ID   VIM4_XENLA              Reviewed;         463 AA.
AC   P24790;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Vimentin-4;
GN   Name=vim4;
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].
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 [MRNA] OF 331-404.
RX   PubMed=3224553; DOI=10.1242/dev.103.2.269;
RA   Sharpe C.R.;
RT   "Developmental expression of a neurofilament-M and two vimentin-like genes
RT   in Xenopus laevis.";
RL   Development 103:269-277(1988).
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; X16844; CAA34742.1; -; mRNA.
DR   PIR; B43549; B43549.
DR   AlphaFoldDB; P24790; -.
DR   SMR; P24790; -.
DR   MaxQB; P24790; -.
DR   PRIDE; P24790; -.
DR   OMA; EGHNADY; -.
DR   Proteomes; UP000186698; 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..463
FT                   /note="Vimentin-4"
FT                   /id="PRO_0000063763"
FT   DOMAIN          97..405
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..89
FT                   /note="Head"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          90..125
FT                   /note="Coil 1A"
FT   REGION          126..147
FT                   /note="Linker 1"
FT   REGION          148..239
FT                   /note="Coil 1B"
FT   REGION          240..262
FT                   /note="Linker 12"
FT   REGION          263..401
FT                   /note="Coil 2"
FT   REGION          402..463
FT                   /note="Tail"
FT   SITE            345
FT                   /note="Stutter"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   463 AA;  53497 MW;  15A1CD9547C99AFA CRC64;
     MATTKSSYRR IFGGNPRSSS SGSRYVTSSS RYSLGSSMRP GTSSSRMVYS TSASPAVFKS
     SSVRLRSSLP PARMADSVDF TLADAVNLEF KANRTNEKAE MIELNDRFAN FIDKVRFLEQ
     QNKILVAELE QLKGKGTSRI GDLYEEEMRE IRRQLDQAIN EKARVEVDRD NLGDDLQRLR
     EKLQDEMIQR EEAEGNLQSF RQDVDNASLA RIDLERKVES LQEEIVFLKK LHDEEIRELQ
     LQIQESHIQV DMDVSKPDLT AALRDVRQQY ENVASKNLAD AEDWYKSKFA DLSEAANRNN
     EALRQAKQDT NDYRRQIQTL TCEIDAMKGS NESYERQMRE MEENFALEAA NYQDTIQRLQ
     EEIQNMKEEM SRHLREYQDL LNVKMALDIE IATYRKLLEG EESRITIPVH SFSTMSLRET
     NLDSHPVDTH SKRTLLIKTV ETRDGQVINE SSQHHDDLDL DLE