Reviewed, UniProtKB/Swiss-Prot P02062 (HBB_HORSE)

Names and origin

Protein names

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

Gene names

Name:

HBB

Organism

Equus caballus (Horse)

Taxonomic identifier

9796 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus

Protein attributes

Sequence length	146 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in oxygen transport from the lung to the various peripheral tissues.
Subunit structure	Heterotetramer of two alpha chains and two beta chains.
Tissue specificity	Red blood cells.
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)
Biological process	oxygen transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	hemoglobin complex Inferred from electronic annotation. Source: InterPro
Molecular function	heme 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

Chain

1 – 146

146

Hemoglobin subunit beta

PRO_0000052975

Sites

Metal binding

63

1

Iron (heme distal ligand)

Metal binding

92

1

Iron (heme proximal ligand)

Secondary structure

1

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146

Helix Strand Turn

Details...

Helix

5 – 15

11

Helix

20 – 34

15

Helix

36 – 45

10

Helix

51 – 56

6

Helix

58 – 75

18

Helix

76 – 80

5

Helix

81 – 94

14

Helix

101 – 118

18

Helix

119 – 121

3

Helix

124 – 141

18

Helix

143 – 145

3

Sequences

	Sequence		Length	Mass (Da)
	P02062-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 734664793DA642EE	FASTA	146	16,008
	10 20 30 40 50 60 VQLSGEEKAA VLALWDKVNE EEVGGEALGR LLVVYPWTQR FFDSFGDLSN PGAVMGNPKV 70 80 90 100 110 120 KAHGKKVLHS FGEGVHHLDN LKGTFAALSE LHCDKLHVDP ENFRLLGNVL VVVLARHFGK 130 140 DFTPELQASY QKVVAGVANA LAHKYH

References

[1]	"Hemoglobins, XXXIII. Note on the sequence of the hemoglobins of the horse." Matsuda G., Maita T., Braunitzer G., Schrank B. Hoppe-Seyler's Z. Physiol. Chem. 361:1107-1116(1980) [PubMed: 7409745] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"Amino acid sequences of some tryptic peptides from the beta-chain of horse hemoglobin." Smith D.B. Can. J. Biochem. 46:825-843(1968) [PubMed: 4876811] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-82 AND 117-146.
[3]	"Amide groups of some tryptic peptides from the beta-chain of horse hemoglobin." Smith D.B., Chung W.P. Can. J. Biochem. 48:1160-1164(1970) [PubMed: 5529282] [Abstract] Cited for: DETERMINATION OF AMIDES, PROTEIN SEQUENCE OF 52-54.
[4]	"Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8-A resolution: (1) X-ray analysis." Perutz M.F., Miurhead H., Cox J.M., Goaman L.C., Mathews F.S., McGandy E.L., Webb L.E. Nature 219:29-32(1968) [PubMed: 5659617] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[5]	"Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 A resolution: the atomic model." Perutz M.F., Muirhead H., Cox J.M., Goaman L.C. Nature 219:131-139(1968) [PubMed: 5659637] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[6]	"The structure of horse methaemoglobin at 2.0-A resolution." Ladner R.C., Heidner E.J., Perutz M.F. J. Mol. Biol. 114:385-414(1977) [PubMed: 561852] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Web resources

Protein Spotlight

The man behind the molecular lung - Issue 21 of April 2002

Cross-references

Sequence databases

PIR

HBHO. B91688.

RefSeq

XP_001504239.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G0B	X-ray	1.90	B	1-146	[»]
1IBE	X-ray	1.80	B	1-146	[»]
1IWH	X-ray	1.55	B	1-146	[»]
1NS6	X-ray	2.05	B	1-146	[»]
1NS9	X-ray	1.60	B	1-146	[»]
1S0H	X-ray	3.00	B	1-146	[»]
1Y8H	X-ray	3.10	B/D	1-146	[»]
1Y8I	X-ray	2.60	B/D	1-146	[»]
1Y8K	X-ray	2.30	B/D	1-146	[»]
2D5X	X-ray	1.45	B	1-146	[»]
2DHB	X-ray	2.80	B	1-146	[»]
2MHB	X-ray	2.00	B	1-146	[»]
2ZLT	X-ray	1.90	B	1-146	[»]
2ZLU	X-ray	2.00	B	1-146	[»]
2ZLV	X-ray	2.00	B	1-146	[»]
2ZLW	X-ray	2.90	B/D	1-146	[»]
2ZLX	X-ray	2.80	B/D	1-146	[»]

ModBase

Search...

Genome annotation databases

Ensembl

ENSECAG00000010020. Equus caballus. [Contig view]

GeneID

100054109.

KEGG

ecb:100054109.

Phylogenomic databases

HOVERGEN

P02062.

OMA

P02062. LPWLTTP.

Family and domain databases

InterPro

IPR012292. Globin.
IPR000971. Globin_subset.
IPR002337. Haemoglobin_b.
[Graphical view]

Gene3D

G3DSA:1.10.490.10. Globin_related. 1 hit.

PANTHER

PTHR11442:SF7. Beta_haem. 1 hit.

Pfam

PF00042. Globin. 1 hit.
[Graphical view]

PRINTS

PR00814. BETAHAEM.

PROSITE

PS01033. GLOBIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

HBB_HORSE

Accession

Primary (citable) accession number: P02062

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)