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Vimentin

 U3IRY0_ANAPL            Unreviewed;       465 AA.
U3IRY0;
13-NOV-2013, integrated into UniProtKB/TrEMBL.
13-NOV-2013, sequence version 1.
10-OCT-2018, entry version 35.
SubName: Full=Vimentin {ECO:0000313|Ensembl:ENSAPLP00000010003};
Name=VIM {ECO:0000313|Ensembl:ENSAPLP00000010003};
Anas platyrhynchos (Mallard) (Anas boschas).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
Anatinae; Anas.
NCBI_TaxID=8839 {ECO:0000313|Ensembl:ENSAPLP00000010003, ECO:0000313|Proteomes:UP000016666};
[1] {ECO:0000313|Ensembl:ENSAPLP00000010003}
NUCLEOTIDE SEQUENCE.
Li N.;
"The genome sequence and transcriptome of duck provide insight into
the interaction host.";
Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|Ensembl:ENSAPLP00000010003}
NUCLEOTIDE SEQUENCE.
PubMed=23749191; DOI=10.1038/ng.2657;
Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H.,
Gan S., Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q.,
Fairley S., Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A.,
Lee T., Kim K.W., Sheng Z., An Y., Searle S., Herrero J.,
Groenen M.A., Crooijmans R.P., Faraut T., Cai Q., Webster R.G.,
Aldridge J.R., Warren W.C., Bartschat S., Kehr S., Marz M.,
Stadler P.F., Smith J., Kraus R.H., Zhao Y., Ren L., Fei J.,
Morisson M., Kaiser P., Griffin D.K., Rao M., Pitel F., Wang J.,
Li N.;
"The duck genome and transcriptome provide insight into an avian
influenza virus reservoir species.";
Nat. Genet. 45:776-783(2013).
[3] {ECO:0000313|Ensembl:ENSAPLP00000010003}
IDENTIFICATION.
Ensembl;
Submitted (SEP-2013) 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; ADON01030569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; ADON01030570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
Ensembl; ENSAPLT00000010706; ENSAPLP00000010003; ENSAPLG00000010218.
GeneTree; ENSGT00910000143989; -.
OMA; QVINEST; -.
OrthoDB; EOG091G12MK; -.
Proteomes; UP000016666; Unassembled WGS sequence.
GO; GO:0005623; C:cell; ISS:AgBase.
GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
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:UP000016666};
Intermediate filament {ECO:0000256|PROSITE-ProRule:PRU01188,
ECO:0000256|RuleBase:RU000685, ECO:0000256|SAAS:SAAS01036494};
Reference proteome {ECO:0000313|Proteomes:UP000016666}.
DOMAIN 99 409 IF rod. {ECO:0000259|PROSITE:PS51842}.
COILED 89 137 {ECO:0000256|SAM:Coils}.
COILED 143 184 {ECO:0000256|SAM:Coils}.
COILED 208 253 {ECO:0000256|SAM:Coils}.
COILED 293 387 {ECO:0000256|SAM:Coils}.
SEQUENCE 465 AA; 53433 MW; 5F71CCB7FCD6C016 CRC64;
AATMSISSKN SSYRRMFGGG SRPSTSSRYV VSSSSRFSGS SLRPSSARFV SASPGGIYAT
KATSVRLRSS MPPMRLHDAV DFTLADAINS EFKANRTNEK VELQELNDRF ANYIEKVRFL
EQQNKILLAE LEQLKGKGTS RLGDLYEEEM RELRRQVDQL TNDKARVEVE RDNLADDITR
LREKFGMLQE MLHCSDIANW SSLSHQDVDN ASLARLDLER KVESLQEEIV FLKKLHDEEI
RELQAQLQEQ HIQIDMDVSK PDLTAALRDV RQQYESVAAK NLQEAEEWYK SKFADLSEAA
NRNNDALRQA KQEANEYRRQ IQSLTCEVDA LKGSNESLER QMREMEENFA LEAANYQDTI
GRLQDEIQNM KEEMARHLRE YQDLLNVKMA LDIEIATYRK LLEGEESRIN MPIPTFASLN
LRAETNIESQ PMVDTHSKRT LLIKTVETRD GQVINETSQH HDDLE


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