VIME_MOUSE
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 03-AUG-2022, entry version 220.
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, Spleen,
RC 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.
CC -!- FUNCTION: Involved with LARP6 in the stabilization of type I collagen
CC mRNAs for CO1A1 and CO1A2. {ECO:0000250}.
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 {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; 59.
DR CORUM; P20152; -.
DR DIP; DIP-188N; -.
DR IntAct; P20152; 33.
DR MINT; P20152; -.
DR STRING; 10090.ENSMUSP00000028062; -.
DR GlyGen; P20152; 3 sites.
DR iPTMnet; P20152; -.
DR PhosphoSitePlus; P20152; -.
DR SwissPalm; P20152; -.
DR REPRODUCTION-2DPAGE; IPI00227299; -.
DR SWISS-2DPAGE; P20152; -.
DR UCD-2DPAGE; P20152; -.
DR EPD; P20152; -.
DR jPOST; P20152; -.
DR PaxDb; P20152; -.
DR PeptideAtlas; P20152; -.
DR PRIDE; P20152; -.
DR ProteomicsDB; 298281; -.
DR Antibodypedia; 938; 3618 antibodies from 58 providers.
DR DNASU; 22352; -.
DR Ensembl; ENSMUST00000028062; ENSMUSP00000028062; ENSMUSG00000026728.
DR GeneID; 22352; -.
DR KEGG; mmu:22352; -.
DR UCSC; uc008ikb.2; mouse.
DR CTD; 7431; -.
DR MGI; MGI:98932; Vim.
DR VEuPathDB; HostDB:ENSMUSG00000026728; -.
DR eggNOG; KOG0977; Eukaryota.
DR GeneTree; ENSGT00940000156146; -.
DR InParanoid; P20152; -.
DR OMA; PPMRLHD; -.
DR OrthoDB; 655109at2759; -.
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 76 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 277 other tissues.
DR ExpressionAtlas; P20152; baseline and differential.
DR Genevisible; P20152; MM.
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:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase 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:0071346; P:cellular response to interferon-gamma; IDA: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: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 GO; GO:0060395; P:SMAD protein signal transduction; IDA:MGI.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR InterPro; IPR027699; Vimentin.
DR PANTHER; PTHR45652:SF5; PTHR45652:SF5; 1.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF04732; Filament_head; 1.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
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
