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Protein

Hemoglobin subunit beta-C

Gene
N/A
Organism
Trematomus newnesi (Dusky notothen)
Status
Reviewed-Annotation score: Annotation score: 3 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 bindingi63 – 631Iron (heme distal ligand)
Metal bindingi92 – 921Iron (heme proximal ligand)

GO - Molecular functioni

Complete GO annotation...

Keywords - Biological processi

Oxygen transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Hemoglobin subunit beta-C
Alternative name(s):
Beta-C-globin
Hemoglobin beta-C chain
OrganismiTrematomus newnesi (Dusky notothen)
Taxonomic identifieri35730 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataEupercariaPerciformesNotothenioideiNototheniidaeTrematomus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 146146Hemoglobin subunit beta-CPRO_0000053137Add
BLAST

Expressioni

Tissue specificityi

Red blood cells.

Interactioni

Subunit structurei

HbC is a heterotetramer of two alpha-1 chains and two beta-C chains.1 Publication

Structurei

Secondary structure

1
146
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1713Combined sources
Helixi20 – 3415Combined sources
Helixi36 – 416Combined sources
Helixi43 – 453Combined sources
Helixi51 – 566Combined sources
Helixi58 – 6912Combined sources
Helixi72 – 765Combined sources
Helixi81 – 9414Combined sources
Helixi101 – 11818Combined sources
Helixi119 – 1213Combined sources
Helixi124 – 14219Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AA1X-ray1.80B/D1-146[»]
ProteinModelPortaliP45721.
SMRiP45721. Positions 1-146.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45721.

Family & Domainsi

Sequence similaritiesi

Belongs to the globin family.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG009709.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin/Proto.
IPR002337. Haemoglobin_b.
[Graphical view]
PfamiPF00042. Globin. 1 hit.
[Graphical view]
PRINTSiPR00814. BETAHAEM.
SUPFAMiSSF46458. SSF46458. 1 hit.
PROSITEiPS01033. GLOBIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P45721-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
VEWTDFERAT IKDIFSKLEY DVVGPATLAR CLVVYPWTQR YFGKFGNLYN
60 70 80 90 100
AAAIAQNAMV SKHGTTILNG LDRAVKNMDD ITNTYAELSV LHSEKLHVDP
110 120 130 140
DNFKLLADCL TIVVAARFGS AFTGEVQAAF QKFMAVVVSS LGKQYR
Length:146
Mass (Da):16,260
Last modified:November 1, 1995 - v1
Checksum:i9C05E8B66E092979
GO

Sequence databases

PIRiD54403.

Cross-referencesi

Sequence databases

PIRiD54403.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AA1X-ray1.80B/D1-146[»]
ProteinModelPortaliP45721.
SMRiP45721. Positions 1-146.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG009709.

Miscellaneous databases

EvolutionaryTraceiP45721.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin/Proto.
IPR002337. Haemoglobin_b.
[Graphical view]
PfamiPF00042. Globin. 1 hit.
[Graphical view]
PRINTSiPR00814. BETAHAEM.
SUPFAMiSSF46458. SSF46458. 1 hit.
PROSITEiPS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular characterization of the functionally distinct hemoglobins of the Antarctic fish Trematomus newnesi."
    D'Avino R., Caruso C., Tamburrini M., Romano M., Rutigliano B., Polverino de Laureto P., Camardella L., Carratore V., di Prisco G.
    J. Biol. Chem. 269:9675-9681(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiHBBC_TRENE
AccessioniPrimary (citable) accession number: P45721
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 11, 2015
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This fish has three hemoglobins: Hb1 (major, about 65-70% of the total), Hb2 (about 5% of the total) and HbC (about 20-25% of the total).

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.