P01935 (HBA3_PANTR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Hemoglobin subunit alpha-3 Alternative name(s): Alpha-3-globin Hemoglobin alpha-2 chain
Organism	Pan troglodytes (Chimpanzee)
Taxonomic identifier	9598 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pan

Protein attributes

Sequence length	141 AA.
Sequence status	Complete.
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	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 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 – 141	141	Hemoglobin subunit alpha-3		PRO_0000052721
Sites
	Metal binding	58	1	Iron (heme distal ligand)
	Metal binding	87	1	Iron (heme proximal ligand)

Sequences

	Sequence		Length	Mass (Da)
	P01935 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 68DB40CD0238E7E9	FASTA	141	15,238
	10 20 30 40 50 60 VLSPADKTNV KAAWGKVGAH AGZYGAEALE RMFLSFPTTK TYFPHFDLSH GSAZVKGHGK 70 80 90 100 110 120 KVAKALSBAV ZHLDDMPNAL SALSBLHAHK LRVBPVBFKL LNHCLLVTLA ABFPSZFTPA 130 140 VHASVDKFLA SVSTVLTSKY R

References

[1]	"Hemoglobin alpha-3 chains in apes. Primary structures and the presumptive nature of back mutation in a normally silent gene." Boyer S.H., Noyes A.N., Boyer M.L., Marr K. J. Biol. Chem. 248:992-1003(1973) [PubMed: 4630856] [Abstract] Cited for: PROTEIN SEQUENCE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
PIR	HAGO3C. B02258.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG009709.
Family and domain databases
InterPro	IPR009050. Globin-like. IPR012292. Globin_dom. IPR000971. Globin_subset. IPR002338. Haemoglobin_a. IPR018331. Haemoglobin_alpha_chain. IPR002339. Haemoglobin_pi. [Graphical view]
Gene3D	G3DSA:1.10.490.10. Globin_related. 1 hit.
PANTHER	PTHR11442:SF14. Pi_haem. 1 hit.
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...

Entry information

Entry name

HBA3_PANTR

Accession

Primary (citable) accession number: P01935

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	October 19, 2011
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program