VIME_CHLAE
ID VIME_CHLAE Reviewed; 466 AA.
AC P84198; Q3HWE4;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Vimentin;
GN Name=VIM;
OS Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=9534;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16378972; DOI=10.1128/jvi.80.2.689-696.2006;
RA Kim J.-K., Fahad A.M., Shanmukhappa K., Kapil S.;
RT "Defining the cellular target(s) of porcine reproductive and respiratory
RT syndrome virus blocking monoclonal antibody 7G10.";
RL J. Virol. 80:689-696(2006).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 144-168 AND 335-359, AND PHOSPHORYLATION.
RX PubMed=10887173; DOI=10.1074/jbc.m001207200;
RA Tzivion G., Luo Z.-J., Avruch J.;
RT "Calyculin A-induced vimentin phosphorylation sequesters 14-3-3 and
RT displaces other 14-3-3 partners in vivo.";
RL J. Biol. Chem. 275:29772-29778(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-412, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17494752; DOI=10.1073/pnas.0701103104;
RA Wang Y., Ding S.-J., Wang W., Jacobs J.M., Qian W.-J., Moore R.J., Yang F.,
RA Camp D.G. II, Smith R.D., Klemke R.L.;
RT "Profiling signaling polarity in chemotactic cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8328-8333(2007).
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-55 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-56 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; DQ190949; ABA39528.1; -; mRNA.
DR AlphaFoldDB; P84198; -.
DR SMR; P84198; -.
DR IntAct; P84198; 2.
DR MINT; P84198; -.
DR iPTMnet; P84198; -.
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 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 Direct protein sequencing; Glycoprotein; Intermediate filament;
KW Isopeptide bond; Membrane; Nucleus; Phosphoprotein; S-nitrosylation;
KW Ubl conjugation.
FT CHAIN 1..466
FT /note="Vimentin"
FT /id="PRO_0000063752"
FT DOMAIN 103..411
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..95
FT /note="Head"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 7
FT /note="Phosphoserine; 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"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 10
FT /note="Phosphoserine"
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"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 26
FT /note="Phosphoserine"
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"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17494752"
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"
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 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08670"
FT MOD_RES 83
FT /note="Phosphoserine"
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 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20152"
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:0000269|PubMed:17494752"
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"
SQ SEQUENCE 466 AA; 53709 MW; 2ADE5F232E11EC9F CRC64;
MTTRSVSSSS YRRMFGGPGT ASRPSSSRSY VTTSTRTYSL GSALRPSTSR SLYASSPGGV
YATRSSAVRL RSSVPGVRLL QDSVDFSLAD AINTEFKNTR TNEKVELQEL NDRFANYIDK
VRFLEQQNKI LLAELEQLKG QGKSRLGDLY EEEMRELRRQ VDQLTNDKAR VEVERDNLTE
DIMRLREKLQ EEMLQREEAE NTLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHEE
EIQELQAQIQ EQHVQIDVDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE
AANRNNDALR QAKQESNEYR RQVQSLTCEV DALKGTNESL ERQMREMEEN FAVEAANYQD
TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY RKLLEGEESR ISLPLPNFSS
LNLRETNLDS LPLVDTHSKR TLLIKTVETR DGQVINETSQ HHDDLE
