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Protein

Extracellular globin-3

Gene
N/A
Organism
Lumbricus terrestris (Common earthworm)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi119 – 1191Iron (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:
Extracellular globin-3
Alternative name(s):
Erythrocruorin
Extracellular globin III
Globin C
OrganismiLumbricus terrestris (Common earthworm)
Taxonomic identifieri6398 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaAnnelidaClitellataOligochaetaHaplotaxidaLumbricinaLumbricidaeLumbricinaeLumbricus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 17172 PublicationsAdd
BLAST
Chaini18 – 170153Extracellular globin-3PRO_0000011213Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi23 – 23Interchain (with chain IV)By similarity
Disulfide bondi24 ↔ 156By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

The extracellular hemoglobin of the earthworm consists of 12 subunits that have a hexagonal bilayer structure with a molecular weight near 3.8 million. Each one-twelfth subunit is composed primarily of disulfide linked trimers (chains A, B, and C) and monomers (chain D).1 Publication

Protein-protein interaction databases

DIPiDIP-29124N.

Structurei

Secondary structure

1
170
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 243Combined sources
Helixi26 – 3712Combined sources
Helixi38 – 403Combined sources
Beta strandi41 – 433Combined sources
Helixi45 – 6319Combined sources
Helixi67 – 704Combined sources
Helixi72 – 743Combined sources
Helixi76 – 783Combined sources
Helixi82 – 10019Combined sources
Turni101 – 1033Combined sources
Helixi105 – 12016Combined sources
Helixi127 – 14418Combined sources
Helixi150 – 16516Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X9FX-ray2.60C/G/K18-170[»]
2GTLX-ray3.50C/G/K18-170[»]
4V93electron microscopy8.10A0/A5/AC/AH/AM/AR/AW/Ab/Ag/Al/Aq/Av20-168[»]
B4/BB/BG/BL/BQ/BV/Ba/Bf/Bk/Bp/Bu/Bz/C3/CA/CF/CK/CP/CU/CZ/Ce/Cj/Co/Ct/Cy1-170[»]
ProteinModelPortaliP11069.
SMRiP11069. Positions 20-168.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11069.

Family & Domainsi

Sequence similaritiesi

Belongs to the globin family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin/Proto.
IPR014610. Haemoglobin_extracell.
[Graphical view]
PfamiPF00042. Globin. 1 hit.
[Graphical view]
PIRSFiPIRSF036517. Ext_hemo. 1 hit.
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.

P11069-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRQLLVLVG LAVVCLADEH EHCCSEEDHR IVQKQWDILW RDTESSKIKI
60 70 80 90 100
GFGRLLLTKL AKDIPDVNDL FKRVDIEHAE GPKFSAHALR ILNGLDLAIN
110 120 130 140 150
LLDDPPALDA ALDHLAHQHE VREGVQKAHF KKFGEILATG LPQVLDDYDA
160 170
LAWKSCLKGI LTKISSRLNA
Length:170
Mass (Da):19,082
Last modified:April 1, 1990 - v3
Checksum:i03306F66E8BE3057
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171A → T (PubMed:2832953).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03082 mRNA. Translation: AAA75013.1.
J05161 Genomic DNA. Translation: AAA98622.1.
PIRiA28563.
A34433.
C28151.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03082 mRNA. Translation: AAA75013.1.
J05161 Genomic DNA. Translation: AAA98622.1.
PIRiA28563.
A34433.
C28151.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X9FX-ray2.60C/G/K18-170[»]
2GTLX-ray3.50C/G/K18-170[»]
4V93electron microscopy8.10A0/A5/AC/AH/AM/AR/AW/Ab/Ag/Al/Aq/Av20-168[»]
B4/BB/BG/BL/BQ/BV/Ba/Bf/Bk/Bp/Bu/Bz/C3/CA/CF/CK/CP/CU/CZ/Ce/Cj/Co/Ct/Cy1-170[»]
ProteinModelPortaliP11069.
SMRiP11069. Positions 20-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29124N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP11069.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin/Proto.
IPR014610. Haemoglobin_extracell.
[Graphical view]
PfamiPF00042. Globin. 1 hit.
[Graphical view]
PIRSFiPIRSF036517. Ext_hemo. 1 hit.
SUPFAMiSSF46458. SSF46458. 1 hit.
PROSITEiPS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGLB3_LUMTE
AccessioniPrimary (citable) accession number: P11069
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: April 1, 1990
Last modified: September 7, 2016
This is version 95 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

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.