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 //