ID M3YJK3_MUSPF Unreviewed; 466 AA.
AC M3YJK3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Vimentin {ECO:0000256|ARBA:ARBA00014147};
GN Name=VIM {ECO:0000313|Ensembl:ENSMPUP00000011510.1,
GN ECO:0000313|RefSeq:XP_004757631.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000011510.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000011510.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004757631.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004757631.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Involved with LARP6 in the stabilization of type I collagen
CC mRNAs for CO1A1 and CO1A2. {ECO:0000256|ARBA:ARBA00003885}.
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:0000256|ARBA:ARBA00002825}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Nucleus matrix {ECO:0000256|ARBA:ARBA00004109}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000256|RuleBase:RU000685}.
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DR EMBL; AEYP01043328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004757631.1; XM_004757574.3.
DR STRING; 9669.ENSMPUP00000011510; -.
DR Ensembl; ENSMPUT00000011700.1; ENSMPUP00000011510.1; ENSMPUG00000011602.1.
DR GeneID; 101671433; -.
DR KEGG; mpuf:101671433; -.
DR CTD; 7431; -.
DR eggNOG; KOG0977; Eukaryota.
DR GeneTree; ENSGT00940000156146; -.
DR HOGENOM; CLU_012560_7_4_1; -.
DR OMA; GGMYATK; -.
DR OrthoDB; 4640531at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IEA:Ensembl.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:1990254; F:keratin filament binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:Ensembl.
DR GO; GO:0005212; F:structural constituent of eye lens; IEA:Ensembl.
DR GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
DR GO; GO:0060020; P:Bergmann glial cell differentiation; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0071225; P:cellular response to muramyl dipeptide; IEA:Ensembl.
DR GO; GO:0071346; P:cellular response to type II interferon; IEA:Ensembl.
DR GO; GO:0045109; P:intermediate filament organization; IEA:Ensembl.
DR GO; GO:0070307; P:lens fiber cell development; IEA:Ensembl.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0043488; P:regulation of mRNA stability; IEA:Ensembl.
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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Intermediate filament {ECO:0000256|ARBA:ARBA00022754,
KW ECO:0000256|RuleBase:RU000685};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715}.
FT DOMAIN 103..411
FT /note="IF rod"
FT /evidence="ECO:0000259|PROSITE:PS51842"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 93..255
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 295..389
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 466 AA; 53642 MW; 19A787040228D25B CRC64;
MSTRSVSSSS YRRMFGGPGT GSRPSSTRSY VTTSTRTYSL GSALRPSTSR SLYTSSPGGG
YVTRSSAVRL RSSVPGVRLL QDSVDFSLAD AINTEFKNTR TNEKVELQEL NDRFANYIDK
VRFLEQQNKI LLAELEQLKG QGKSRLGDLY EEEMRELRRQ VDQLTNDKAR VEVERDNLAE
DIMRLREKLQ EEMLQREEAE STLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHEE
EIQELQAQIQ DQHVQIDMDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE
AANRNNDALR QAKQESNEYR RQVQSLTCEV DALKGTNESL ERQMREMEDN FAVEAANYQD
TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY RKLLEGEESR IALPLPNFSS
LNLRETNLDS LPLVDTHSKR TLLIKTVETR DGQVINETSQ HHDDLE
//
