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P31000 (VIME_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vimentin
Gene names
Name:Vim
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. Ref.6

Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2 By similarity. Ref.6

Subunit structure

Homopolymer assembled from elementary dimers. Interacts with HCV core protein. Interacts with LGSN and SYNM. Interacts (via rod region) with PLEC (via CH 1 domain). Interacts with SLC6A4. Interacts with STK33. Interacts with LARP6. Interacts with RAB8B. Interacts with TOR1A; the interaction associates TOR1A with the cytoskeleton. Interacts with TOR1AIP1. Ref.7

Subcellular location

Nucleus matrix. Cytoplasm By similarity Ref.3.

Domain

The central alpha-helical coiled-coil rod region mediates elementary homodimerization 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 inhibit the formation of filaments By similarity. Filament disassembly during mitosis is promoted by phosphorylation at Ser-55 as well as by nestin Probable. Phosphorylated at Ser-56 by CDK5 during neutrophil secretion in the cytoplasm. Phosphorylated by STK33 By similarity. Ref.8

Sequence similarities

Belongs to the intermediate filament family.

Ontologies

Keywords
   Cellular componentCytoplasm
Intermediate filament
Nucleus
   DomainCoiled coil
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from expression pattern PubMed 18077910. Source: RGD

cellular response to fibroblast growth factor stimulus

Inferred from expression pattern PubMed 15195687. Source: RGD

decidualization

Inferred from expression pattern PubMed 17653607. Source: RGD

fat cell differentiation

Inferred from expression pattern PubMed 8680470. Source: RGD

positive regulation of glial cell proliferation

Inferred from mutant phenotype PubMed 21250919. Source: RGD

regulation of Schwann cell migration

Inferred from direct assay PubMed 22371530. Source: RGD

regulation of axonogenesis

Inferred from direct assay PubMed 22371530. Source: RGD

response to estradiol

Inferred from expression pattern PubMed 21915674. Source: RGD

response to radiation

Inferred from expression pattern PubMed 17649822. Source: RGD

response to selenium ion

Inferred from expression pattern PubMed 22002783. Source: RGD

response to vitamin D

Inferred from expression pattern PubMed 18687349. Source: RGD

response to zinc ion

Inferred from expression pattern PubMed 22017769. Source: RGD

skeletal muscle tissue regeneration

Inferred from expression pattern PubMed 18941770. Source: RGD

   Cellular_componentaxon

Inferred from direct assay PubMed 18431495. Source: RGD

cell body

Inferred from direct assay PubMed 7879923. Source: RGD

cell projection

Inferred from direct assay PubMed 7879923. Source: RGD

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoskeleton

Inferred from direct assay PubMed 10906761. Source: RGD

cytosol

Inferred from direct assay PubMed 10906761. Source: RGD

intermediate filament

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from direct assay PubMed 21915674. Source: RGD

type III intermediate filament

Traceable author statement Ref.1. Source: RGD

   Molecular_functionkinase binding

Inferred from physical interaction PubMed 11082283. Source: RGD

protein binding

Inferred from physical interaction Ref.7. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 12700184. Source: RGD

protein phosphatase 2A binding

Inferred from direct assay PubMed 10906761. Source: RGD

structural constituent of cytoskeleton

Inferred from sequence or structural similarity. Source: UniProtKB

structural molecule activity

Traceable author statement Ref.1. Source: RGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

YwhabP352133EBI-368510,EBI-917309

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 466465Vimentin
PRO_0000063759

Regions

Region2 – 9594Head
Region96 – 407312Rod
Region96 – 13136Coil 1A
Region132 – 15322Linker 1
Region154 – 24592Coil 1B
Region246 – 26823Linker 12
Region269 – 407139Coil 2
Region408 – 46659Tail
Coiled coil96 – 13136
Coiled coil154 – 24592
Coiled coil303 – 407105

Sites

Site3511Stutter By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue51Phosphoserine By similarity
Modified residue71Phosphoserine; by PKA and PKC; alternate By similarity
Modified residue81Phosphoserine By similarity
Modified residue91Phosphoserine; by PKC By similarity
Modified residue101Phosphoserine; by PKC By similarity
Modified residue201Phosphothreonine By similarity
Modified residue251Phosphoserine By similarity
Modified residue261Phosphoserine By similarity
Modified residue291Phosphoserine By similarity
Modified residue331Phosphothreonine; alternate By similarity
Modified residue341Phosphoserine; alternate By similarity
Modified residue381Phosphotyrosine By similarity
Modified residue391Phosphoserine; by CaMK2, PKA, PKC and ROCK2 By similarity
Modified residue421Phosphoserine; by PKC By similarity
Modified residue471Phosphoserine; by PKA By similarity
Modified residue491Phosphoserine By similarity
Modified residue511Phosphoserine; by PKA and PKC By similarity
Modified residue531Phosphotyrosine By similarity
Modified residue551Phosphoserine Probable
Modified residue561Phosphoserine; by CDK5 and CDK1 By similarity
Modified residue611Phosphotyrosine By similarity
Modified residue661Phosphoserine; by PKA and PKC By similarity
Modified residue721Phosphoserine; by AURKB and ROCK2 By similarity
Modified residue731Phosphoserine By similarity
Modified residue831Phosphoserine; by CaMK2 By similarity
Modified residue1171Phosphotyrosine By similarity
Modified residue1201N6-acetyllysine; alternate By similarity
Modified residue1201N6-succinyllysine; alternate By similarity
Modified residue1291N6-acetyllysine; alternate By similarity
Modified residue1291N6-succinyllysine; alternate By similarity
Modified residue1391N6-acetyllysine By similarity
Modified residue1441Phosphoserine By similarity
Modified residue1681N6-acetyllysine By similarity
Modified residue1881N6-acetyllysine; alternate By similarity
Modified residue1881N6-succinyllysine; alternate By similarity
Modified residue2141Phosphoserine By similarity
Modified residue2231N6-acetyllysine By similarity
Modified residue2261Phosphoserine By similarity
Modified residue2351N6-acetyllysine By similarity
Modified residue2611Phosphoserine By similarity
Modified residue2661Phosphothreonine By similarity
Modified residue2941N6-acetyllysine; alternate By similarity
Modified residue2941N6-succinyllysine; alternate By similarity
Modified residue2991Phosphoserine By similarity
Modified residue3731N6-acetyllysine By similarity
Modified residue4091Phosphoserine By similarity
Modified residue4121Phosphoserine By similarity
Modified residue4191Phosphoserine By similarity
Modified residue4201Phosphoserine By similarity
Modified residue4261Phosphothreonine By similarity
Modified residue4301Phosphoserine By similarity
Modified residue4361Phosphothreonine By similarity
Modified residue4451N6-acetyllysine; alternate By similarity
Modified residue4451N6-succinyllysine; alternate By similarity
Modified residue4461Phosphothreonine By similarity
Modified residue4581Phosphothreonine By similarity
Modified residue4591Phosphoserine By similarity
Glycosylation71O-linked (GlcNAc); alternate By similarity
Glycosylation331O-linked (GlcNAc); alternate By similarity
Glycosylation341O-linked (GlcNAc); alternate By similarity

Experimental info

Mutagenesis551S → A: Retains filamentous network during mitosis when transfected alone and when coexpressed with nestin. Ref.8
Mutagenesis458 – 4592TS → AA: Induces loss of filamentous network when coexpressed with nestin.

Sequences

Sequence LengthMass (Da)Tools
P31000 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 501CDCD706166829

FASTA46653,733
        10         20         30         40         50         60 
MSTRSVSSSS YRRMFGGSGT SSRPSSNRSY VTTSTRTYSL GSALRPSTSR SLYSSSPGGA 

        70         80         90        100        110        120 
YVTRSSAVRL RSSMPGVRLL QDSVDFSLAD AINTEFKNTR TNEKVELQEL NDRFANYIDK 

       130        140        150        160        170        180 
VRFLEQQNKI LLAELEQLKG QGKSRLGDLY EEEMRELRRQ VDQLTNDKAR VEVERDNLAE 

       190        200        210        220        230        240 
DIMRLREKLQ EEMLQREEAE STLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHDE 

       250        260        270        280        290        300 
EIQELQAQIQ EQHVQIDVDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE 

       310        320        330        340        350        360 
AANRNNDALR QAKQESNEYR RQVQSLTCEV DALKGTNESL ERQMREMEEN FALEAANYQD 

       370        380        390        400        410        420 
TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY RKLLEGEESR ISLPLPNFSS 

       430        440        450        460 
LNLRETNLES LPLVDTHSKR TLLIKTVETR DGQVINETSQ HHDDLE 

« Hide

References

« Hide 'large scale' references
[1]"Differential expression of vimentin in rat prostatic tumors."
Bussemakers M.J.G., Verhaegh G.W.C.T., van Bokhoven A., Debruyne F.M.J., Schalken J.A.
Biochem. Biophys. Res. Commun. 182:1254-1259(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Fischer.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
[3]"Proteome analysis of a rat liver nuclear insoluble protein fraction and localization of a novel protein, ISP36, to compartments in the interchromatin space."
Segawa M., Niino K., Mineki R., Kaga N., Murayama K., Sugimoto K., Watanabe Y., Furukawa K., Horigome T.
FEBS J. 272:4327-4338(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 37-50, SUBCELLULAR LOCATION.
Tissue: Liver.
[4]Lubec G., Afjehi-Sadat L., Kang S.U., Lubec S.
Submitted (SEP-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 51-64; 123-129; 223-235; 295-304; 321-341; 346-364; 391-401 AND 411-424, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain and Spinal cord.
[5]Paine M.L.
Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 86-160.
Tissue: Mammary gland.
[6]"The role of the vimentin intermediate filaments in rat 3Y1 cells elucidated by immunoelectron microscopy and computer-graphic reconstruction."
Katsumoto T., Mitsushima A., Kurimura T.
Biol. Cell 68:139-146(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Rab8B GTPase and junction dynamics in the testis."
Lau A.S., Mruk D.D.
Endocrinology 144:1549-1563(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB8B.
[8]"Nestin promotes the phosphorylation-dependent disassembly of vimentin intermediate filaments during mitosis."
Chou Y.-H., Khuon S., Herrmann H., Goldman R.D.
Mol. Biol. Cell 14:1468-1478(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-55, MUTAGENESIS OF SER-55 AND 458-THR-SER-459.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X62952 mRNA. Translation: CAA44722.1.
BC061847 mRNA. Translation: AAH61847.1.
M84481 mRNA. Translation: AAA42339.1.
PIRS22119.
RefSeqNP_112402.1. NM_031140.1.
UniGeneRn.2710.

3D structure databases

ProteinModelPortalP31000.
SMRP31000. Positions 101-138, 328-406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249676. 9 interactions.
IntActP31000. 6 interactions.
MINTMINT-4563959.
STRING10116.ENSRNOP00000024430.

PTM databases

PhosphoSiteP31000.

Proteomic databases

PaxDbP31000.
PRIDEP31000.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID81818.
KEGGrno:81818.
UCSCRGD:621646. rat.

Organism-specific databases

CTD7431.
RGD621646. Vim.

Phylogenomic databases

eggNOGNOG146769.
HOGENOMHOG000230977.
HOVERGENHBG013015.
InParanoidP31000.
KOK07606.
PhylomeDBP31000.

Gene expression databases

GenevestigatorP31000.

Family and domain databases

InterProIPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
IPR027699. Vimentin.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF27. PTHR23239:SF27. 1 hit.
PfamPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio615731.
PROP31000.

Entry information

Entry nameVIME_RAT
AccessionPrimary (citable) accession number: P31000
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 128 of the entry and version 2 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