ID A0A3L8SYV9_CHLGU Unreviewed; 459 AA.
AC A0A3L8SYV9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=IF rod domain-containing protein {ECO:0000259|PROSITE:PS51842};
GN ORFNames=DV515_00001471 {ECO:0000313|EMBL:RLW11187.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW11187.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW11187.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW11187.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW11187.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
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. {ECO:0000256|ARBA:ARBA00002825}.
CC -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000256|RuleBase:RU000685}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLW11187.1}.
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DR EMBL; QUSF01000003; RLW11187.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8SYV9; -.
DR STRING; 44316.ENSEGOP00005002639; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.5.500; Single helix bin; 1.
DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR006821; Intermed_filament_DNA-bd.
DR PANTHER; PTHR45652; GLIAL FIBRILLARY ACIDIC PROTEIN; 1.
DR PANTHER; PTHR45652:SF5; VIMENTIN; 1.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF04732; Filament_head; 1.
DR SMART; SM01391; Filament; 1.
DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Intermediate filament {ECO:0000256|ARBA:ARBA00022754,
KW ECO:0000256|RuleBase:RU000685};
KW Reference proteome {ECO:0000313|Proteomes:UP000276834}.
FT DOMAIN 96..404
FT /note="IF rod"
FT /evidence="ECO:0000259|PROSITE:PS51842"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 86..248
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 288..382
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 459 AA; 53151 MW; FC6AB29A166BEA46 CRC64;
MSISTKNSSY RRMFGGGSRP STGTRYITSS SRYSLGSALR PSSARYVSAS PGGVYATKTT
SVRLRSSMPP MRLHDSVDFS LADAINTEFK ANRTNEKVEL QELNDRFANY IDKVRFLEQQ
NKILLAELEQ LKGKGTSRLG DLYEEEMREL RRQVDQLTND KARVEVERDN LADDIMRLRE
KLQEEMLQRE EAENTLQSFR QDVDNASLAR LDLERKVESL QEEIVFLKKL HDEEIRELQA
QLQEQHIQID MDVSKPDLTA ALRDVRQQYE SVAAKNLQEA EEWYKSKFAD LSEAANRNND
ALRQAKQEAN EYRRQIQSLT CEVDALKGSN ESLERQMREM EENFALEAAN YQDTIGRLQD
EIQNMKEEMA RHLREYQDLL NVKMALDIEI ATYRKLLEGE ESRINMPIPT FAALNLRETN
IESQPMVDTH SKRTLLIKTV ETRDGQVINE TSQHHDDLE
//
