ID   VIME_CYPCA              Reviewed;         455 AA.
AC   Q92155;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Vimentin;
GN   Name=vim;
OS   Cyprinus carpio (Common carp).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Cyprinus.
OX   NCBI_TaxID=7962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Optic nerve;
RX   PubMed=1661817; DOI=10.1016/0169-328x(91)90121-d;
RA   Cohen I., Shani Y., Blaugrund E., Schwartz M.;
RT   "Isolation and sequence analysis of two intermediate filament cDNA clones
RT   from fish optic nerve.";
RL   Brain Res. Mol. Brain Res. 11:181-185(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   -!- 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; S76850; AAB20706.2; -; mRNA.
DR   PIR; A43950; A43950.
DR   AlphaFoldDB; Q92155; -.
DR   SMR; Q92155; -.
DR   PRIDE; Q92155; -.
DR   Proteomes; UP000694384; 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   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;
KW   Reference proteome.
FT   CHAIN           1..455
FT                   /note="Vimentin"
FT                   /id="PRO_0000063767"
FT   DOMAIN          94..402
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..87
FT                   /note="Head"
FT   REGION          25..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..122
FT                   /note="Coil 1A"
FT   REGION          123..144
FT                   /note="Linker 1"
FT   REGION          145..236
FT                   /note="Coil 1B"
FT   REGION          237..259
FT                   /note="Linker 12"
FT   REGION          260..398
FT                   /note="Coil 2"
FT   REGION          399..455
FT                   /note="Tail"
FT   COILED          87..122
FT   COILED          145..236
FT   COILED          294..398
FT   SITE            342
FT                   /note="Stutter"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   455 AA;  52492 MW;  53CEF648043D3E22 CRC64;
     MASRTNTSSY KRMFGGERPA MVRSTYSSRQ YSSPVRTTSR VSYSSASSAS PSIYMSKGAR
     VRSSGPLPRL ATETLDFGLA DAINTEFKTN RTNEKAEMQH LNDRFASYID KVRFLEQQNK
     ILIAELEQMR GKGSSRVGDL YQDEMRELRR QVDQLTNEKA TVEVDRDNLG EDIERLKEKL
     QEEMLQREDA ENTLRGFRQD VDNASLARLH LETKVESLQE EIAFLKKLHD EELAELQIQI
     QEQHVQIDME VAKPDLTAAL KDVRQQYETL ASRNLQESEE WYKSKFADLS EAAARNNEAI
     RLAKQEANDY RRQLQSLTCD LEALKGTNES LERQLREMED NFSMEASGYQ DTIARLEDDI
     RNMKDEMARH LREYQDLLNV KMALDIEIAT YRKLLEGEES RITTPFPNLS SLTLRETMKE
     TRPAMDSLSK KVVIKTIETR DGHIINESSQ NDDLE