ID   VIM1_XENLA              Reviewed;         458 AA.
AC   P24789; Q5U486; Q68EZ6;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Vimentin-1/2;
GN   Name=vim1;
GN   and
GN   Name=vim2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   PubMed=2806127; DOI=10.1242/dev.105.2.279;
RA   Herrmann H., Fouquet B., Franke W.W.;
RT   "Expression of intermediate filament proteins during development of Xenopus
RT   laevis. I. cDNA clones encoding different forms of vimentin.";
RL   Development 105:279-298(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (VIM1 AND VIM2).
RC   TISSUE=Kidney, and Spleen;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
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.
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   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; X16843; CAA34741.1; -; mRNA.
DR   EMBL; BC080051; AAH80051.1; -; mRNA.
DR   EMBL; BC085223; AAH85223.1; -; mRNA.
DR   PIR; A43549; A43549.
DR   RefSeq; NP_001080908.1; NM_001087439.1.
DR   AlphaFoldDB; P24789; -.
DR   SMR; P24789; -.
DR   BioGRID; 98845; 1.
DR   IntAct; P24789; 1.
DR   PRIDE; P24789; -.
DR   DNASU; 386601; -.
DR   GeneID; 386601; -.
DR   KEGG; xla:386601; -.
DR   CTD; 386601; -.
DR   Xenbase; XB-GENE-866225; vim.L.
DR   OMA; PPMRLHD; -.
DR   OrthoDB; 655109at2759; -.
DR   Proteomes; UP000186698; Chromosome 6L.
DR   Bgee; 386601; Expressed in lung and 19 other tissues.
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..458
FT                   /note="Vimentin-1/2"
FT                   /id="PRO_0000063762"
FT   DOMAIN          96..404
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..88
FT                   /note="Head"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          89..124
FT                   /note="Coil 1A"
FT   REGION          125..146
FT                   /note="Linker 1"
FT   REGION          147..238
FT                   /note="Coil 1B"
FT   REGION          239..261
FT                   /note="Linker 12"
FT   REGION          262..400
FT                   /note="Coil 2"
FT   REGION          401..458
FT                   /note="Tail"
FT   SITE            344
FT                   /note="Stutter"
FT                   /evidence="ECO:0000255"
FT   VARIANT         43
FT                   /note="S -> SS (in vim2)"
SQ   SEQUENCE   458 AA;  52845 MW;  29A46C76F256AC0C CRC64;
     MATTKSSYRR IFGGNPRSSS SGNRYATSST RYTLGSAMRP STSSRMVYST SSSPAVFKSS
     SVRLRSSLPP ARMADSVDFA LADAVNLEFK ANRTNEKAEM IELNDRFANF IDKVRFLEQQ
     NKILVAELEQ LKGKGTSRIG DLYEEEMREL RRQLDQATND KARVEVDRDN LADDLQRLRE
     KLQDEMIQKE EAEGNLQSFR QDVDNASLAR IDLERKVESL QEEIAFLKKL HDEEIRELQL
     QIQESHIQVD MDVSKPDLTA ALRDVRQQYE NVAAKNLSDA EEWYKSKFAD LSEAANRNND
     ALRQAKQETS DFRRQIQTLT CEIDAMKGSN ESYERQMREM EENFAIEAAN YQDTIQRLQE
     EIQNMKEEMA RHLREYQDLL NVKMALDIEI ATYRKLLEGE ESRISLPVHS FSTMSLRETN
     LDSHPAETHS KRTVLIKTVE TRDGQVVNES SQHHDDFE