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Vimentin

 F1NJ08_CHICK            Unreviewed;       460 AA.
F1NJ08;
03-MAY-2011, integrated into UniProtKB/TrEMBL.
03-MAY-2011, sequence version 1.
10-APR-2019, entry version 60.
SubName: Full=Vimentin {ECO:0000313|Ensembl:ENSGALP00000014107};
Name=VIM {ECO:0000313|Ensembl:ENSGALP00000014107};
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00000014107, ECO:0000313|Proteomes:UP000000539};
[1] {ECO:0000313|Ensembl:ENSGALP00000014107, ECO:0000313|Proteomes:UP000000539}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000014107,
ECO:0000313|Proteomes:UP000000539};
PubMed=15592404; DOI=10.1038/nature03154;
International Chicken Genome Sequencing Consortium;
Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C.,
Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E.,
Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W.,
Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A., Kremitzki C.,
Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E.,
Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J.,
Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M.,
Paton B., Smith J., Morrice D., Daniels L., Tempest H.G.,
Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V.,
Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J.,
van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J.,
Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H.,
Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S.,
Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J.,
Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H.,
Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C.,
Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C.,
Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P.,
King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S.,
Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S.,
Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S.,
Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z.,
Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J.,
Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z.,
Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J.,
Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G.,
Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D.,
Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G.,
Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A.,
Mardis E.R., Wilson R.K.;
"Sequence and comparative analysis of the chicken genome provide
unique perspectives on vertebrate evolution.";
Nature 432:695-716(2004).
[2] {ECO:0000313|Ensembl:ENSGALP00000014107}
IDENTIFICATION.
STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000014107};
Ensembl;
Submitted (JUL-2011) to UniProtKB.
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000256|PROSITE-ProRule:PRU01188,
ECO:0000256|RuleBase:RU000685, ECO:0000256|SAAS:SAAS01036505}.
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EMBL; AADN05000033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_001041541.2; NM_001048076.2.
UniGene; Gga.9346; -.
PRIDE; F1NJ08; -.
Ensembl; ENSGALT00000014123; ENSGALP00000014107; ENSGALG00000008677.
GeneID; 420519; -.
KEGG; gga:420519; -.
CTD; 7431; -.
eggNOG; ENOG410IFZ1; Eukaryota.
eggNOG; ENOG410XRBS; LUCA.
GeneTree; ENSGT00940000156146; -.
KO; K07606; -.
OMA; QVINEST; -.
OrthoDB; 655109at2759; -.
PhylomeDB; F1NJ08; -.
TreeFam; TF330122; -.
Reactome; R-GGA-264870; Caspase-mediated cleavage of cytoskeletal proteins.
Reactome; R-GGA-390522; Striated Muscle Contraction.
Proteomes; UP000000539; Chromosome 2.
Bgee; ENSGALG00000008677; Expressed in 10 organ(s), highest expression level in female gonad.
ExpressionAtlas; F1NJ08; baseline and differential.
GO; GO:0005623; C:cell; IDA:AgBase.
GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
GO; GO:0042995; C:cell projection; IDA:AgBase.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0005777; C:peroxisome; IEA:Ensembl.
GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0005844; C:polysome; IEA:Ensembl.
GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:1990254; F:keratin filament binding; IEA:Ensembl.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:Ensembl.
GO; GO:0005212; F:structural constituent of eye lens; IEA:Ensembl.
GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
GO; GO:0060020; P:Bergmann glial cell differentiation; IEA:Ensembl.
GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0071225; P:cellular response to muramyl dipeptide; IEA:Ensembl.
GO; GO:0045109; P:intermediate filament organization; IEA:Ensembl.
GO; GO:0070307; P:lens fiber cell development; IEA:Ensembl.
GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl.
GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
GO; GO:0043488; P:regulation of mRNA stability; IEA:Ensembl.
GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
InterPro; IPR001664; IF.
InterPro; IPR018039; IF_conserved.
InterPro; IPR039008; IF_rod_dom.
InterPro; IPR006821; Intermed_filament_DNA-bd.
InterPro; IPR027699; Vimentin.
PANTHER; PTHR23239; PTHR23239; 1.
PANTHER; PTHR23239:SF27; PTHR23239:SF27; 1.
Pfam; PF00038; Filament; 1.
Pfam; PF04732; Filament_head; 1.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
3: Inferred from homology;
Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01188,
ECO:0000256|SAAS:SAAS01036532, ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000000539};
Intermediate filament {ECO:0000256|PROSITE-ProRule:PRU01188,
ECO:0000256|RuleBase:RU000685, ECO:0000256|SAAS:SAAS01036494};
Reference proteome {ECO:0000313|Proteomes:UP000000539}.
DOMAIN 97 405 IF rod. {ECO:0000259|PROSITE:PS51842}.
COILED 87 135 {ECO:0000256|SAM:Coils}.
COILED 141 249 {ECO:0000256|SAM:Coils}.
COILED 289 383 {ECO:0000256|SAM:Coils}.
SEQUENCE 460 AA; 53215 MW; 06F894EA0AFC3AB0 CRC64;
MSFTSSKNSS YRRMFGGGSR PSSGTRYITS STRYSLGSAL RPSSARYVSA SPGGVYATKA
TSVRLRSSMP PMRMHDAVDF TLADAINTEF KANRTNEKVE LQELNDRFAN YIDKVRFLEQ
QNKILLAELE QLKGKGTSRL GDLYEEEMRE LRRQVDQLTN DKARVEVERD NLADDIMRLR
EKLQEEMLQR EEAESTLQSF RQDVDNASLA RLDLERKVES LQEEIVFLKK LHDEEIRELQ
AQLQEQHIQI DMDVSKPDLT AALRDVRQQY ESVAAKNLQE AEEWYKSKFA DLSEAANRNN
DALRQAKQEA NEYRRQIQSL TCEVDALKGS NESLERQMRE MEENFAVEAA NYQDTIGRLQ
DEIQNMKEEM ARHLREYQDL LNVKMALDIE IATYRKLLEG EESRINMPIP TFASLNLRET
NIESQPIVDT HSKRTLLIKT VETRDGQVIN ETSQHHDDLE


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1C-460-C100 Mouse Monoclonal to Vimentin Antigen Vimentin Isotype IgM Antigen Vimentin Isotype IgM 0.1 mg
1C-460-C025 Mouse Monoclonal to Vimentin Antigen Vimentin Isotype IgM Antigen Vimentin Isotype IgM 0.025 mg
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Related Genes :
[VIM] Vimentin
[Vim] Vimentin
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[Ctsg] Cathepsin G (EC 3.4.21.20) (Vimentin-specific protease) (VSP)
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[VIM] Vimentin
[VIM] Vimentin (Fragment)
[VIM] Vimentin
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[VIM] Vimentin (Fragment)
[Vim rCG_55877] Vimentin (Vimentin, isoform CRA_b)
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[vim1; vim2] Vimentin-1/2
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[VIM CK820_G0041162] VIM isoform 1 (VIM isoform 2) (VIM isoform 5) (Vimentin)
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Bibliography :
[30995202] Vimentin is required for normal accumulation of body fat.
[30995157] Rudhira/BCAS3 couples microtubules and intermediate filaments to promote cell migration for angiogenic remodeling.
[30992462] p27/Kip1 functions as a tumor suppressor and oncoprotein in osteosarcoma.
[30992429] Development of a patient-derived xenograft model of glioblastoma via intravitreal injection in mice.
[30989663] Loss of G3BP1 suppresses proliferation, migration, and invasion of esophageal cancer cells via Wnt/β-catenin and PI3K/AKT signaling pathways.
[30989413] Polymeric Micellar Formulation Enhances Antimicrobial and Anticancer Properties of Salinomycin.
[30988817] Metadherin overexpression in perihilar cholangiocarcinoma is associated with lymph node metastasis and poor prognosis.
[30988806] Effect of asiatic acid on epithelial-mesenchymal transition of human alveolar epithelium A549 cells induced by TGF-β1.
[30988707] Overexpression of fibronectin type III domain containing 3B is correlated with epithelial-mesenchymal transition and predicts poor prognosis in lung adenocarcinoma.
[30988641] JAM3 functions as a novel tumor suppressor and is inactivated by DNA methylation in colorectal cancer.