ID   VIM1_CARAU              Reviewed;         170 AA.
AC   P48671;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Vimentin A1;
DE   Flags: Fragment;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   PubMed=8035174; DOI=10.1046/j.1471-4159.1994.63020470.x;
RA   Glasgow E., Druger R.K., Fuchs C., Levine E.M., Giordano S., Schechter N.;
RT   "Cloning of multiple forms of goldfish vimentin: differential expression in
RT   CNS.";
RL   J. Neurochem. 63:470-481(1994).
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. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in low amounts in retina, optic nerve,
CC       and brain and in higher amounts in spinal cord.
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L23840; AAA21755.1; -; mRNA.
DR   PIR; I50482; I50482.
DR   AlphaFoldDB; P48671; -.
DR   SMR; P48671; -.
DR   PRIDE; P48671; -.
DR   Proteomes; UP000515129; Genome assembly.
DR   GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR027699; Vimentin.
DR   PANTHER; PTHR45652:SF5; PTHR45652:SF5; 1.
DR   Pfam; PF00038; 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; Intermediate filament; Reference proteome.
FT   CHAIN           <1..170
FT                   /note="Vimentin A1"
FT                   /id="PRO_0000063764"
FT   DOMAIN          <1..115
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          <1..111
FT                   /note="Coil 2"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          112..170
FT                   /note="Tail"
FT   NON_TER         1
SQ   SEQUENCE   170 AA;  19657 MW;  E2F7EA6BF932C57C CRC64;
     DLTEAANKSN EALRLAKQES NDYRRQVQAL TCEVDALKGT NESLERQMRE MEENFAMESS
     SSQDKIVQLE EDTQNMKDEM AKHLHEYQDL LNVKMALDIE IATYRKLLEG EESRISTPLP
     NFSSFNLRET MLELKPNIES TFTKKVLIKT IETRDGQVLN ESTQNHDDLE