ID Q5FWJ3_MOUSE Unreviewed; 466 AA.
AC Q5FWJ3;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 170.
DE RecName: Full=Vimentin {ECO:0000256|ARBA:ARBA00014147};
GN Name=Vim {ECO:0000313|EMBL:AAH89335.1, ECO:0000313|MGI:MGI:98932};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAH89335.1};
RN [1] {ECO:0000313|EMBL:BAE21803.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21803.1}, and NOD
RC {ECO:0000313|EMBL:BAE41790.1};
RC TISSUE=Head {ECO:0000313|EMBL:BAE21803.1};
RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA Carninci P., Hayashizaki Y.;
RT "High-efficiency full-length cDNA cloning.";
RL Methods Enzymol. 303:19-44(1999).
RN [2] {ECO:0000313|EMBL:BAE21803.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21803.1}, and NOD
RC {ECO:0000313|EMBL:BAE41790.1};
RC TISSUE=Head {ECO:0000313|EMBL:BAE21803.1};
RX PubMed=11042159; DOI=10.1101/gr.145100;
RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT full-length cDNA libraries for rapid discovery of new genes.";
RL Genome Res. 10:1617-1630(2000).
RN [3] {ECO:0000313|EMBL:BAE21803.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21803.1}, and NOD
RC {ECO:0000313|EMBL:BAE41790.1};
RC TISSUE=Head {ECO:0000313|EMBL:BAE21803.1};
RX PubMed=11076861; DOI=10.1101/gr.152600;
RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT pipeline with 384 multicapillary sequencer.";
RL Genome Res. 10:1757-1771(2000).
RN [4] {ECO:0000313|EMBL:BAE21803.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21803.1}, and NOD
RC {ECO:0000313|EMBL:BAE41790.1};
RC TISSUE=Head {ECO:0000313|EMBL:BAE21803.1};
RX PubMed=11217851; DOI=10.1038/35055500;
RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT "Functional annotation of a full-length mouse cDNA collection.";
RL Nature 409:685-690(2001).
RN [5] {ECO:0000313|EMBL:BAE21803.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21803.1}, and NOD
RC {ECO:0000313|EMBL:BAE41790.1};
RC TISSUE=Head {ECO:0000313|EMBL:BAE21803.1};
RX PubMed=12466851; DOI=10.1038/nature01266;
RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT "Analysis of the mouse transcriptome based on functional annotation of
RT 60,770 full-length cDNAs.";
RL Nature 420:563-573(2002).
RN [6] {ECO:0000313|EMBL:AAH89335.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6 {ECO:0000313|EMBL:AAH89335.1};
RC TISSUE=Brain {ECO:0000313|EMBL:AAH89335.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7] {ECO:0007829|PubMed:15345747}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [8] {ECO:0000313|EMBL:BAE41790.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21803.1}, and NOD
RC {ECO:0000313|EMBL:BAE41790.1};
RC TISSUE=Head {ECO:0000313|EMBL:BAE21803.1};
RA Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F.,
RA Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M.,
RA Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K.,
RA Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T.,
RA Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [9] {ECO:0007829|PubMed:15592455}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [10] {ECO:0000313|EMBL:BAE21803.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21803.1}, and NOD
RC {ECO:0000313|EMBL:BAE41790.1};
RC TISSUE=Head {ECO:0000313|EMBL:BAE21803.1};
RG The FANTOM Consortium;
RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT "The Transcriptional Landscape of the Mammalian Genome.";
RL Science 309:1559-1563(2005).
RN [11] {ECO:0000313|EMBL:BAE21803.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE21803.1}, and NOD
RC {ECO:0000313|EMBL:BAE41790.1};
RC TISSUE=Head {ECO:0000313|EMBL:BAE21803.1};
RX PubMed=16141073; DOI=10.1126/science.1112009;
RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT "Antisense Transcription in the Mammalian Transcriptome.";
RL Science 309:1564-1566(2005).
RN [12] {ECO:0007829|PubMed:17947660}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17947660;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [13] {ECO:0007829|PubMed:17242355}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [14] {ECO:0007829|PubMed:19144319}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [15] {ECO:0007829|PubMed:19131326}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [16] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [17] {ECO:0007829|PubMed:23806337}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Involved with LARP6 in the stabilization of type I collagen
CC mRNAs for CO1A1 and CO1A2. {ECO:0000256|ARBA:ARBA00003885}.
CC -!- FUNCTION: Vimentins are class-III intermediate filaments found in
CC various non-epithelial cells, especially mesenchymal cells. Vimentin is
CC attached to the nucleus, endoplasmic reticulum, and mitochondria,
CC either laterally or terminally. {ECO:0000256|ARBA:ARBA00002825}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Nucleus matrix {ECO:0000256|ARBA:ARBA00004109}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000256|RuleBase:RU000685}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC089335; AAH89335.1; -; mRNA.
DR EMBL; AK133726; BAE21803.1; -; mRNA.
DR EMBL; AK170429; BAE41790.1; -; mRNA.
DR RefSeq; NP_035831.2; NM_011701.4.
DR AlphaFoldDB; Q5FWJ3; -.
DR SMR; Q5FWJ3; -.
DR MaxQB; Q5FWJ3; -.
DR TopDownProteomics; Q5FWJ3; -.
DR Antibodypedia; 938; 4214 antibodies from 58 providers.
DR DNASU; 22352; -.
DR GeneID; 22352; -.
DR KEGG; mmu:22352; -.
DR AGR; MGI:98932; -.
DR CTD; 7431; -.
DR MGI; MGI:98932; Vim.
DR VEuPathDB; HostDB:ENSMUSG00000026728; -.
DR OMA; GGMYATK; -.
DR OrthoDB; 4640531at2759; -.
DR BioGRID-ORCS; 22352; 7 hits in 81 CRISPR screens.
DR ChiTaRS; Vim; mouse.
DR ExpressionAtlas; Q5FWJ3; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:1990254; F:keratin filament binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0071225; P:cellular response to muramyl dipeptide; IEA:Ensembl.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl.
DR GO; GO:0043488; P:regulation of mRNA stability; IEA:Ensembl.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.5.500; Single helix bin; 1.
DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR PANTHER; PTHR45652; GLIAL FIBRILLARY ACIDIC PROTEIN; 1.
DR PANTHER; PTHR45652:SF5; VIMENTIN; 1.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF04732; Filament_head; 1.
DR SMART; SM01391; Filament; 1.
DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Intermediate filament {ECO:0000256|ARBA:ARBA00022754,
KW ECO:0000256|RuleBase:RU000685};
KW S-nitrosylation {ECO:0000256|ARBA:ARBA00022799}.
FT DOMAIN 103..411
FT /note="IF rod"
FT /evidence="ECO:0000259|PROSITE:PS51842"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 93..255
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 295..389
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 466 AA; 53688 MW; A94EECEA6D70C899 CRC64;
MSTRSVSSSS YRRMFGGSGT SSRPSSNRSY VTTSTRTYSL GSALRPSTSR SLYSSSPGGA
YVTRSSAVRL RSSVPGVRLL QDSVDFSLAD AINTEFKNTR TNEKVELQEL NDRFANYIDK
VRFLEQQNKI LLAELEQLKG QGKSRLGDLY EEEMRELRRQ VDQLTNDKAR VEVERDNLAE
DIMRLREKLQ EEMLQREEAE STLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHDE
EIQELQAQIQ EQHVQIDVDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE
AANRNNDALR QAKQESNEYR RQVQSLTCEV DALKGTNESL ERQMREMEEN FALEAANYQD
TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY RKLLEGEESR ISLPLPTFSS
LNLRETNLES LPLVDTHSKR TLLIKTVETR DGQVINETSQ HHDDLE
//