ID   VIME_ONCMY              Reviewed;         461 AA.
AC   P48674;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Vimentin;
GN   Name=vim;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Spleen;
RX   PubMed=8907703; DOI=10.1242/jcs.109.3.569;
RA   Herrmann H., Muenick M.D., Brettel M., Fouquet B., Markl J.;
RT   "Vimentin in a cold-water fish, the rainbow trout: highly conserved primary
RT   structure but unique assembly properties.";
RL   J. Cell Sci. 109:569-578(1996).
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   -!- SUBUNIT: Homomer assembled from elementary dimers. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08670}.
CC       Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08670}. Nucleus matrix
CC       {ECO:0000250|UniProtKB:P31000}.
CC   -!- DOMAIN: The central alpha-helical coiled-coil IF rod domain mediates
CC       elementary homodimerization. {ECO:0000250}.
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       {ECO:0000250|UniProtKB:P08670}.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; Z50738; CAA90601.1; -; mRNA.
DR   RefSeq; NP_001118201.1; NM_001124729.1.
DR   AlphaFoldDB; P48674; -.
DR   SMR; P48674; -.
DR   PRIDE; P48674; -.
DR   GeneID; 100136784; -.
DR   KEGG; omy:100136784; -.
DR   CTD; 7431; -.
DR   OrthoDB; 655109at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR   GO; GO:0005856; C:cytoskeleton; IDA:AgBase.
DR   GO; GO:0005882; C:intermediate filament; ISS:UniProtKB.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
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   Coiled coil; Cytoplasm; Cytoskeleton; Intermediate filament; Nucleus.
FT   CHAIN           1..461
FT                   /note="Vimentin"
FT                   /id="PRO_0000063768"
FT   DOMAIN          99..407
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..91
FT                   /note="Head"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..127
FT                   /note="Coil 1A"
FT   REGION          128..149
FT                   /note="Linker 1"
FT   REGION          150..241
FT                   /note="Coil 1B"
FT   REGION          242..264
FT                   /note="Linker 12"
FT   REGION          265..403
FT                   /note="Coil 2"
FT   REGION          404..461
FT                   /note="Tail"
FT   COILED          92..127
FT   COILED          150..241
FT   COILED          299..403
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            347
FT                   /note="Stutter"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   461 AA;  53325 MW;  D49B1DE4F79D2E30 CRC64;
     MNRTTSRQTT SSSSYKRMFG GEGRPSVGMA RSTLSSRQYS SPVRSSRMSY SVSAPPSIYA
     SKNVRLRSSA PMPRLSSDTV DFALSDAINS EFKANRTNEK AEMQHLNDRF ASYIDKVRFL
     EQQNKILLAE LEQLKGKGAS RIGDLYEDEM RDLRRQVDQL TNEKAHVEVD RDNMGEDIER
     LREKLQDEMI QKEEAEHNLQ SFRQDVDNAS LARLDLERKV ESLQEEIIFL RKLHDEEVAE
     LQAQIQDQHV QIDMDVAKPD LTAALRDVRV QYETLASRNL QDSEDWYKSK FADLSEAANR
     NTDAIRQAKQ EANEYRRQVQ ALTCEVDSLK GTNESMERQM RELEESFGCE ANNFQDTISR
     LEDDIRNMKD EMARHLREYQ DLLNVKMALD IEIATYRKLL EGEESRITTP MPNFSSFNLR
     ESMLEARPMI DNLSKKVVIK TIETRDGHVI NESTQNHDDL E