ID   VIME_CHICK              Reviewed;         460 AA.
AC   P09654; Q91023;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Vimentin;
GN   Name=VIM;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3036797; DOI=10.1016/s0021-9258(18)47536-9;
RA   Zehner Z.E., Li Y., Roe B.A., Paterson B.M., Sax C.M.;
RT   "The chicken vimentin gene. Nucleotide sequence, regulatory elements, and
RT   comparison to the hamster gene.";
RL   J. Biol. Chem. 262:8112-8120(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 454-460.
RX   PubMed=6573660; DOI=10.1073/pnas.80.4.911;
RA   Zehner Z.E., Paterson B.M.;
RT   "Characterization of the chicken vimentin gene: single copy gene producing
RT   multiple mRNAs.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:911-915(1983).
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 assembled from elementary dimers. Component of a
CC       complex composed at least of ACTB, AP2M1, AP2A1, AP2A2, MEGF10 and VIM
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08670}.
CC       Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08670}. Nucleus matrix
CC       {ECO:0000250|UniProtKB:P31000}. Cell membrane
CC       {ECO:0000250|UniProtKB:P20152}.
CC   -!- DOMAIN: The central alpha-helical coiled-coil IF rod domain mediates
CC       elementary homodimerization. {ECO:0000250}.
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       {ECO:0000250|UniProtKB:P08670}.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; M15852; AAA49134.1; -; Genomic_DNA.
DR   EMBL; M15850; AAA49134.1; JOINED; Genomic_DNA.
DR   EMBL; M15851; AAA49134.1; JOINED; Genomic_DNA.
DR   EMBL; V00447; CAA23726.2; -; Genomic_DNA.
DR   PIR; A29329; A29329.
DR   AlphaFoldDB; P09654; -.
DR   SMR; P09654; -.
DR   BioGRID; 681466; 1.
DR   IntAct; P09654; 1.
DR   STRING; 9031.ENSGALP00000014107; -.
DR   PaxDb; P09654; -.
DR   PRIDE; P09654; -.
DR   VEuPathDB; HostDB:geneid_420519; -.
DR   eggNOG; KOG0977; Eukaryota.
DR   InParanoid; P09654; -.
DR   PhylomeDB; P09654; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0042995; C:cell projection; IDA:AgBase.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005882; C:intermediate filament; ISS:UniProtKB.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
KW   Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton; Intermediate filament;
KW   Membrane; Nucleus; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..460
FT                   /note="Vimentin"
FT                   /id="PRO_0000063761"
FT   DOMAIN          97..405
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2..89
FT                   /note="Head"
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..460
FT                   /note="Tail"
FT   COILED          90..125
FT   COILED          148..239
FT   COILED          297..401
FT   SITE            345
FT                   /note="Stutter"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   460 AA;  53142 MW;  C3B509E21ABA6DF3 CRC64;
     MSFTSSKNSS YRRMFGGGSR PSSGTRYITS STRYSLGSAL RPSSARYVSA SPGGVYRTKA
     TSVRLRSSMP PMRMHDAVDF TLADAINTEF KANRTNEKVE LQELNDRFAN YIDKVRFLEQ
     QNKILLAELE QLKGKGTSRL GDLYEEEMRD VRRQVDQLTN DKARVEVERD NLADDIMRLR
     EKLQEEMLQR EEAESTLQSF RQDVDNASLA GLDLERPVES LQEEIVFLKK LHDEEIRELQ
     AQLQEQHIQI DMDVSKPDLT AALRDVRQQY ESVAAKNLQE AEEWYKSKFA DLSEAANRNN
     DALRQAKQEA NEYRRQIQSL TCEVDALKGS NESLERQMRE MEENFAVEAA NYQDTIGRLQ
     DEIQNMKEEM ARHLREYQDL LNVKMALDIE IATYRKLLEG EESRINMPIP TFASLNLRET
     NIESQPIVDT HSKRTLLIKT VETRDGQVIN ETSQHHDDLE