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P01934 (HBA3_GORGO) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Hemoglobin subunit alpha-3
Alternative name(s):
Alpha-3-globin
Hemoglobin alpha-2 chain
OrganismGorilla gorilla gorilla (Lowland gorilla) [Complete proteome]
Taxonomic identifier9595 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeGorilla

Protein attributes

Sequence length141 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Miscellaneous

Two kinds of alpha-3 chains were found in one gorilla. An Asx replaces one Ser (at position 131, 133, or 138) in the tryptic peptide comprising residues 128-139.

Sequence similarities

Belongs to the globin family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 141141Hemoglobin subunit alpha-3
PRO_0000052643

Sites

Metal binding581Iron (heme distal ligand)
Metal binding871Iron (heme proximal ligand)

Sequences

Sequence LengthMass (Da)Tools
P01934 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 26DB4610C73E32E9

FASTA14115,238
        10         20         30         40         50         60 
VLSPADKTNV KAAWGKVGAH AGDYGAEALE RMFLSFPTTK TYFPHFDLSH GSAZVKGHGK 

        70         80         90        100        110        120 
KVAKALTBAV ZHLDDMPNAL SALSBLHAHK LRVBPVBFKL LNHCLLVTLA ABFPSZFTPA 

       130        140 
VHASVDKFLA SVSTVLTSKY R 

« Hide

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

PIRHAGO3. A02258.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG009709.

Family and domain databases

InterProIPR009050. Globin-like.
IPR012292. Globin_dom.
IPR000971. Globin_subset.
IPR002338. Haemoglobin_a.
IPR018331. Haemoglobin_alpha_chain.
IPR002339. Haemoglobin_pi.
[Graphical view]
Gene3DG3DSA:1.10.490.10. Globin_related. 1 hit.
PANTHERPTHR11442:SF14. Pi_haem. 1 hit.
PfamPF00042. Globin. 1 hit.
[Graphical view]
PRINTSPR00612. ALPHAHAEM.
PR00815. PIHAEM.
SUPFAMSSF46458. Globin_like. 1 hit.
PROSITEPS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHBA3_GORGO
AccessionPrimary (citable) accession number: P01934
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 16, 2011
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families