ID   VIM2_CARAU              Reviewed;         243 AA.
AC   P48672;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Vimentin A2;
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; L23842; AAA21756.1; -; mRNA.
DR   PIR; I50483; I50483.
DR   AlphaFoldDB; P48672; -.
DR   SMR; P48672; -.
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   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; Intermediate filament; Reference proteome.
FT   CHAIN           <1..243
FT                   /note="Vimentin A2"
FT                   /id="PRO_0000063765"
FT   DOMAIN          <1..188
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          <1..22
FT                   /note="Coil 1B"
FT   REGION          23..45
FT                   /note="Linker 12"
FT   REGION          46..184
FT                   /note="Coil 2"
FT   REGION          185..243
FT                   /note="Tail"
FT   NON_TER         1
SQ   SEQUENCE   243 AA;  28099 MW;  592B461265CE3DC2 CRC64;
     GFSLQDELDF LKKLHDEELA DVQAQIQDQQ VQVDMDMAKP DLTAALRDVR LQYENLATKN
     IQESEDWYKS KFADMTEAAN KSNEALRLAK QEANEYRRQV QALTCEVDAL KGTNESLERQ
     MREIEENFAI ESSSSQDNIA RLEEDIRNMK DEMAKHLREY QDLLNVKMAL DIEIATYRKL
     LEGEESRITT PLPNLSSFNL RDAILETKPI LENTFSKKVL IKTIETRDGE VINESTQNHD
     DLE