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Protein

Extracellular giant hemoglobin major globin subunit A1

Gene

ghbA1

Organism
Oligobrachia mashikoi (Beard worm)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The extracellular giant hemoglobin is able to bind and transport oxygen and hydrosulfide simultaneously and reversibly at two different sites.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei79 – 791HydrosulfideCurated
Metal bindingi110 – 1101Iron (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 giant hemoglobin major globin subunit A1
Short name:
Major globin chain b
Gene namesi
Name:ghbA1
OrganismiOligobrachia mashikoi (Beard worm)
Taxonomic identifieri55676 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaAnnelidaPolychaetaPalpataCanalipalpataSabellidaSiboglinidaeOligobrachia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16162 PublicationsAdd
BLAST
Chaini17 – 156140Extracellular giant hemoglobin major globin subunit A1PRO_0000052518Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi18 ↔ 1461 Publication
Disulfide bondi137 – 137Interchain (with C-142 in subunit B2)1 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

The 400 kDa hemoglobin consists of a spherical 24-mer arranged as a double layer of dome-shaped dodecamers. Each dodecamer is composed of the 3-fold trimer of the tetramer A1-A2-B1-B2 having one intra-tetramer (A1-B2) disulfide bond and one inter-tetramer (B1-B2) disulfide bond per tetramer.1 Publication

Structurei

Secondary structure

1
156
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 3415Combined sources
Helixi40 – 5314Combined sources
Helixi56 – 627Combined sources
Turni63 – 686Combined sources
Helixi73 – 9018Combined sources
Turni91 – 944Combined sources
Helixi96 – 10914Combined sources
Beta strandi111 – 1133Combined sources
Helixi117 – 13014Combined sources
Helixi131 – 1344Combined sources
Helixi140 – 15314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D2MX-ray2.85A17-156[»]
2D2NX-ray3.20A17-156[»]
2ZFOX-ray1.95A17-156[»]
2ZS0X-ray1.60A17-156[»]
2ZS1X-ray1.70A17-156[»]
ProteinModelPortaliQ7M419.
SMRiQ7M419. Positions 17-156.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7M419.

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.

Q7M419-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVLIIFACL VVMASAVCNR LEQILVKTQW AQSYGEAENR AAFSRDLFSE
60 70 80 90 100
LFNIQGSSRA LFSGVGVDDM NSAAFTAHCL RVTGALNRLI SQLDQQATIN
110 120 130 140 150
ADLAHLAGQH ASRNLDASNF AAMGQAVMSV VPTHLDCFNQ HAWGECYERI

ASGISG
Length:156
Mass (Da):16,866
Last modified:January 23, 2007 - v2
Checksum:iE8F6B30F5121343B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB185392 mRNA. Translation: BAD86543.1.
PIRiS72252.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB185392 mRNA. Translation: BAD86543.1.
PIRiS72252.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D2MX-ray2.85A17-156[»]
2D2NX-ray3.20A17-156[»]
2ZFOX-ray1.95A17-156[»]
2ZS0X-ray1.60A17-156[»]
2ZS1X-ray1.70A17-156[»]
ProteinModelPortaliQ7M419.
SMRiQ7M419. Positions 17-156.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ7M419.

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...

Publicationsi

  1. "Purification, characterization and sequence analyses of the extracellular giant hemoglobin from Oligobrachia mashikoi."
    Nakagawa T., Onoda S., Kanemori M., Sasayama Y., Fukumori Y.
    Zool. Sci. 22:283-291(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-26.
  2. "Electrospray ionization mass spectrometric composition of the 400 kDa hemoglobin from the pogonophoran Oligobrachia mashikoi and the primary structures of three major globin chains."
    Yuasa H.J., Green B.N., Takagi T., Suzuki N., Vinogradov S.N., Suzuki T.
    Biochim. Biophys. Acta 1296:235-244(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-156, PROTEIN SEQUENCE OF 17-48, IDENTIFICATION BY MASS SPECTROMETRY.
  3. "Structure of an extracellular giant hemoglobin of the gutless beard worm Oligobrachia mashikoi."
    Numoto N., Nakagawa T., Kita A., Sasayama Y., Fukumori Y., Miki K.
    Proc. Natl. Acad. Sci. U.S.A. 102:14521-14526(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 17-156, SUBUNIT, METAL, DISULFIDE BONDS.

Entry informationi

Entry nameiGLBA1_OLIMA
AccessioniPrimary (citable) accession number: Q7M419
Secondary accession number(s): Q5KSB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: January 23, 2007
Last modified: October 14, 2015
This is version 63 of the entry and version 2 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.