VIME_BOVIN
ID VIME_BOVIN Reviewed; 466 AA.
AC P48616; Q17QM7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Vimentin;
GN Name=VIM;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8144034; DOI=10.1016/0378-1119(94)90554-1;
RA Hess J.F., Casselman J.T., FitzGerald P.G.;
RT "Nucleotide sequence of the bovine vimentin-encoding cDNA.";
RL Gene 140:257-259(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Interacts with BCAS3 (By
CC similarity). Interacts with LGSN (By similarity). Interacts with SYNM
CC (By similarity). Interacts (via rod region) with PLEC (via CH 1 domain)
CC (By similarity). 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 Interacts with TOR1AIP1 (By similarity). Interacts with TOR1AIP1 (By
CC similarity). Interacts with DIAPH1 (By similarity). Interacts with
CC EPPK1; interaction is dependent of higher-order structure of
CC intermediate filament (By similarity). Interacts with the non-receptor
CC tyrosine kinase SRMS; the interaction leads to phosphorylation of VIM
CC (By similarity). Interacts with NOD2 (By similarity). Interacts (via
CC head region) with CORO1C (By similarity). Interacts with HDGF (By
CC similarity). Interacts with PRKCE (via phorbol-ester/DAG-type 2 domain)
CC (By similarity). Interacts with BFSP2 (By similarity). Interacts with
CC PPL (By similarity). {ECO:0000250|UniProtKB:P08670,
CC ECO:0000250|UniProtKB:P20152, ECO:0000250|UniProtKB:P31000}.
CC -!- INTERACTION:
CC P48616; P18341: TGFB1; NbExp=2; IntAct=EBI-1221453, EBI-8537762;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08670}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08670}. Nucleus matrix
CC {ECO:0000250|UniProtKB:P31000}. Cell membrane
CC {ECO:0000250|UniProtKB:P20152}.
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: One of the most prominent phosphoproteins in various cells of
CC mesenchymal origin. Phosphorylation is enhanced during cell division,
CC at which time vimentin filaments are significantly reorganized.
CC Phosphorylation by PKN1 inhibits the formation of filaments. Filament
CC disassembly during mitosis is promoted by phosphorylation at Ser-55 as
CC well as by nestin. Phosphorylated at Ser-56 by CDK5 during neutrophil
CC secretion in the cytoplasm. Phosphorylated by STK33. Phosphorylated on
CC tyrosine residues by SRMS. {ECO:0000250|UniProtKB:P08670,
CC 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 -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; L13263; AAA53661.1; -; mRNA.
DR EMBL; BC118269; AAI18270.1; -; mRNA.
DR RefSeq; NP_776394.2; NM_173969.3.
DR AlphaFoldDB; P48616; -.
DR SMR; P48616; -.
DR IntAct; P48616; 3.
DR MINT; P48616; -.
DR STRING; 9913.ENSBTAP00000024572; -.
DR iPTMnet; P48616; -.
DR PaxDb; P48616; -.
DR PeptideAtlas; P48616; -.
DR PRIDE; P48616; -.
DR Ensembl; ENSBTAT00000024572; ENSBTAP00000024572; ENSBTAG00000018463.
DR GeneID; 280955; -.
DR KEGG; bta:280955; -.
DR CTD; 7431; -.
DR VEuPathDB; HostDB:ENSBTAG00000018463; -.
DR VGNC; VGNC:36796; VIM.
DR eggNOG; KOG0977; Eukaryota.
DR GeneTree; ENSGT00940000156146; -.
DR HOGENOM; CLU_012560_7_4_1; -.
DR InParanoid; P48616; -.
DR OMA; PPMRLHD; -.
DR OrthoDB; 655109at2759; -.
DR TreeFam; TF330122; -.
DR Reactome; R-BTA-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-BTA-390522; Striated Muscle Contraction.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000018463; Expressed in bone marrow and 106 other tissues.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005882; C:intermediate filament; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0005777; C:peroxisome; IEA:Ensembl.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005844; C:polysome; IEA:Ensembl.
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; ISS:UniProtKB.
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:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
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:0001701; P:in utero embryonic development; TAS:AgBase.
DR GO; GO:0045109; P:intermediate filament organization; ISS:UniProtKB.
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:0032930; P:positive regulation of superoxide anion generation; IDA:ARUK-UCL.
DR GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
DR GO; GO:0043488; P:regulation of mRNA stability; IEA:Ensembl.
DR GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
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 Glycoprotein; Intermediate filament; Isopeptide bond; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; 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_0000063751"
FT DOMAIN 103..411
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..31
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:0000250|UniProtKB:P08670"
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:0000250|UniProtKB:P08670"
FT MOD_RES 10
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 20
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 25
FT /note="Phosphoserine; by PKA and PKC"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 26
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 34
FT /note="Phosphoserine; by PKC; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 39
FT /note="Phosphoserine; by CaMK2, PKA, PKC and ROCK2"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 42
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 53
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31000"
FT MOD_RES 56
FT /note="Phosphoserine; by CDK5 and CDK1"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 61
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 66
FT /note="Phosphoserine; by PKA and PKC"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 72
FT /note="Phosphoserine; by AURKB and ROCK2"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 83
FT /note="Phosphoserine; by CaMK2"
FT /evidence="ECO:0000250|UniProtKB:P20152"
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:0000250|UniProtKB:P08670"
FT MOD_RES 120
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 129
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 129
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 139
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 168
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 188
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 188
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 223
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 235
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 294
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 294
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 373
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
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:0000250|UniProtKB:P08670"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 426
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
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:0000250|UniProtKB:P20152"
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:0000250|UniProtKB:P08670"
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 148
FT /note="D -> Q (in Ref. 1; AAA53661)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="V -> A (in Ref. 1; AAA53661)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="D -> H (in Ref. 1; AAA53661)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="E -> A (in Ref. 1; AAA53661)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 53728 MW; 8722F645FED23BDC CRC64;
MSTRSVSSSS YRRMFGGPGT ASRPSSTRSY VTTSTRTYSL GSALRPTTSR TLYTSSPGGV
YATRSSAVRL RSGVPGVRLL QDSVDFSLAD AINTEFKNTR TNEKVELQEL NDRFANYIDK
VRFLEQQNKI LLAELEQLKG QGKSRLGDLY EEEMRELRRQ VDQLTNDKAR VEVERDNLAE
DIMRLREKLQ EEMLQREEAE STLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHDE
EIQELQAQIQ EQHVQIDMDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE
AANRNNDALR QAKQESNEYR RQVQTLTCEV DALKGTNESL ERQMREMEEN FSVEAANYQD
TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY RKLLEGEESR ISLPLPNFSS
LNLRETNLDS LPLVDTHSKR TLLIKTVETR DGQVINETSQ HHDDLE
