ID   VIMB_CARAU              Reviewed;         450 AA.
AC   P48673;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Vimentin beta;
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       brain, and spinal cord and in very high amounts in eye lens.
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}.
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DR   EMBL; L23841; AAA21757.1; -; mRNA.
DR   PIR; I50484; I50484.
DR   AlphaFoldDB; P48673; -.
DR   SMR; P48673; -.
DR   PRIDE; P48673; -.
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; 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; Intermediate filament; Reference proteome.
FT   CHAIN           1..450
FT                   /note="Vimentin beta"
FT                   /id="PRO_0000063766"
FT   DOMAIN          89..397
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..81
FT                   /note="Head"
FT   REGION          24..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..117
FT                   /note="Coil 1A"
FT   REGION          118..139
FT                   /note="Linker 1"
FT   REGION          140..231
FT                   /note="Coil 1B"
FT   REGION          232..254
FT                   /note="Linker 12"
FT   REGION          255..393
FT                   /note="Coil 2"
FT   REGION          394..450
FT                   /note="Tail"
SQ   SEQUENCE   450 AA;  52139 MW;  D5CCF229AC9011EE CRC64;
     MSSRTSTSSY KRMFGAERQA MVRSTYSSRQ YSSPGRTTSR VSYSSASSTS PSLYMSKSAR
     SATRLATETL DFGLADAINT EFKANRTNEK AEMQHVNDRF ASYIEEVRFL EQQNKILTAE
     LEQMRGKGSS RVGDLYEDEM RELRRQVDQL INEKASVEVD RDNLGENIER LRQKLQEEML
     QREDAENSLR SFRQDVDNAS LARLDLERKV ESLQEEIAFL KKLHDEELAE LQMQIQERHV
     QIDMEVAKPD LTAALRDVRQ QYETLASRNL QESEEWYKSK FADLSEAATR NSEAVRLAKH
     EANDYRRQLQ SLTCDLEALR GTNGSLERQM REMEDNFSIE ASGYQDTIVR LEDDIRNTKD
     EMARHLREYQ NLLNVKMALD IEIATYRNLL EGEEYRITTP FPNLSSLSLR ESMKEIRPAM
     DSLSKKVVIK TIETRDGHII NQSTQKDNLE