VIME_MESAU
ID VIME_MESAU Reviewed; 465 AA.
AC P02544;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Vimentin;
GN Name=VIM;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lens;
RX PubMed=6194898; DOI=10.1016/0092-8674(83)90224-6;
RA Quax W.J., Egberts W.V., Hendriks W., Quax-Jeuken Y.E.F.M., Bloemendal H.;
RT "The structure of the vimentin gene.";
RL Cell 35:215-223(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lens;
RX PubMed=6304716; DOI=10.1073/pnas.80.12.3548;
RA Quax-Jeuken Y.E.F.M., Quax W.J., Bloemendal H.;
RT "Primary and secondary structure of hamster vimentin predicted from the
RT nucleotide sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:3548-3552(1983).
RN [3]
RP PHOSPHORYLATION AT SER-55.
RX PubMed=2019567; DOI=10.1016/s0021-9258(20)89448-4;
RA Chou Y.-H., Ngai K.-L., Goldman R.;
RT "The regulation of intermediate filament reorganization in mitosis. p34cdc2
RT phosphorylates vimentin at a unique N-terminal site.";
RL J. Biol. Chem. 266:7325-7328(1991).
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: Phosphorylation by PKN1 inhibits the formation of filaments.
CC Filament disassembly during mitosis is promoted by phosphorylation at
CC Ser-54 as well as by nestin. One of the most prominent phosphoproteins
CC in various cells of mesenchymal origin. Phosphorylation is enhanced
CC during cell division, at which time vimentin filaments are
CC significantly reorganized. Phosphorylated at Ser-55 by CDK5 during
CC neutrophil secretion in the cytoplasm. Phosphorylated by STK33.
CC Phosphorylated on tyrosine residues by SRMS.
CC {ECO:0000250|UniProtKB:P08670, 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; K00927; AAA37104.1; -; Genomic_DNA.
DR EMBL; K00921; AAA37104.1; JOINED; Genomic_DNA.
DR EMBL; K00922; AAA37104.1; JOINED; Genomic_DNA.
DR EMBL; K00923; AAA37104.1; JOINED; Genomic_DNA.
DR EMBL; K00924; AAA37104.1; JOINED; Genomic_DNA.
DR EMBL; K00925; AAA37104.1; JOINED; Genomic_DNA.
DR EMBL; K00926; AAA37104.1; JOINED; Genomic_DNA.
DR PIR; A90842; VEHY.
DR AlphaFoldDB; P02544; -.
DR SMR; P02544; -.
DR STRING; 10036.XP_005081318.1; -.
DR iPTMnet; P02544; -.
DR PRIDE; P02544; -.
DR eggNOG; KOG0977; Eukaryota.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005882; C:intermediate filament; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; 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 GO; GO:0045107; P:intermediate filament polymerization; IDA:CAFA.
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..465
FT /note="Vimentin"
FT /id="PRO_0000063755"
FT DOMAIN 102..410
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..94
FT /note="Head"
FT REGION 95..130
FT /note="Coil 1A"
FT REGION 131..152
FT /note="Linker 1"
FT REGION 153..244
FT /note="Coil 1B"
FT REGION 245..267
FT /note="Linker 12"
FT REGION 268..406
FT /note="Coil 2"
FT REGION 407..465
FT /note="Tail"
FT COILED 95..130
FT COILED 153..244
FT COILED 302..406
FT MOTIF 325..328
FT /note="[IL]-x-C-x-x-[DE] motif"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT SITE 350
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 21
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P20152"
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 46
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 50
FT /note="Phosphoserine; by PKA and PKC"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 52
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31000"
FT MOD_RES 55
FT /note="Phosphoserine; by CDK5 and CDK1"
FT /evidence="ECO:0000269|PubMed:2019567"
FT MOD_RES 60
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 71
FT /note="Phosphoserine; by AURKB and ROCK2"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 116
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 119
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 119
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 128
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 128
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 138
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 167
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 187
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 187
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 222
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 234
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 293
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 293
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 372
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P84198"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 425
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 435
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 444
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 444
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 445
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 457
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 458
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 103
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 128
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 222
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 261
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 293
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 312
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 372
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 438
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT CONFLICT 43
FT /note="L -> A (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="Y -> D (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="R -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 53730 MW; 81E6B65451E3EC54 CRC64;
MSTRSVSSSS YRRMFGGPGT SNRQSSNRSY VTTSTRTYSL GSLRPSTSRS LYSSSPGGAY
VTRSSAVRLR SSMPGVRLLQ DSVDFSLADA INTEFKNTRT NEKVELQELN DRFANYIDKV
RFLEQQNKIL LAELEQLKGQ GKSRLGDLYE EEMRELRRQV DQLTNDKARV EVERDNLAED
IMRLREKLQE EMLQREEAES TLQSFRQDVD NASLARLDLE RKVESLQEEI AFLKKLHDEE
IQELQAQIQE QHVQIDVDVS KPDLTAALRD VRQQYESVAA KNLQEAEEWY KSKFADLSEA
ANRNNDALRQ AKQESNEYRR QVQSLTCEVD ALKGTNESLE RQMREMEENF ALEAANYQDT
IGRLQDEIQN MKEEMARHLR EYQDLLNVKM ALDIEIATYR KLLEGEESRI SLPLPNFSSL
NLRETNLESL PLVDTHSKRT LLIKTVETRD GQVINETSQH HDDLE
