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P02543 (VIME_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Vimentin
Gene names
Name:VIM
OrganismSus scrofa (Pig) [Complete proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length275 AA.
Sequence statusFragments.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells.

Subunit structure

Homopolymer. Interacts with LGSN and SYNM. Interacts (via rod region) with PLEC (via CH 1 domain). Interacts with SLC6A4 By similarity. Interacts with STK33 By similarity.

Post-translational modification

One of the most prominent phosphoproteins in various cells of mesenchymal origin. Phosphorylation is enhanced during cell division, at which time vimentin filaments are significantly reorganized. Phosphorylation by PKN1 inhibits the formation of filaments. Filament disassembly during mitosis is promoted by phosphorylation at Ser-54 as well as by nestin. Phosphorylated at Ser-55 by CDK5 during neutrophil secretion in the cytoplasm. Phosphorylated by STK33 By similarity.

Sequence similarities

Belongs to the intermediate filament family.

Ontologies

Keywords
   Cellular componentIntermediate filament
   DomainCoiled coil
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Cellular componentintermediate filament

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionstructural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 275275Vimentin
PRO_0000063758

Regions

Region1 – 9696Head
Region97 – 216120Rod
Region97 – ›98›2Coil 1A
Region‹99 – 216›118Coil 2
Region217 – 27559Tail

Amino acid modifications

Modified residue11N-acetylserine By similarity
Modified residue61Phosphoserine; by PKA and PKC By similarity
Modified residue71Phosphoserine By similarity
Modified residue81Phosphoserine; by PKC By similarity
Modified residue91Phosphoserine; by PKC By similarity
Modified residue191Phosphothreonine By similarity
Modified residue241Phosphoserine; by PKA and PKC By similarity
Modified residue251Phosphoserine; by PKC By similarity
Modified residue261Phosphoserine By similarity
Modified residue281Phosphoserine By similarity
Modified residue321Phosphothreonine By similarity
Modified residue331Phosphoserine; by PKC By similarity
Modified residue371Phosphotyrosine By similarity
Modified residue381Phosphoserine; by CaMK2, PKA, PKC and ROCK2 By similarity
Modified residue411Phosphoserine; by PKC
Modified residue461Phosphoserine; by PKA By similarity
Modified residue481Phosphoserine By similarity
Modified residue501Phosphoserine; by PKA and PKC By similarity
Modified residue541Phosphoserine By similarity
Modified residue551Phosphoserine; by CDK5 and CDK1 By similarity
Modified residue621Phosphotyrosine By similarity
Modified residue661Phosphoserine; by PKA and PKC By similarity
Modified residue731Phosphoserine; by AURKB and ROCK2 By similarity
Modified residue741Phosphoserine By similarity
Modified residue1011N6-acetyllysine By similarity
Modified residue1081Phosphoserine By similarity
Modified residue1821N6-acetyllysine By similarity
Modified residue2111N6-acetyllysine By similarity
Modified residue2181Phosphoserine By similarity
Modified residue2211Phosphoserine By similarity
Modified residue2281Phosphoserine By similarity
Modified residue2291Phosphoserine By similarity
Modified residue2391Phosphoserine By similarity
Modified residue2541N6-acetyllysine By similarity
Modified residue2551Phosphothreonine By similarity
Modified residue2671Phosphothreonine By similarity
Modified residue2681Phosphoserine By similarity

Experimental info

Non-adjacent residues98 – 992

Sequences

Sequence LengthMass (Da)Tools
P02543 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 37F495BD1A0E0236

FASTA27530,989
        10         20         30         40         50         60 
STRTVSSSSY RRMFGGPGTA SRPSSSRSYV TTSTRTYSLG SALRPSTSRS LSTSSPGGVG 

        70         80         90        100        110        120 
YYATRSSAVR LRSSVPGVRL LQDAVDFSLA DAINTEFKWY KSKFADLSEA ANRNNDALRQ 

       130        140        150        160        170        180 
AKQESNEYRR QVQSLTCEVD ALKGTNESLE RQMREMEENF AVEAANYQDT IGRLQDEIQN 

       190        200        210        220        230        240 
MKEEMARHLR EYQDLLNVKM ALDIEIATYR KLLEGEESRI SLPLPNFSSL NLRETNLESL 

       250        260        270 
PLVDTHSKRT LLIKTVETRD GQVINETSQH HNDLE

« Hide

References

[1]"Amino acid sequence characterization of mammalian vimentin, the mesenchymal intermediate filament protein."
Geisler N., Plessmann U., Weber K.
FEBS Lett. 163:22-24(1983) [PubMed: 6628686] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-98.
Tissue: Lens.
[2]"Related amino acid sequences in neurofilaments and non-neural intermediate filaments."
Geisler N., Plessmann U., Weber K.
Nature 296:448-450(1982) [PubMed: 7199625] [Abstract]
Cited for: PROTEIN SEQUENCE OF 99-136.
Tissue: Lens.
[3]"Comparison of the proteins of two immunologically distinct intermediate-sized filaments by amino acid sequence analysis: desmin and vimentin."
Geisler N., Weber K.
Proc. Natl. Acad. Sci. U.S.A. 78:4120-4123(1981) [PubMed: 6945574] [Abstract]
Cited for: PROTEIN SEQUENCE OF 137-275.
Tissue: Lens.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRS05207.

3D structure databases

ProteinModelPortalP02543.
SMRP02543. Positions 137-215.
ModBaseSearch...

Protein-protein interaction databases

STRINGP02543.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG013015.

Family and domain databases

InterProIPR016044. F.
IPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
[Graphical view]
PANTHERPTHR23239. IF. 1 hit.
PfamPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVIME_PIG
AccessionPrimary (citable) accession number: P02543
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 19, 2011
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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