ID VIME_MOUSE Reviewed; 466 AA. AC P20152; O08704; Q8CCH1; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 229. DE RecName: Full=Vimentin; GN Name=Vim; 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; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2744479; DOI=10.1016/0378-1119(89)90020-6; RA Wood L., Theriault N., Vogeli G.; RT "Vimentin cDNA clones covering the complete intermediate-filament protein RT are found in an EHS tumor cDNA library."; RL Gene 76:171-175(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; TISSUE=Spleen; RA Podolin P.L., Prystowsky M.B.; RL Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2325630; DOI=10.1007/bf00280364; RA Hennekes H., Kuehn S., Traub P.; RT "Coding sequence and flanking regions of the mouse vimentin gene."; RL Mol. Gen. Genet. 221:33-36(1990). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Smooth muscle; RX PubMed=2140597; RA Capetanaki Y., Kuisk I., Rothblum K., Starnes S.; RT "Mouse vimentin: structural relationship to fos, jun, CREB and tpr."; RL Oncogene 5:645-655(1990). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Rauscher A.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-115. RC STRAIN=BALB/cJ; RX PubMed=8543176; DOI=10.1016/0378-1119(95)00600-1; RA Nakamura N., Shida M., Hirayoshi K., Nagata K.; RT "Transcriptional regulation of the vimentin-encoding gene in mouse myeloid RT leukemia M1 cells."; RL Gene 166:281-286(1995). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 32-188. RC STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [8] RP PROTEIN SEQUENCE OF 5-69, AND PHOSPHORYLATION AT SER-7; SER-9; SER-10; RP SER-21; SER-25; SER-26; SER-34; SER-39; SER-42; SER-47; SER-51 AND SER-66. RC TISSUE=Smooth muscle; RX PubMed=2500966; DOI=10.1021/bi00433a035; RA Ando S., Tanabe K., Gonda Y., Sato C., Inagaki M.; RT "Domain- and sequence-specific phosphorylation of vimentin induces RT disassembly of the filament structure."; RL Biochemistry 28:2974-2979(1989). RN [9] RP PROTEIN SEQUENCE OF 72-91. RC TISSUE=Fibroblast; RX PubMed=7523108; DOI=10.1002/elps.11501501101; RA Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.; RT "Separation and sequencing of familiar and novel murine proteins using RT preparative two-dimensional gel electrophoresis."; RL Electrophoresis 15:735-745(1994). RN [10] RP PHOSPHORYLATION AT SER-39 AND SER-83. RX PubMed=1850997; DOI=10.1016/0006-291x(91)91658-y; RA Ando S., Tokui T., Yamauchi T., Sugiura H., Tanabe K., Inagaki M.; RT "Evidence that Ser-82 is a unique phosphorylation site on vimentin for RT Ca2(+)-calmodulin-dependent protein kinase II."; RL Biochem. Biophys. Res. Commun. 175:955-962(1991). RN [11] RP PHOSPHORYLATION AT SER-39 AND SER-72. RX PubMed=9565595; DOI=10.1074/jbc.273.19.11728; RA Goto H., Kosako H., Tanabe K., Yanagida M., Sakurai M., Amano M., RA Kaibuchi K., Inagaki M.; RT "Phosphorylation of vimentin by Rho-associated kinase at a unique amino- RT terminal site that is specifically phosphorylated during cytokinesis."; RL J. Biol. Chem. 273:11728-11736(1998). RN [12] RP INTERACTION WITH PLEC. RX PubMed=15128297; DOI=10.1111/j.1432-1033.2004.04095.x; RA Sevcik J., Urbanikova L., Kost'an J., Janda L., Wiche G.; RT "Actin-binding domain of mouse plectin. Crystal structure and binding to RT vimentin."; RL Eur. J. Biochem. 271:1873-1884(2004). RN [13] RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE. RC STRAIN=129/SvJ {ECO:0000269|PubMed:15037121}; RX PubMed=15037121; DOI=10.1016/j.exer.2003.09.028; RA Sandilands A., Wang X., Hutcheson A.M., James J., Prescott A.R., RA Wegener A., Pekny M., Gong X., Quinlan R.A.; RT "Bfsp2 mutation found in mouse 129 strains causes the loss of CP49' and RT induces vimentin-dependent changes in the lens fibre cell cytoskeleton."; RL Exp. Eye Res. 78:875-889(2004). RN [14] RP TISSUE SPECIFICITY. RX PubMed=14985306; DOI=10.1167/iovs.03-0677; RA Alizadeh A., Clark J., Seeberger T., Hess J., Blankenship T., RA FitzGerald P.G.; RT "Characterization of a mutation in the lens-specific CP49 in the 129 strain RT of mouse."; RL Invest. Ophthalmol. Vis. Sci. 45:884-891(2004). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic brain; 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 [16] 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 [17] RP INTERACTION WITH SYNM. RX PubMed=17356066; DOI=10.1242/jcs.03423; RA Jing R., Wilhelmsson U., Goodwill W., Li L., Pan Y., Pekny M., Skalli O.; RT "Synemin is expressed in reactive astrocytes in neurotrauma and interacts RT differentially with vimentin and GFAP intermediate filament networks."; RL J. Cell Sci. 120:1267-1277(2007). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-53 AND TYR-61, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Mast cell; RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864; 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; 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 [20] RP INTERACTION WITH LGSN. RX PubMed=18178558; DOI=10.1074/jbc.m709144200; RA Wyatt K., Gao C., Tsai J.-Y., Fariss R.N., Ray S., Wistow G.; RT "A role for lengsin, a recruited enzyme, in terminal differentiation in the RT vertebrate lens."; RL J. Biol. Chem. 283:6607-6615(2008). RN [21] RP INTERACTION WITH TOR1A. RX PubMed=18827015; DOI=10.1242/jcs.029454; RA Nery F.C., Zeng J., Niland B.P., Hewett J., Farley J., Irimia D., Li Y., RA Wiche G., Sonnenberg A., Breakefield X.O.; RT "TorsinA binds the KASH domain of nesprins and participates in linkage RT between nuclear envelope and cytoskeleton."; RL J. Cell Sci. 121:3476-3486(2008). RN [22] RP TISSUE SPECIFICITY. RX PubMed=19267394; DOI=10.1002/humu.20981; RA Roth W., Reuter U., Wohlenberg C., Bruckner-Tuderman L., Magin T.M.; RT "Cytokines as genetic modifiers in K5-/- mice and in human epidermolysis RT bullosa simplex."; RL Hum. Mutat. 30:832-841(2009). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-214 AND SER-459, AND 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 [24] RP INTERACTION WITH BFSP2 AND PPL, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RP AND DEVELOPMENTAL STAGE. RX PubMed=19029034; DOI=10.1167/iovs.08-2894; RA Yoon K.H., FitzGerald P.G.; RT "Periplakin interactions with lens intermediate and beaded filaments."; RL Invest. Ophthalmol. Vis. Sci. 50:1283-1289(2009). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-49; SER-56; SER-66; RP SER-420 AND SER-430, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Embryonic fibroblast; 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 [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-56; SER-83; SER-325; RP SER-419; SER-420 AND SER-459, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, RC Spleen, and Testis; 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 [27] RP TISSUE SPECIFICITY, IDENTIFICATION IN A COMPLEX WITH EZR; AHNAK; BFSP1; RP BFSP2; ANK2; PLEC; PRX AND SPECTRIN, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=21745462; DOI=10.1016/j.ydbio.2011.06.036; RA Maddala R., Skiba N.P., Lalane R. III, Sherman D.L., Brophy P.J., Rao P.V.; RT "Periaxin is required for hexagonal geometry and membrane organization of RT mature lens fibers."; RL Dev. Biol. 357:179-190(2011). RN [28] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-120; LYS-129; LYS-139; LYS-168; RP LYS-188; LYS-223; LYS-235; LYS-294 AND LYS-373, SUCCINYLATION [LARGE SCALE RP ANALYSIS] AT LYS-120; LYS-129; LYS-188; LYS-294 AND LYS-445, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; 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). RN [29] RP INTERACTION WITH PLEC. RX PubMed=24940650; DOI=10.1038/jid.2014.255; RA Bouameur J.E., Favre B., Fontao L., Lingasamy P., Begre N., Borradori L.; RT "Interaction of plectin with keratins 5 and 14: dependence on several RT plectin domains and keratin quaternary structure."; RL J. Invest. Dermatol. 134:2776-2783(2014). RN [30] RP INTERACTION WITH CORO1C. RX PubMed=27178841; DOI=10.1016/j.ejcb.2016.04.004; RA Behrens J., Solga R., Ziemann A., Rastetter R.H., Berwanger C., RA Herrmann H., Noegel A.A., Clemen C.S.; RT "Coronin 1C-free primary mouse fibroblasts exhibit robust rearrangements in RT the orientation of actin filaments, microtubules and intermediate RT filaments."; RL Eur. J. Cell Biol. 95:239-251(2016). RN [31] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=27559293; RA FitzGerald P., Sun N., Shibata B., Hess J.F.; RT "Expression of the type VI intermediate filament proteins CP49 and filensin RT in the mouse lens epithelium."; RL Mol. Vis. 22:970-989(2016). 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:0000250|UniProtKB:P31000}. CC -!- FUNCTION: Involved with LARP6 in the stabilization of type I collagen CC mRNAs for CO1A1 and CO1A2. {ECO:0000250|UniProtKB:P08670}. CC -!- SUBUNIT: Homomer assembled from elementary dimers (By similarity). CC Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, CC ANK2, PLEC, PRX and spectrin (PubMed:21745462). Interacts with BCAS3 CC (By similarity). Interacts with LGSN (PubMed:18178558). Interacts with CC SYNM (PubMed:17356066). Interacts (via rod region) with PLEC (via CH 1 CC domain) (PubMed:15128297). Interacts with PLEC isoform 1C CC (PubMed:24940650). Interacts with STK33 (By similarity). Interacts with CC LARP6 (By similarity). Interacts with RAB8B (By similarity). Interacts CC with TOR1A; the interaction associates TOR1A with the cytoskeleton CC (PubMed:18827015). Interacts with TOR1AIP1 (By similarity). Interacts CC with DIAPH1 (By similarity). Interacts with EPPK1; interaction is CC dependent of higher-order structure of intermediate filament (By CC similarity). Interacts with the non-receptor tyrosine kinase SRMS; the CC interaction leads to phosphorylation of VIM (By similarity). Interacts CC with NOD2 (By similarity). Interacts (via head region) with CORO1C CC (PubMed:27178841). Interacts with HDGF (By similarity). Interacts with CC PRKCE (via phorbol-ester/DAG-type 2 domain) (By similarity). Interacts CC with BFSP2 (PubMed:19029034). Interacts with PPL (PubMed:19029034). CC Interacts with PKP1 and PKP2 (By similarity). CC {ECO:0000250|UniProtKB:P08670, ECO:0000250|UniProtKB:P31000, CC ECO:0000269|PubMed:15128297, ECO:0000269|PubMed:17356066, CC ECO:0000269|PubMed:18178558, ECO:0000269|PubMed:18827015, CC ECO:0000269|PubMed:19029034, ECO:0000269|PubMed:21745462, CC ECO:0000269|PubMed:24940650, ECO:0000269|PubMed:27178841}. CC -!- INTERACTION: CC P20152; Q9R269: Ppl; NbExp=2; IntAct=EBI-299269, EBI-368293; CC P20152; P35465: Pak1; Xeno; NbExp=2; IntAct=EBI-299269, EBI-444379; CC P20152; Q96RG2: PASK; Xeno; NbExp=2; IntAct=EBI-299269, EBI-1042651; CC P20152; P17452: toxA; Xeno; NbExp=4; IntAct=EBI-299269, EBI-9541048; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19029034, CC ECO:0000269|PubMed:27559293}. Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:P08670}. Nucleus matrix CC {ECO:0000250|UniProtKB:P31000}. Cell membrane CC {ECO:0000269|PubMed:19029034}. CC -!- TISSUE SPECIFICITY: Detected in eye lens fiber cells (at protein level) CC (PubMed:15037121, PubMed:14985306, PubMed:19029034, PubMed:21745462, CC PubMed:27559293). Expressed in retinal lens epithelial cells (at CC protein level) (PubMed:27559293). Expressed in Langerhans cells in the CC epidermis (at protein level) (PubMed:19267394). CC {ECO:0000269|PubMed:14985306, ECO:0000269|PubMed:15037121, CC ECO:0000269|PubMed:19029034, ECO:0000269|PubMed:19267394, CC ECO:0000269|PubMed:21745462, ECO:0000269|PubMed:27559293}. CC -!- DEVELOPMENTAL STAGE: Expressed in the cytoplasm of anterior lens CC epithelial cells, expression becomes predominantly membranous as lens CC fiber cell differentiation progresses at 3 weeks of age. CC {ECO:0000269|PubMed:19029034}. CC -!- DOMAIN: The central alpha-helical coiled-coil IF rod domain mediates CC elementary homodimerization. {ECO:0000250}. CC -!- DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for CC cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 CC transnitrosylase complex. {ECO:0000250|UniProtKB:P08670}. CC -!- PTM: Phosphorylation by PKN1 inhibits the formation of filaments. CC Filament disassembly during mitosis is promoted by phosphorylation at CC Ser-55 as well as by nestin. One of the most prominent phosphoproteins CC in various cells of mesenchymal origin. Phosphorylation is enhanced CC during cell division, at which time vimentin filaments are CC significantly reorganized. Phosphorylated at Ser-56 by CDK5 during CC neutrophil secretion in the cytoplasm. Phosphorylated by STK33. CC Phosphorylated on tyrosine residues by SRMS. CC {ECO:0000250|UniProtKB:P08670, ECO:0000250|UniProtKB:P31000}. CC -!- PTM: S-nitrosylation is induced by interferon-gamma and oxidatively- CC modified low-densitity lipoprotein (LDL(ox)) possibly implicating the CC iNOS-S100A8/9 transnitrosylase complex. {ECO:0000250|UniProtKB:P08670}. CC -!- DISRUPTION PHENOTYPE: Morphological change from tubular conformation to CC circular conformation of beaded filament structures in retinal lens CC epithelium, potentially due to loss of contacts with surrounding CC intermediate filaments (PubMed:27559293). BFSP2 and VIM double knockout CC mice show a complete loss of cytoplasmic cytoskeleton in retinal lens CC fiber cells (PubMed:15037121). {ECO:0000269|PubMed:15037121, CC ECO:0000269|PubMed:27559293}. CC -!- SIMILARITY: Belongs to the intermediate filament family. CC {ECO:0000255|PROSITE-ProRule:PRU01188}. 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; M24849; AAA40555.1; -; mRNA. DR EMBL; X56397; CAA39807.1; -; mRNA. DR EMBL; M26251; AAA40556.1; -; mRNA. DR EMBL; Z22526; CAA80251.1; -; Genomic_DNA. DR EMBL; X51438; CAA35803.1; -; mRNA. DR EMBL; Y07738; CAA69019.1; -; Genomic_DNA. DR EMBL; AK033175; BAC28181.1; -; mRNA. DR EMBL; D50805; BAA19834.1; -; Genomic_DNA. DR CCDS; CCDS15696.1; -. DR PIR; A43803; A43803. DR RefSeq; NP_035831.2; NM_011701.4. DR AlphaFoldDB; P20152; -. DR SMR; P20152; -. DR BioGRID; 204524; 63. DR CORUM; P20152; -. DR DIP; DIP-188N; -. DR IntAct; P20152; 33. DR MINT; P20152; -. DR STRING; 10090.ENSMUSP00000028062; -. DR GlyCosmos; P20152; 3 sites, No reported glycans. DR GlyGen; P20152; 11 sites, 1 O-linked glycan (9 sites). DR iPTMnet; P20152; -. DR PhosphoSitePlus; P20152; -. DR SwissPalm; P20152; -. DR REPRODUCTION-2DPAGE; IPI00227299; -. DR EPD; P20152; -. DR jPOST; P20152; -. DR PaxDb; 10090-ENSMUSP00000028062; -. DR PeptideAtlas; P20152; -. DR ProteomicsDB; 298281; -. DR Pumba; P20152; -. DR Antibodypedia; 938; 4214 antibodies from 58 providers. DR DNASU; 22352; -. DR Ensembl; ENSMUST00000028062.8; ENSMUSP00000028062.3; ENSMUSG00000026728.10. DR GeneID; 22352; -. DR KEGG; mmu:22352; -. DR UCSC; uc008ikb.2; mouse. DR AGR; MGI:98932; -. DR CTD; 7431; -. DR MGI; MGI:98932; Vim. DR VEuPathDB; HostDB:ENSMUSG00000026728; -. DR eggNOG; KOG0977; Eukaryota. DR GeneTree; ENSGT00940000156146; -. DR InParanoid; P20152; -. DR OMA; GGMYATK; -. DR OrthoDB; 4640531at2759; -. DR PhylomeDB; P20152; -. DR TreeFam; TF330122; -. DR Reactome; R-MMU-264870; Caspase-mediated cleavage of cytoskeletal proteins. DR Reactome; R-MMU-390522; Striated Muscle Contraction. DR Reactome; R-MMU-9013422; RHOBTB1 GTPase cycle. DR Reactome; R-MMU-9646399; Aggrephagy. DR BioGRID-ORCS; 22352; 7 hits in 81 CRISPR screens. DR ChiTaRS; Vim; mouse. DR PRO; PR:P20152; -. DR Proteomes; UP000000589; Chromosome 2. DR RNAct; P20152; Protein. DR Bgee; ENSMUSG00000026728; Expressed in endothelial cell of lymphatic vessel and 280 other cell types or tissues. DR ExpressionAtlas; P20152; baseline and differential. DR GO; GO:0030424; C:axon; ISO:MGI. DR GO; GO:0044297; C:cell body; ISO:MGI. DR GO; GO:0031252; C:cell leading edge; IDA:MGI. DR GO; GO:0042995; C:cell projection; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0005882; C:intermediate filament; IDA:MGI. DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI. DR GO; GO:0043005; C:neuron projection; IDA:MGI. DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. DR GO; GO:0005777; C:peroxisome; ISO:MGI. DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005844; C:polysome; ISO:MGI. DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI. DR GO; GO:0045098; C:type III intermediate filament; TAS:MGI. DR GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:1990254; F:keratin filament binding; ISO:MGI. DR GO; GO:0019900; F:kinase binding; ISO:MGI. DR GO; GO:0060090; F:molecular adaptor activity; ISO:MGI. DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI. DR GO; GO:0051721; F:protein phosphatase 2A binding; ISO:MGI. DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI. DR GO; GO:0003723; F:RNA binding; IPI:MGI. DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IMP:MGI. DR GO; GO:0005212; F:structural constituent of eye lens; IDA:MGI. DR GO; GO:0014002; P:astrocyte development; IGI:MGI. DR GO; GO:0060020; P:Bergmann glial cell differentiation; IMP:MGI. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB. DR GO; GO:0071225; P:cellular response to muramyl dipeptide; ISS:UniProtKB. DR GO; GO:0071346; P:cellular response to type II interferon; IDA:MGI. DR GO; GO:0045109; P:intermediate filament organization; IMP:UniProtKB. DR GO; GO:0045103; P:intermediate filament-based process; IMP:MGI. DR GO; GO:0070307; P:lens fiber cell development; IDA:MGI. DR GO; GO:0010977; P:negative regulation of neuron projection development; IGI:MGI. DR GO; GO:0031175; P:neuron projection development; IGI:MGI. DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISO:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB. DR GO; GO:0060252; P:positive regulation of glial cell proliferation; ISO:MGI. DR GO; GO:0045727; P:positive regulation of translation; ISO:MGI. DR GO; GO:0050770; P:regulation of axonogenesis; ISO:MGI. DR GO; GO:0043488; P:regulation of mRNA stability; ISO:MGI. DR GO; GO:1900147; P:regulation of Schwann cell migration; ISO:MGI. 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. DR SWISS-2DPAGE; P20152; -. DR UCD-2DPAGE; P20152; -. DR Genevisible; P20152; MM. PE 1: Evidence at protein level; KW Acetylation; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Glycoprotein; Intermediate filament; KW Isopeptide bond; Membrane; Nucleus; Phosphoprotein; Reference proteome; KW S-nitrosylation; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P08670" FT CHAIN 2..466 FT /note="Vimentin" FT /id="PRO_0000063756" FT DOMAIN 103..411 FT /note="IF rod" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188" FT REGION 1..33 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2..95 FT /note="Head" FT REGION 96..131 FT /note="Coil 1A" FT REGION 132..153 FT /note="Linker 1" FT REGION 154..245 FT /note="Coil 1B" FT REGION 246..268 FT /note="Linker 12" FT REGION 269..407 FT /note="Coil 2" FT REGION 408..466 FT /note="Tail" FT COILED 96..131 FT COILED 154..245 FT COILED 303..407 FT MOTIF 326..329 FT /note="[IL]-x-C-x-x-[DE] motif" FT /evidence="ECO:0000250|UniProtKB:P08670" FT SITE 351 FT /note="Stutter" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:P08670" FT MOD_RES 5 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08670" FT MOD_RES 7 FT /note="Phosphoserine; by PKA and PKC; alternate" FT /evidence="ECO:0000269|PubMed:2500966" FT MOD_RES 8 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08670" FT MOD_RES 9 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000269|PubMed:2500966" FT MOD_RES 10 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000269|PubMed:2500966" FT MOD_RES 20 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P08670" FT MOD_RES 21 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000269|PubMed:2500966" FT MOD_RES 25 FT /note="Phosphoserine; by PKA and PKC" FT /evidence="ECO:0000269|PubMed:2500966" FT MOD_RES 26 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000269|PubMed:2500966" FT MOD_RES 34 FT /note="Phosphoserine; by PKC; alternate" FT /evidence="ECO:0000269|PubMed:2500966" FT MOD_RES 39 FT /note="Phosphoserine; by CaMK2, PKA, PKC and ROCK2" FT /evidence="ECO:0000269|PubMed:1850997, FT ECO:0000269|PubMed:2500966, ECO:0000269|PubMed:9565595, FT ECO:0007744|PubMed:19131326" FT MOD_RES 42 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000269|PubMed:2500966" FT MOD_RES 47 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000269|PubMed:2500966" FT MOD_RES 49 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19131326" FT MOD_RES 51 FT /note="Phosphoserine; by PKA and PKC" FT /evidence="ECO:0000269|PubMed:2500966, FT ECO:0007744|PubMed:21183079" FT MOD_RES 53 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:17947660" FT MOD_RES 55 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P31000" FT MOD_RES 56 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT MOD_RES 61 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:17947660" FT MOD_RES 66 FT /note="Phosphoserine; by PKA and PKC" FT /evidence="ECO:0000269|PubMed:2500966, FT ECO:0007744|PubMed:19131326" FT MOD_RES 72 FT /note="Phosphoserine; by AURKB and ROCK2" FT /evidence="ECO:0000269|PubMed:9565595" FT MOD_RES 73 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08670" FT MOD_RES 83 FT /note="Phosphoserine; by CaMK2" FT /evidence="ECO:0000269|PubMed:1850997, FT ECO:0007744|PubMed:15345747, ECO:0007744|PubMed:21183079" FT MOD_RES 87 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08670" FT MOD_RES 117 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P08670" FT MOD_RES 120 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 120 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 129 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 129 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 139 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 144 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08670" FT MOD_RES 168 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 188 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 188 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 214 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319" FT MOD_RES 223 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 226 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08670" FT MOD_RES 235 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 294 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 294 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 299 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08670" FT MOD_RES 325 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 373 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 409 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08670" FT MOD_RES 412 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P84198" FT MOD_RES 419 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 420 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19131326, FT ECO:0007744|PubMed:21183079" FT MOD_RES 426 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P08670" FT MOD_RES 430 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19131326" FT MOD_RES 436 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P08670" FT MOD_RES 438 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08670" FT MOD_RES 445 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P08670" FT MOD_RES 445 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 446 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P08670" FT MOD_RES 458 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P08670" FT MOD_RES 459 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT CARBOHYD 7 FT /note="O-linked (GlcNAc) serine; alternate" FT /evidence="ECO:0000250" FT CARBOHYD 33 FT /note="O-linked (GlcNAc) threonine" FT /evidence="ECO:0000250" FT CARBOHYD 34 FT /note="O-linked (GlcNAc) serine; alternate" FT /evidence="ECO:0000250" FT CROSSLNK 104 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P08670" FT CROSSLNK 120 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P08670" FT CROSSLNK 129 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P08670" FT CROSSLNK 139 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P08670" FT CROSSLNK 223 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P08670" FT CROSSLNK 262 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P08670" FT CROSSLNK 294 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P08670" FT CROSSLNK 313 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P08670" FT CROSSLNK 373 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P08670" FT CROSSLNK 439 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P08670" FT CROSSLNK 445 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:P08670" FT CROSSLNK 445 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P08670" FT CONFLICT 70 FT /note="L -> S (in Ref. 6; BAA19834)" FT /evidence="ECO:0000305" FT CONFLICT 110..115 FT /note="LNDRFA -> ILLAEL (in Ref. 6; BAA19834)" FT /evidence="ECO:0000305" FT CONFLICT 156..157 FT /note="EL -> DV (in Ref. 4; CAA35803)" FT /evidence="ECO:0000305" FT CONFLICT 164 FT /note="L -> F (in Ref. 2; CAA39807)" FT /evidence="ECO:0000305" FT CONFLICT 338 FT /note="E -> V (in Ref. 4; CAA35803)" FT /evidence="ECO:0000305" FT CONFLICT 374 FT /note="E -> D (in Ref. 1; AAA40555)" FT /evidence="ECO:0000305" 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 //