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Protein

Globin

Gene
N/A
Organism
Aplysia limacina (Sea hare)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi96 – 961Iron (heme proximal ligand)

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Biological processi

Oxygen transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Globin
Alternative name(s):
Myoglobin
OrganismiAplysia limacina (Sea hare)
Taxonomic identifieri6502 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaHeterobranchiaEuthyneuraEuopisthobranchiaAplysiomorphaAplysioideaAplysiidaeAplysia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 147146GlobinPRO_0000052473Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2016Combined sources
Helixi22 – 3615Combined sources
Helixi38 – 436Combined sources
Turni45 – 495Combined sources
Helixi52 – 565Combined sources
Helixi61 – 7818Combined sources
Helixi82 – 9817Combined sources
Helixi103 – 11816Combined sources
Helixi127 – 14418Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DM1X-ray1.99A2-147[»]
1MBAX-ray1.60A2-146[»]
2FALX-ray1.80A2-146[»]
2FAMX-ray2.00A2-147[»]
3MBAX-ray2.00A2-146[»]
4MBAX-ray2.00A2-146[»]
5MBAX-ray1.90A2-146[»]
ProteinModelPortaliP02210.
SMRiP02210. Positions 2-147.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02210.

Family & Domainsi

Sequence similaritiesi

Belongs to the globin family.PROSITE-ProRule annotation

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR002336. Erythrocruorin.
IPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin/Proto.
[Graphical view]
PfamiPF00042. Globin. 1 hit.
[Graphical view]
PRINTSiPR00611. ERYTHCRUORIN.
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.

P02210-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLSAAEADL AGKSWAPVFA NKDANGDAFL VALFEKFPDS ANFFADFKGK
60 70 80 90 100
SVADIKASPK LRDVSSRIFT RLNEFVNNAA DAGKMSAMLS QFAKEHVGFG
110 120 130 140
VGSAQFENVR SMFPGFVASV AAPPAGADAA WTKLFGLIID ALKAAGK
Length:147
Mass (Da):15,456
Last modified:January 23, 2007 - v4
Checksum:i631C4959E1B7CC86
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231D → N AA sequence (PubMed:4759566).Curated
Sequence conflicti27 – 282DA → LD AA sequence (PubMed:4759566).Curated
Sequence conflicti78 – 781N → D AA sequence (PubMed:4759566).Curated
Sequence conflicti81 – 811D → N AA sequence (PubMed:4759566).Curated
Sequence conflicti130 – 1301Missing AA sequence (PubMed:4759566).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79304 mRNA. Translation: CAA55885.1.
PIRiS64703. GGGAA.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79304 mRNA. Translation: CAA55885.1.
PIRiS64703. GGGAA.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DM1X-ray1.99A2-147[»]
1MBAX-ray1.60A2-146[»]
2FALX-ray1.80A2-146[»]
2FAMX-ray2.00A2-147[»]
3MBAX-ray2.00A2-146[»]
4MBAX-ray2.00A2-146[»]
5MBAX-ray1.90A2-146[»]
ProteinModelPortaliP02210.
SMRiP02210. Positions 2-147.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP02210.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR002336. Erythrocruorin.
IPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin/Proto.
[Graphical view]
PfamiPF00042. Globin. 1 hit.
[Graphical view]
PRINTSiPR00611. ERYTHCRUORIN.
SUPFAMiSSF46458. SSF46458. 1 hit.
PROSITEiPS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Aplysia limacina myoglobin cDNA cloning: an alternative mechanism of oxygen stabilization as studied by active-site mutagenesis."
    Cutruzzola F., Travaglini Allocatelli C., Brancaccio A., Brunori M.
    Biochem. J. 314:83-90(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "The amino acid sequence of myoglobin from the mollusc Aplysia limacina."
    Tentori L., Vivaldi G., Carta S., Marinucci M., Massa A., Antonini E., Brunori M.
    Int. J. Pept. Protein Res. 5:187-200(1973) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-147, ACETYLATION AT SER-2.
    Tissue: Buccal muscle.
  3. "Aplysia limacina myoglobin. Crystallographic analysis at 1.6-A resolution."
    Bolognesi M., Onesti S., Gatti G., Coda A., Ascenzi P., Brunori M.
    J. Mol. Biol. 205:529-544(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
  4. "Binding mode of azide to ferric Aplysia limacina myoglobin. Crystallographic analysis at 1.9-A resolution."
    Mattevi A., Gatti G., Coda A., Rizzi M., Ascenzi P., Brunori M., Bolognesi M.
    J. Mol. Recognit. 4:1-6(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SEQUENCE REVISION.
  5. "Engineering His(E7) affects the control of heme reactivity in Aplysia limacina myoglobin."
    Federici L., Savino C., Musto R., Travaglini-Allocatelli C., Cutruzzola F., Brunori M.
    Biochem. Biophys. Res. Commun. 269:58-63(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS).

Entry informationi

Entry nameiGLB_APLLI
AccessioniPrimary (citable) accession number: P02210
Secondary accession number(s): Q93114
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: December 9, 2015
This is version 95 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

This molluscan globin lacks one of the heme-binding histidine residues found in most other globins.

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.