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P02544 (VIME_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 92. 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
OrganismMesocricetus auratus (Golden hamster)
Taxonomic identifier10036 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Mesocricetus

Protein attributes

Sequence length465 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.

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

Subunit structure

Homopolymer assembled from elementary dimers. 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. Interacts with LARP6 By similarity. Interacts with RAB8B By similarity.

Subcellular location

Cytoplasm By similarity.

Domain

The central alpha-helical coiled-coil rod region mediates elementary homodimerization By similarity.

Post-translational modification

Phosphorylation by PKN1 inhibits the formation of filaments. Filament disassembly during mitosis is promoted by phosphorylation at Ser-54 as well as by nestin By similarity. 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. Phosphorylated at Ser-55 by CDK5 during neutrophil secretion in the cytoplasm. Phosphorylated by STK33 By similarity. Ref.3

Sequence similarities

Belongs to the intermediate filament family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 465464Vimentin
PRO_0000063755

Regions

Region2 – 9493Head
Region95 – 406312Rod
Region95 – 13036Coil 1A
Region131 – 15222Linker 1
Region153 – 24492Coil 1B
Region245 – 26723Linker 12
Region268 – 406139Coil 2
Region407 – 46559Tail
Coiled coil95 – 13036
Coiled coil153 – 24492
Coiled coil302 – 406105

Sites

Site3501Stutter By similarity

Amino acid modifications

Modified residue21N-acetylserine
Modified residue51Phosphoserine By similarity
Modified residue71Phosphoserine; by PKA and PKC By similarity
Modified residue81Phosphoserine By similarity
Modified residue91Phosphoserine; by PKC By similarity
Modified residue101Phosphoserine; by PKC By similarity
Modified residue201Phosphothreonine By similarity
Modified residue211Phosphoserine; by PKC By similarity
Modified residue251Phosphoserine; by PKA and PKC By similarity
Modified residue261Phosphoserine; by PKC By similarity
Modified residue291Phosphoserine By similarity
Modified residue331Phosphothreonine By similarity
Modified residue341Phosphoserine; by PKC By similarity
Modified residue381Phosphotyrosine By similarity
Modified residue391Phosphoserine; by CaMK2, PKA, PKC and ROCK2 By similarity
Modified residue421Phosphoserine; by PKC By similarity
Modified residue461Phosphoserine; by PKA By similarity
Modified residue481Phosphoserine By similarity
Modified residue501Phosphoserine; by PKA and PKC By similarity
Modified residue521Phosphotyrosine By similarity
Modified residue541Phosphoserine By similarity
Modified residue551Phosphoserine; by CDK5 and CDK1 Ref.3
Modified residue601Phosphotyrosine By similarity
Modified residue651Phosphoserine By similarity
Modified residue711Phosphoserine; by AURKB and ROCK2 By similarity
Modified residue721Phosphoserine By similarity
Modified residue821Phosphoserine By similarity
Modified residue1031N6-acetyllysine By similarity
Modified residue1161Phosphotyrosine By similarity
Modified residue1191N6-acetyllysine By similarity
Modified residue1381N6-acetyllysine By similarity
Modified residue1431Phosphoserine By similarity
Modified residue2131Phosphoserine By similarity
Modified residue2251Phosphoserine By similarity
Modified residue2601Phosphoserine By similarity
Modified residue2651Phosphothreonine By similarity
Modified residue2911N6-acetyllysine By similarity
Modified residue2981Phosphoserine By similarity
Modified residue3721N6-acetyllysine By similarity
Modified residue4011N6-acetyllysine By similarity
Modified residue4081Phosphoserine By similarity
Modified residue4111Phosphoserine By similarity
Modified residue4181Phosphoserine By similarity
Modified residue4191Phosphoserine By similarity
Modified residue4251Phosphothreonine By similarity
Modified residue4291Phosphoserine By similarity
Modified residue4351Phosphothreonine By similarity
Modified residue4441N6-acetyllysine By similarity
Modified residue4451Phosphothreonine By similarity
Modified residue4571Phosphothreonine By similarity
Modified residue4581Phosphoserine By similarity

Experimental info

Sequence conflict431L → A Ref.2
Sequence conflict1161Y → D Ref.2
Sequence conflict1831R → I Ref.2

Sequences

Sequence LengthMass (Da)Tools
P02544 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 81E6B65451E3EC54

FASTA46553,730
        10         20         30         40         50         60 
MSTRSVSSSS YRRMFGGPGT SNRQSSNRSY VTTSTRTYSL GSLRPSTSRS LYSSSPGGAY 

        70         80         90        100        110        120 
VTRSSAVRLR SSMPGVRLLQ DSVDFSLADA INTEFKNTRT NEKVELQELN DRFANYIDKV 

       130        140        150        160        170        180 
RFLEQQNKIL LAELEQLKGQ GKSRLGDLYE EEMRELRRQV DQLTNDKARV EVERDNLAED 

       190        200        210        220        230        240 
IMRLREKLQE EMLQREEAES TLQSFRQDVD NASLARLDLE RKVESLQEEI AFLKKLHDEE 

       250        260        270        280        290        300 
IQELQAQIQE QHVQIDVDVS KPDLTAALRD VRQQYESVAA KNLQEAEEWY KSKFADLSEA 

       310        320        330        340        350        360 
ANRNNDALRQ AKQESNEYRR QVQSLTCEVD ALKGTNESLE RQMREMEENF ALEAANYQDT 

       370        380        390        400        410        420 
IGRLQDEIQN MKEEMARHLR EYQDLLNVKM ALDIEIATYR KLLEGEESRI SLPLPNFSSL 

       430        440        450        460 
NLRETNLESL PLVDTHSKRT LLIKTVETRD GQVINETSQH HDDLE

« Hide

References

[1]"The structure of the vimentin gene."
Quax W.J., Egberts W.V., Hendriks W., Quax-Jeuken Y.E.F.M., Bloemendal H.
Cell 35:215-223(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Lens.
[2]"Primary and secondary structure of hamster vimentin predicted from the nucleotide sequence."
Quax-Jeuken Y.E.F.M., Quax W.J., Bloemendal H.
Proc. Natl. Acad. Sci. U.S.A. 80:3548-3552(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Lens.
[3]"The regulation of intermediate filament reorganization in mitosis. p34cdc2 phosphorylates vimentin at a unique N-terminal site."
Chou Y.-H., Ngai K.-L., Goldman R.
J. Biol. Chem. 266:7325-7328(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-55.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		K00927 expand/collapse EMBL AC list , K00921, K00922, K00923, K00924, K00925, K00926 Genomic DNA. Translation: AAA37104.1.
PIRVEHY. A90842.

3D structure databases

ProteinModelPortalP02544.
SMRP02544. Positions 100-137, 327-405.
ModBaseSearch...

Proteomic databases

PRIDEP02544.

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. PTHR23239. 1 hit.
PfamPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVIME_MESAU
AccessionPrimary (citable) accession number: P02544
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 92 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

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