119

18

Helix

120 – 122

3

Helix

125 – 144

20

Sequences

	Sequence		Length	Mass (Da)
	P80044 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 0C9A4B07948A81B2	FASTA	147	16,264
	10 20 30 40 50 60 MVEWTDKERS IISDIFSHMD YDDIGPKALS RCLIVYPWTQ RHFSGFGNLY NAEAIIGNAN 70 80 90 100 110 120 VAAHGIKVLH GLDRGVKNMD NIAATYADLS TLHSEKLHVD PDNFKLLSDC ITIVLAAKMG 130 140 HAFTAETQGA FQKFLAVVVS ALGKQYH

References

[1]	"Antarctic fish hemoglobins: evidence for adaptive evolution at subzero temperature." Bargelloni L., Marcato S., Patarnello T. Proc. Natl. Acad. Sci. U.S.A. 95:8670-8675(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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 OF 2-147, FUNCTION, SUBUNIT, X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). Tissue: Blood.
[3]	"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

EMBL
GenBank
DDBJ

AF067570 mRNA. Translation: AAC41388.1.

PIR

S21678.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HBH	X-ray	2.20	B/D	2-147	[»]
1PBX	X-ray	2.50	B	2-147	[»]
1S5X	X-ray	2.40	B	2-146	[»]
1S5Y	X-ray	2.50	B/D	2-146	[»]
2H8D	X-ray	1.78	B/D	2-146	[»]
2H8F	X-ray	1.30	B/D	2-146	[»]
2PEG	X-ray	1.48	B	2-147	[»]
3GKV	X-ray	1.40	B	2-147	[»]
3GQG	X-ray	1.73	B/D	2-147	[»]
4G51	X-ray	2.50	B/D	2-147	[»]
4IRO	X-ray	2.20	B/D	2-147	[»]

ProteinModelPortal

P80044.

SMR

P80044. Positions 2-147.

ModBase

Search...

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.
IPR002337. Haemoglobin_b.
[Graphical view]

PANTHER

PTHR11442:SF7. PTHR11442:SF7. 1 hit.

Pfam

PF00042. Globin. 1 hit.
[Graphical view]

PRINTS

PR00814. BETAHAEM.

SUPFAM

SSF46458. Globin_like. 1 hit.

PROSITE

PS01033. GLOBIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P80044.

Entry information

Entry name

HBB_TREBE

Accession

Primary (citable) accession number: P80044
Secondary accession number(s): O93350

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program