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Vimentin

 VIME_ONCMY              Reviewed;         461 AA.
P48674;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
16-JAN-2019, entry version 70.
RecName: Full=Vimentin;
Name=vim;
Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii;
Salmoniformes; Salmonidae; Salmoninae; Oncorhynchus.
NCBI_TaxID=8022;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Spleen;
PubMed=8907703;
Herrmann H., Muenick M.D., Brettel M., Fouquet B., Markl J.;
"Vimentin in a cold-water fish, the rainbow trout: highly conserved
primary structure but unique assembly properties.";
J. Cell Sci. 109:569-578(1996).
-!- FUNCTION: Vimentins are class-III intermediate filaments found in
various non-epithelial cells, especially mesenchymal cells.
Vimentin is attached to the nucleus, endoplasmic reticulum, and
mitochondria, either laterally or terminally.
-!- SUBUNIT: Homopolymer assembled from elementary dimers.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08670}.
Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08670}. Nucleus
matrix {ECO:0000250|UniProtKB:P31000}.
-!- DOMAIN: The central alpha-helical coiled-coil IF rod domain
mediates elementary homodimerization. {ECO:0000250}.
-!- PTM: One of the most prominent phosphoproteins in various cells of
mesenchymal origin. Phosphorylation is enhanced during cell
division, at which time vimentin filaments are significantly
reorganized. {ECO:0000250|UniProtKB:P08670}.
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000255|PROSITE-ProRule:PRU01188}.
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EMBL; Z50738; CAA90601.1; -; mRNA.
RefSeq; NP_001118201.1; NM_001124729.1.
UniGene; Omy.11950; -.
ProteinModelPortal; P48674; -.
SMR; P48674; -.
PRIDE; P48674; -.
GeneID; 100136784; -.
CTD; 7431; -.
HOVERGEN; HBG013015; -.
OrthoDB; 655109at2759; -.
GO; GO:0005737; C:cytoplasm; IDA:AgBase.
GO; GO:0005856; C:cytoskeleton; IDA:AgBase.
GO; GO:0005882; C:intermediate filament; ISS:UniProtKB.
GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
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.
2: Evidence at transcript level;
Coiled coil; Cytoplasm; Cytoskeleton; Intermediate filament; Nucleus.
CHAIN 1 461 Vimentin.
/FTId=PRO_0000063768.
DOMAIN 99 407 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 1 91 Head.
REGION 92 127 Coil 1A.
REGION 128 149 Linker 1.
REGION 150 241 Coil 1B.
REGION 242 264 Linker 12.
REGION 265 403 Coil 2.
REGION 404 461 Tail.
COILED 92 127
COILED 150 241
COILED 299 403
SITE 347 347 Stutter. {ECO:0000250}.
SEQUENCE 461 AA; 53325 MW; D49B1DE4F79D2E30 CRC64;
MNRTTSRQTT SSSSYKRMFG GEGRPSVGMA RSTLSSRQYS SPVRSSRMSY SVSAPPSIYA
SKNVRLRSSA PMPRLSSDTV DFALSDAINS EFKANRTNEK AEMQHLNDRF ASYIDKVRFL
EQQNKILLAE LEQLKGKGAS RIGDLYEDEM RDLRRQVDQL TNEKAHVEVD RDNMGEDIER
LREKLQDEMI QKEEAEHNLQ SFRQDVDNAS LARLDLERKV ESLQEEIIFL RKLHDEEVAE
LQAQIQDQHV QIDMDVAKPD LTAALRDVRV QYETLASRNL QDSEDWYKSK FADLSEAANR
NTDAIRQAKQ EANEYRRQVQ ALTCEVDSLK GTNESMERQM RELEESFGCE ANNFQDTISR
LEDDIRNMKD EMARHLREYQ DLLNVKMALD IEIATYRKLL EGEESRITTP MPNFSSFNLR
ESMLEARPMI DNLSKKVVIK TIETRDGHVI NESTQNHDDL E


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Kits Elisa; taq POLYMERASE

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