VIME_CRIGR
ID VIME_CRIGR Reviewed; 448 AA.
AC P48670;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Vimentin;
DE Flags: Fragment;
GN Name=VIM;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6688458; DOI=10.1007/bf00777481;
RA Bloemendal H., Quax W., Quax-Jeuken Y., Dodemont H., Ramaekers F.,
RA Dunia I., Benedetti L.;
RT "Organization and expression of the vimentin gene.";
RL Mol. Biol. Rep. 9:115-118(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 69-448.
RA Khodjakov A.L., Koonce M.P.;
RL Submitted (MAY-1995) 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 -!- 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-37 as
CC well as by nestin. Phosphorylated at Ser-38 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; M16718; AAA37029.1; -; mRNA.
DR EMBL; X87227; CAA60679.1; -; mRNA.
DR PIR; I48128; I48128.
DR AlphaFoldDB; P48670; -.
DR SMR; P48670; -.
DR IntAct; P48670; 1.
DR STRING; 10029.XP_007622787.1; -.
DR PRIDE; P48670; -.
DR eggNOG; KOG0977; Eukaryota.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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:0045109; P:intermediate filament organization; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Glycoprotein; Intermediate filament; Isopeptide bond; Membrane; Nucleus;
KW Phosphoprotein; S-nitrosylation; Ubl conjugation.
FT CHAIN <1..448
FT /note="Vimentin"
FT /id="PRO_0000063753"
FT DOMAIN 85..393
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION <1..77
FT /note="Head"
FT REGION 78..113
FT /note="Coil 1A"
FT REGION 114..135
FT /note="Linker 1"
FT REGION 136..227
FT /note="Coil 1B"
FT REGION 228..250
FT /note="Linker 12"
FT REGION 251..389
FT /note="Coil 2"
FT REGION 390..448
FT /note="Tail"
FT COILED 78..113
FT COILED 136..227
FT COILED 285..389
FT MOTIF 308..311
FT /note="[IL]-x-C-x-x-[DE] motif"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT SITE 333
FT /note="Stutter"
FT /evidence="ECO:0000250"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 17
FT /note="Phosphoserine; by PKC; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 22
FT /note="Phosphoserine; by CaMK2, PKA, PKC and ROCK2"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 35
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31000"
FT MOD_RES 38
FT /note="Phosphoserine; by CDK5 and CDK1"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 43
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 48
FT /note="Phosphoserine; by PKA and PKC"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 54
FT /note="Phosphoserine; by AURKB and ROCK2"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 65
FT /note="Phosphoserine; by CaMK2"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 99
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 102
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 102
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 111
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 111
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 121
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 150
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 170
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 170
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 205
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 217
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 276
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 276
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 355
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P84198"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 408
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 418
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 427
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 427
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 428
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 440
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CARBOHYD 16
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 17
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 86
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 102
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 111
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 205
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 244
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 276
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 295
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 355
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 421
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 427
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 427
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT NON_TER 1
SQ SEQUENCE 448 AA; 51849 MW; 2518FDFE759B3B87 CRC64;
PRHLEPAGSN RSYVTTSTRT YSLGALRPST SRSLYSSSPG GAYVTRSSAV RLRSSMPGVR
LLQDSVDFSL ADAINTEFKN TRTNEKVELQ ELNDRFADYI DKVRFLEQQN KILLAELEQL
KGQGKSRLGD LYEEEMRELR RQVDQLTNDK ARVEVERDNL AEDIIRLREK LQEEMLQREE
AESTLQSFRQ DVDNASLARL DLERKVESLQ EEIAFLKKLH DEEIQELQAQ IQEQHVQIDV
DVSKPDLTAA LRDVRQQYES VAAKNLQEAE EWYKSKFADL SEAANRNNDA LRQAKQESNE
YRRQVQSLTC EVDALKGTNE SLERQMREME ENFALEAANY QDTIGRLQDE IQNMKEEMAR
HLREYQDLLN VKMALDIEIA TYRKLLEGEE SRISLPLPNF SSLNLRETNL ESLPLVDTHS
KRTLLIKTVE TRDGQVINET SQHHDDLE
