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P80044

- HBB_TREBE

UniProt

P80044 - HBB_TREBE

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Protein
Hemoglobin subunit beta
Gene
hbb
Organism
Trematomus bernacchii (Emerald rockcod) (Pagothenia bernacchii)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in oxygen transport from gills to the various peripheral tissues.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Iron (heme distal ligand)
Metal bindingi93 – 931Iron (heme proximal ligand)

GO - Molecular functioni

  1. heme binding Source: InterPro
  2. iron ion binding Source: InterPro
  3. oxygen binding Source: InterPro
  4. oxygen transporter activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Oxygen transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Hemoglobin subunit beta
Alternative name(s):
Beta-globin
Hemoglobin beta chain
Gene namesi
Name:hbb
OrganismiTrematomus bernacchii (Emerald rockcod) (Pagothenia bernacchii)
Taxonomic identifieri40690 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataPercomorphariaPerciformesNotothenioideiNototheniidaeTrematomus

Subcellular locationi

GO - Cellular componenti

  1. hemoglobin complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 147146Hemoglobin subunit beta
PRO_0000053046Add
BLAST

Expressioni

Tissue specificityi

Red blood cells.

Interactioni

Subunit structurei

Hb1 is a heterotetramer of two alpha chains and two beta chains.1 Publication

Protein-protein interaction databases

MINTiMINT-1507087.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1813
Helixi21 – 3515
Helixi37 – 426
Helixi44 – 463
Helixi52 – 565
Helixi59 – 7012
Helixi73 – 764
Turni77 – 804
Helixi82 – 854
Helixi87 – 959
Helixi102 – 11918
Helixi120 – 1223
Helixi125 – 14420

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HBHX-ray2.20B/D2-147[»]
1PBXX-ray2.50B2-147[»]
1S5XX-ray2.40B2-147[»]
1S5YX-ray2.50B/D2-147[»]
2H8DX-ray1.78B/D2-147[»]
2H8FX-ray1.30B/D2-147[»]
2PEGX-ray1.48B2-147[»]
3GKVX-ray1.40B2-147[»]
3GQGX-ray1.73B/D2-147[»]
4G51X-ray2.50B/D2-147[»]
4IROX-ray2.20B/D2-147[»]
ProteinModelPortaliP80044.
SMRiP80044. Positions 2-147.

Miscellaneous databases

EvolutionaryTraceiP80044.

Family & Domainsi

Sequence similaritiesi

Belongs to the globin family.

Phylogenomic databases

HOVERGENiHBG009709.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR002337. Haemoglobin_b.
[Graphical view]
PANTHERiPTHR11442:SF7. PTHR11442:SF7. 1 hit.
PfamiPF00042. Globin. 1 hit.
[Graphical view]
PRINTSiPR00814. BETAHAEM.
SUPFAMiSSF46458. SSF46458. 1 hit.
PROSITEiPS01033. GLOBIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P80044-1 [UniParc]FASTAAdd to Basket

« Hide

MVEWTDKERS IISDIFSHMD YDDIGPKALS RCLIVYPWTQ RHFSGFGNLY    50
NAEAIIGNAN VAAHGIKVLH GLDRGVKNMD NIAATYADLS TLHSEKLHVD 100
PDNFKLLSDC ITIVLAAKMG HAFTAETQGA FQKFLAVVVS ALGKQYH 147
Length:147
Mass (Da):16,264
Last modified:January 23, 2007 - v2
Checksum:i0C9A4B07948A81B2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF067570 mRNA. Translation: AAC41388.1.
PIRiS21678.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF067570 mRNA. Translation: AAC41388.1 .
PIRi S21678.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 2-147 [» ]
1S5Y X-ray 2.50 B/D 2-147 [» ]
2H8D X-ray 1.78 B/D 2-147 [» ]
2H8F X-ray 1.30 B/D 2-147 [» ]
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 [» ]
ProteinModelPortali P80044.
SMRi P80044. Positions 2-147.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1507087.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG009709.

Miscellaneous databases

EvolutionaryTracei P80044.

Family and domain databases

Gene3Di 1.10.490.10. 1 hit.
InterProi IPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR002337. Haemoglobin_b.
[Graphical view ]
PANTHERi PTHR11442:SF7. PTHR11442:SF7. 1 hit.
Pfami PF00042. Globin. 1 hit.
[Graphical view ]
PRINTSi PR00814. BETAHAEM.
SUPFAMi SSF46458. SSF46458. 1 hit.
PROSITEi PS01033. GLOBIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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).

Entry informationi

Entry nameiHBB_TREBE
AccessioniPrimary (citable) accession number: P80044
Secondary accession number(s): O93350
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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