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P23741 (HBB_LATCH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 68. 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 beta
Alternative name(s):
Beta-globin
Hemoglobin beta chain
Gene names
Name:HBB
OrganismLatimeria chalumnae (West Indian ocean coelacanth) [Reference proteome]
Taxonomic identifier7897 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiCoelacanthiformesCoelacanthidaeLatimeria

Protein attributes

Sequence length146 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 (an easy dimerization is also reported).

Tissue specificity

Red blood cells.

Sequence similarities

Belongs to the globin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 146146Hemoglobin subunit beta
PRO_0000052985

Sites

Metal binding631Iron (heme distal ligand) By similarity
Metal binding921Iron (heme proximal ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
P23741 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: E61EA7DBB67EFC52

FASTA14616,872
        10         20         30         40         50         60 
VHWTETERAT IETVYQKLHL DEVGREALTR LFIVYPWTTR YFKSFGDLSS SKAIASNPKV 

        70         80         90        100        110        120 
TEHGLKVMNK LTEAIHNLDH IKDLFHKLSE KHFHELHVDP QNFKLLSKCL IIVLATKLGK 

       130        140 
QLTPDVQATW EKLLSVVVAA LSREYH 

« Hide

References

[1]"A 'living fossil' sequence: primary structure of the coelacanth (Latimeria chalumnae) hemoglobin -- evolutionary and functional aspects."
Gorr T., Kleinschmidt T., Sgouros J.G., Kasang L.
Biol. Chem. Hoppe-Seyler 372:599-612(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"Close tetrapod relationships of the coelacanth Latimeria indicated by haemoglobin sequences."
Gorr T., Kleinschmidt T., Fricke H.
Nature 351:394-397(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PHYLOGENETIC COMPARISONS.

Cross-references

Sequence databases

PIRS15449.

3D structure databases

ProteinModelPortalP23741.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG009709.

Family and domain databases

Gene3D1.10.490.10. 1 hit.
InterProIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR002337. Haemoglobin_b.
[Graphical view]
PANTHERPTHR11442:SF7. PTHR11442:SF7. 1 hit.
PfamPF00042. Globin. 1 hit.
[Graphical view]
PRINTSPR00814. BETAHAEM.
SUPFAMSSF46458. Globin_like. 1 hit.
PROSITEPS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHBB_LATCH
AccessionPrimary (citable) accession number: P23741
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: April 3, 2013
This is version 68 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